TW201827453A - Constructs targeting hiv peptide/mhc complexes and uses thereof - Google Patents

Abstract

The present application provides constructs comprising an antibody moiety that specifically bind to a complex comprising a human immunodeficiency virus 1 (HIV-1) reverse transcriptase (RT) peptide and an MHC class I protein. Also provided are methods of making and using these constructs.

Description

Construct targeting HIV peptide / MHC complex and its use

The present invention relates to a construct comprising an antibody portion that specifically binds to a complex comprising a human immunodeficiency virus 1 (HIV-1) reverse transcriptase (RT) peptide and an MHC class I protein, including its manufacturing method and use, Such as for treating and / or diagnosing diseases.

Human immunodeficiency virus (HIV) is a lentivirus that causes HIV infection and acquired immunodeficiency syndrome (AIDS). Lentivirus is a genus of viruses of the Retroviridae family. Lentiviruses are transmitted as single-stranded, positive-enveloped RNA viruses. HIV has been divided into two types: HIV-1 and HIV-2. HIV-1 is more toxic and more infectious than HIV-2. HIV-1 is the cause of most HIV infections worldwide. HIV-2's ability to spread is relatively poor. It is mainly found in West Africa and some cases have been found in India and Europe. HIV has several main genes encoding structural proteins and several auxiliary genes. The HIV genome contains three major genes, gag , pol, and env , which encode major structural proteins, and essential viral enzymes. Pol encodes reverse transcriptase (RT), RNase H, integrase and HIV protease. Reverse transcriptase is required to transcribe DNA from RNA templates. Integrases are necessary to integrate double-stranded viral DNA into the host genome. HIV protease is needed to break down the precursor Gag polymerized protein to produce structural proteins. Reverse transcriptase (RT) is a vital enzyme in the HIV replication cycle. RT is used by retroviruses to transcribe their single-stranded RNA genome to single-stranded DNA and to subsequently construct complementary strands of DNA to provide a DNA double helix that can be integrated into the host cell chromosome. Functional HIV1-RT is a heterodimer containing 66 kDa (p66) and 51 kDa (p51) subunits. p66 contains two domains, the N-terminal polymerase domain (440 residues) and the C-terminal RNase H domain (120 residues). p51 is processed by protein cleavage of p66 and corresponds to the polymerase domain of p66 subunits. For chronically infected patients who have not started antiretroviral therapy (ART) before, up to 98% or greater than 98% of the potential viruses can carry escape mutations, which brings to the cytotoxic T lymphocytes against a common epitope (CTL) resistance, thereby causing a clear barrier when clearing potential virus nests in these patients to cure HIV infection (Deng, K. et al. (2015) Nature 517 (7534): 381-385). For a review of various T cell gene modification and gene editing strategies that are attempted to inhibit HIV-1 replication, see Leibman, RS, & Riley, JL (2015) Molecular Therapy 23 (7): 1149-1159 and June, CH, & .... Levine, BL ( 2015) Phil Trans R Soc B 370 (1680): 20140374. Recent developments in the use of phage display to generate mAbs have made it possible to select agents with refined specificity for defined epitopes from large antibody lineages. In the case of having HLA-A01 and HLA-A02 antigen specific for solid tumor of a plurality of such mAb has been successfully selected from a phage display library (Noy et al., Expert Rev Anticancer Ther 5 (3 ):.. 523-536 , 2005; Chames et al., Proc Natl Acad Sci USA 97: 7969-7974, 2000; Held et al., Eur J Immunol 34:.. ..... 2919-2929, 2004; Lev et al., Cancer Re s. 62: 3184-3194, 2002; Klechevsky et al., Cancer Res . 68 (15): 6360-6367, 2008). Recently, it has been shown that human mAbs specific for the human WT1 / HLA-A02 complex (fully described T-cell epitopes) via Fc-mediated effector cell function inhibit multiple cancer cell lines in cell analysis and in vivo models And primary cancer cells (Dao et al., Sci . Transl . Med . 5: 176ra33, 2013; Veomett et al., Clin . Cancer Res . Doi: 10.1158 / 1078-0432, 2014). The disclosures of all publications, patents, patent applications and published patent applications mentioned herein are hereby incorporated by reference in their entirety.

In one aspect, the application provides binding to a complex comprising HIV-1 RT peptide and MHC class I protein (referred to herein as "HIV-1 RT / MHC class I complex" or "RTMC") A structure (such as a separated structure). In some embodiments, these constructs ("anti-RTMC constructs") comprise antibody portions that specifically bind to a complex comprising HIV-1 RT peptide and MHC class I protein (referred to herein as "anti-RTMC" Antibody section "). Therefore, in some embodiments, an anti-RTMC construct (such as an isolated anti-RTMC construct) is provided that includes an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein. In some embodiments, the HIV-1 RT / MHC class I complex is present on the cell surface. In some embodiments, the HIV-1 RT / MHC class I complex is present on the surface of immune cells, such as T cells. In some embodiments, the anti-RTMC construct comprises an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the MHC class I protein is HLA-A. In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is the HLA-A * 02: 01 subtype of the HLA-A02 dual gene. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I An antibody portion of a complex of proteins, wherein the antibody portion cross-reacts with a complex comprising an HIV-1 RT peptide and a second MHC class I protein (having an HLA dual gene different from the MHC class I protein). In some embodiments, the antibody portion cross-reacts with a complex comprising a variant of HIV-1 RT peptide containing an amino acid substitution (such as a conservative amino acid substitution) and MHC class I protein. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of the protein complex, wherein the HIV-1 RT peptide is about 8 to about 12 (such as about any of 8, 9, 10, 11, or 12) amino acids in length. In some embodiments, the HIV-1 RT peptide is derived from the region corresponding to amino acids 181 to 189 of SEQ ID NO: 1. In some embodiments, the HIV-1 RT peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 5-18. In some embodiments, the HIV-1 RT peptide has the amino acid sequence YQYVDDLYV (SEQ ID NO: 6). In some embodiments, the isolated anti-RTMC construct cross-reacts with a complex comprising a variant of an HIV-1 RT peptide having an amino acid sequence of any of the following and an MHC class I protein: YQYMDDLYV (SEQ ID NO: 5), YQYIDDLYV (SEQ ID NO: 7), CQYMDDLYV (SEQ ID NO: 8) or CQYVDDLYV (SEQ ID NO: 9). In some embodiments, the HIV-1 RT peptide has the amino acid sequence YQYMDDLYV (SEQ ID NO: 5). In some embodiments, the isolated anti-RTMC construct cross-reacts with a complex comprising a variant of HIV-1 RT peptide having an amino acid sequence of any of the following and MHC class I protein: YQYVDDLYV (SEQ ID NO: 6), YQYIDDLYV (SEQ ID NO: 7), CQYMDDLYV (SEQ ID NO: 8) or CQYVDDLYV (SEQ ID NO: 9). In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of the protein complex, wherein the antibody portion is a full-length antibody, Fab, Fab ', (Fab') 2, Fv or single chain Fv (scFv). In some embodiments, the antibody portion is a fully human antibody portion, a semi-synthetic antibody portion with human antibody framework regions, or a humanized antibody portion. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of the protein complex, where the antibody portion binds to an equilibrium dissociation constant (K _d ) between about 0.1 pM and about 500 nM (such as about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM , 1 nM, 10 nM, 50 nM, 100 nM, or 500 nM, including any range between these values) HIV-1 RT / MHC class I complex. In some embodiments, the isolated anti RTMC construct bound to K _d between about 500 nM to about 0.1 pM ((such as about 0.1 pM, 1.0 pM, 10 pM , 50 pM, 100 pM, 500 pM, 1 nM , Any of 10 nM, 50 nM, 100 nM, or 500 nM, including any range between these values) HIV-1 RT / MHC class I complex. In some embodiments, the anti-RTMC construct The body comprises an antibody portion which specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the antibody portion comprises: i) a heavy chain variable domain comprising: comprising an amino acid sequence SEQ ID NO: The heavy chain complementarity determining region (HC-CDR) 1 of 240, or a variant thereof containing at most about 3 (such as about any of 1, 2, or 3) amino acid substitutions, including SEQ ID NO: 241- HC-CDR2 of the amino acid sequence of any of 244, or a variant thereof containing up to about 3 (such as about any of 1, 2, or 3) amino acid substitutions, and comprising SEQ ID NO : HC-CDR3 of the amino acid sequence of any one of 245-246, or a variant thereof containing at most about 3 (such as about any of 1, 2, or 3) amino acid substitutions; and ii ) Light chain variable domain, comprising: comprising SEQ ID NO: The amino acid sequence of any one of 247-249 has a light chain complementarity determining region (LC-CDR) 1 or contains up to about 3 (such as about any of 1, 2, or 3) amino groups Acid-substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 250-253, or up to about 3 (such as about any of 1, 2, or 3 ) Amino acid substituted variants thereof. In some embodiments, the anti-RTMC construct comprises an antibody portion that specifically binds to an HIV-1 RT peptide and MHC class I protein, wherein the antibody portion comprises: i) a heavy chain variable domain comprising: comprising SEQ ID NO: HC-CDR1 of the amino acid sequence of any of 75-96 (and consisting of it in some embodiments), or containing up to about 5 (such as about 1, 2, 3, 4 or 5 Any one of them) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any of SEQ ID NOs: 97-124 (and consisting of it in some embodiments), or comprising Up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof, and the amino acid sequence comprising any of SEQ ID NO: 125-163 HC-CDR3 (and consisting of it in some embodiments), or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions; and ii) a light chain variable domain comprising: an LC-CDR1 comprising the amino acid sequence of any of SEQ ID NOs: 164-189 (and consisting of it in some embodiments), or comprising up to about 5 (Such as about any of 1, 2, 3, 4, or 5) Variants of the amino acid substitution, LC-CDR2 comprising the amino acid sequence of any of SEQ ID NOs: 190-207 (and consisting of it in some embodiments), or containing up to about 3 (such as About any of 1, 2, or 3) amino acid substituted variants thereof, and an amino acid sequence comprising any of SEQ ID NO: 208-239 (and consisting of it in some embodiments ), Or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions. In some embodiments, the anti-RTMC construct comprises an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96 (and consisting of it in some embodiments), including the amino group of any one of SEQ ID NO: 97-124 HC-CDR2 of the acid sequence (and consisting of it in some embodiments), and the HC comprising the amino acid sequence of any of SEQ ID NO: 125-163 (and consisting of it in some embodiments) -CDR3; or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the HC-CDR region; and ii) light chain variable domain Which includes: LC-CDR1 comprising the amino acid sequence of any of SEQ ID NO: 164-189 (and consisting of it in some embodiments), including any of SEQ ID NO: 190-207 LC-CDR2 of the amino acid sequence of (and consisting of in some embodiments), and the amino acid sequence comprising any of SEQ ID NO: 208-239 (and in some embodiments by Composition) LC-CDR3; or in LC-C The DR region contains up to about 5 (such as about any of 1, 2, 3, 4 or 5) amino acid substituted variants thereof. In some embodiments, the anti-RTMC construct comprises an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the antibody portion comprises a) comprising SEQ ID NO: 19-46 The heavy chain variable domain of the amino acid sequence of any of (and consisting of, in some embodiments), or at least about 95% (such as at least about 95) of any of SEQ ID NOs: 19-46 %, 96%, 97%, 98%, or 99%) variants of sequence identity; and b) an amino acid sequence comprising any of SEQ ID NOs: 47-74 (and In some embodiments it consists of) a light chain variable domain, or has at least about 95% (such as at least about 95%, 96%, 97%, 98%) from any of SEQ ID NOs: 47-74 Or any of 99%) variants of sequence identity. In some embodiments, the antibody portion comprises: a heavy chain variable domain comprising the amino acid sequence of any of SEQ ID NOs: 19-46 (and consisting of it in some embodiments), and light A chain variable domain, which comprises the amino acid sequence of any one of SEQ ID NOs: 47-74 (and consists of it in some embodiments). In some embodiments, the anti-RTMC construct comprises a first antibody portion that competes with a second antibody portion according to any of the antibody portions described above for binding to a target HIV-1 RT / MHC class I complex . In some embodiments, the first antibody portion and the second antibody portion bind to the same, or substantially the same epitope. In some embodiments, the binding of the first antibody moiety to the target HIV-1 RT / MHC class I complex inhibits the binding of the second antibody moiety to the target HIV-1 RT / MHC class I complex by at least about 70% (Such as at least about any of 75%, 80%, 85%, 90%, 95%, 98%, or 99%), or vice versa. In some embodiments, the first antibody portion and the second antibody portion cross-competitively bind to the target HIV-1 RT / MHC class I complex, that is, each of the first and second antibody portions compete with each other for binding to Target HIV-1 RT / MHC class I complex. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the isolated anti-RTMC constructs are full-length antibodies. In some embodiments, the isolated anti-RTMC construct is monospecific. In some embodiments, the isolated anti-RTMC construct is multispecific. In some embodiments, the isolated anti-RTMC construct is bispecific. In some embodiments, the isolated anti-RTMC molecules are tandem scFv, bifunctional antibody (Db), single chain bifunctional antibody (scDb), dual affinity retargeting (DART) antibody, dual variable domain (DVD) antibody , Pestle-mortar (KiH) antibody, docking lock (DNL) antibody, chemically cross-linked antibody, heteromultimeric antibody or heteroconjugate antibody. In some embodiments, the isolated anti-RTMC construct is a tandem scFv comprising two scFvs connected by peptide linkers. In some embodiments, the peptide linker comprises (and in some embodiments consists of the following) the amino acid sequence of SEQ ID NO: 276. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of the protein complex, wherein the isolated anti-RTMC construct further comprises a second antigen binding portion that specifically binds to the second antigen. In some embodiments, the second antigen binding portion is an antibody portion. In some embodiments, the second antigen is an antigen on the surface of T cells. In some embodiments, the T cells are selected from the group consisting of: cytotoxic T cells, helper T cells, and natural killer T cells. In some embodiments, the second antigen is selected from the group consisting of CD3γ, CD3δ, CD3ε, CD3ζ, CD28, OX40, GITR, CD137, CD27, CD40L, and HVEM. In some embodiments, the second antigen is CD3ε, and the isolated anti-RTMC construct comprises an N-terminal scFv specific for HIV-1 RT / MHC class I complex and a C-terminal scFv specific for CD3ε Connect scFv in series. In some embodiments, the second antigen is an antigen on the surface of natural killer cells, neutrophils, monocytes, macrophages, or dendritic cells. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of the protein complex, where the isolated anti-RTMC construct is a chimeric antigen receptor (CAR). In some embodiments, the chimeric antigen receptor comprises an extracellular domain containing an antibody portion, a transmembrane domain, and an intracellular signaling domain. In some embodiments, the intracellular signaling domain includes CD3ζ intracellular signaling sequences and costimulatory signaling sequences. In some embodiments, the costimulatory signaling sequence is a CD28 or 4-1BB intracellular signaling sequence. In some embodiments, the intracellular signaling domain comprises CD3ζ intracellular signaling sequences and CD28 and / or 4-1BB intracellular signaling sequences. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of the protein complex, wherein the isolated anti-RTMC construct is a chimeric antibody / T cell receptor (abTCR). In some embodiments, the anti-RTMC abTCR comprises an extracellular domain containing an antibody portion and a T cell receptor (TCR) module (TCRM) containing a TCR transmembrane domain. In some embodiments, TCRM can recruit at least one TCR related signaling module. In some embodiments, the TCR-related signaling module is selected from the group consisting of CD3δε, CD3γε, and ζζ. In some embodiments, the antibody portion comprises: a) a first polypeptide chain comprising a first antigen binding domain, the first antigen binding domain comprising _VH and _CH1 antibody domains; and b) comprising a second antigen binding domain the second polypeptide chain, the second antigen binding domain comprises an antibody V _L and a C _L domain, wherein the first antigen-binding domain of the V _H and C _H 1 domain and the second antigen binding domains V _L and C _L domains of Form a Fab-like antigen binding module that specifically binds to RTMC. In some embodiments, according to any of the anti-RTMC constructs described above (such as isolated anti-RTMC constructs), the anti-RTMC construct comprises specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of the protein complex, wherein the isolated anti-RTMC construct is an immunoconjugate comprising the antibody portion and the effector molecule. In some embodiments, the effector molecule is a therapeutic agent selected from the group consisting of drugs, toxins, radioisotopes, proteins, peptides, and nucleic acids. In some embodiments, the therapeutic agent is a drug or toxin. In some embodiments, the effector molecule is a label. In other embodiments, host cells expressing or related to the RTMC construct or polypeptide component thereof are provided. In some embodiments, nucleic acids encoding anti-RTMC constructs or polypeptide components thereof are provided. In some embodiments, a vector comprising nucleic acid is provided. In some embodiments, effector cells that exhibit or are associated with anti-RTMC constructs are provided. In some embodiments, the effector cells are T cells. In other embodiments, there is provided a pharmaceutical composition comprising an anti-RTMC construct (such as an isolated anti-RTMC construct) according to any of the embodiments described above, a host cell, nucleic acid, vector, or effector cell . In some embodiments, the pharmaceutical composition further comprises a pharmaceutically acceptable carrier. In some embodiments, a method for detecting a cell presenting a complex comprising HIV-1 RT peptide and MHC class I protein on its surface is provided, which comprises: allowing the cell to be in accordance with any of the embodiments described above One of the anti-RTMC constructs (such as an isolated anti-RTMC construct), the anti-RTMC construct comprising: a) an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) Markers; and detect the presence of markers on cells. In some embodiments, there is provided a method of treating an individual suffering from HIV-1 infection, comprising administering to the individual an effective amount of a pharmaceutical composition according to any of the embodiments described above, the pharmaceutical combination Objects include anti-RTMC constructs (such as isolated anti-RTMC constructs). In some embodiments, the pharmaceutical composition further comprises cells (such as effector cells) associated with the isolated anti-RTMC construct. In some embodiments, there is provided a method of treating an individual with HIV-1 infection, comprising administering to the individual an effective amount of effector cells exhibiting any of the anti-RTMC CAR or anti-RTMC abTCR described above . In some embodiments, the effector cells are T cells. In some embodiments, the individual is a human. In some embodiments, there is provided a method of diagnosing an individual with HIV-1 infection, which comprises: a) administering to the individual an effective amount of a marker-containing experience according to any of the embodiments described above Isolate the anti-RTMC construct; and b) Determine the content of the marker in the individual, where the content of the marker above the threshold level indicates that the individual has HIV-1 infection. In some embodiments, a method of diagnosing an individual with HIV-1 infection is provided, comprising: a) combining a sample derived from the individual with a marker-containing experience according to any of the embodiments described above Contact with the isolated anti-RTMC construct; and b) determine the number of cells bound to the isolated anti-RTMC construct in the sample, where the value of the number of cells bound to the isolated anti-RTMC construct is higher than the threshold level The individual has HIV-1 infection. In some embodiments, the individual is a human. Also provided is a method of manufacturing any of the constructs described herein, articles and kits suitable for the methods described herein.

Cross-Reference to Related Applications This application claims the priority of US Provisional Application No. 62 / 399,210 filed on September 23, 2016, which is incorporated by reference in its entirety. Submit the sequence table in the form of an ASCII text file The following content submitted in the ASCII text file is incorporated into the text by reference in full text: the sequence table in the computer readable form (CRF) (file name: 750042000740SEQLIST.txt, record date: 2017 September 22, size: 145 KB). The present application provides an isolated construct (referred to herein as an "anti-RTMC construct") that includes a complex that specifically binds to an HIV-1 RT peptide and MHC class I protein (referred to herein as an "HIV-1 RT / MHC class I complex" or "RTMC") antibody portion (referred to herein as "anti-RTMC antibody portion"). Proteins expressed by viruses such as HIV represent an excellent target for immunotherapy because they are not expressed in normal cells. RT is an intracellular protein that has not been successfully targeted against cell surface proteins by cytotoxic effect cell therapy. YQYMDDLYV is the HLA-A2 restricted HIV-1 epitope in HIV-1 RT. The YQYMDDLYV epitope is one of the 14 most conserved regions of the HIV proteome in the four main HIV-1 branch lines A, B, C and D (Létourneau, S. et al. (2007)PloS one , 2 (10): e984; Harrer, E. et al. (1996)Journal of Infectious Diseases 173 (2): 476-479). Since this epitope is located in the active site of RT and is the target of many reverse transcriptase inhibitors, it has great clinical relevance. One of the most common mutations that cause drug resistance in RT, M184V, is in this region (Shafer, R. W., & Schapiro, J. M. (2008)AIDS reviews 10 (2): 67). The anti-RTMC construct specifically recognizes the HIV-1 RT / MHC class I complex. In some embodiments, the HIV-1 RT / MHC class I complex is on the surface expressing HIV-1 RT cells. The anti-RTMC construct can specifically bind to the N-terminal part, C-terminal part or middle part of the HIV-1 RT peptide in the complex, and / or different subtypes containing HIV-1 RT peptide and MHC class I protein At least one complex cross-reacts (eg, the anti-RTMC construct binds to both HIV-1 RT peptide / HLA-A * 02: 01 complex and HIV-1 RT peptide / HLA-A * 02: 02 complex). The anti-RTMC construct allows specific targeting of RTMC presenting cells (ie cells presenting on their surface binding to the MHC molecule HIV-1 RT peptide), such as infected cells expressing HIV-1 RT. This strategy provides significant technical advantages due to the use of antibodies against HIV-1 RT protein, which cannot specifically target RTMC presenting cells using these antibodies. In addition, when fused to a detectable part, the anti-RTMC antibody part allows diagnosis and prognosis of HIV-1 infection with high sensitivity to changes in the number and distribution of RTMC presenting cells. Using phage display technology, we produced multiple individual antigen-binding antibody fragments that have specificity and high affinity for the HIV-1 RT 181 peptide / HLA-A * 02: 01 complex. Flow cytometry and T cell-mediated cytotoxicity analysis showed that the antibody recognized HIV-1 RT peptide-pulsed T2 cells in an HIV-1 RT and HLA-A * 02: 01 restricted manner. When armed with anti-CD3 bispecific antibodies, the antibodies redirect human T cells to kill HIV-1 RT positive and HLA-A * 02: 01 positive target cells. The data provided herein indicates that antibodies against HIV-1 RT peptides in the case of HLA complexes can be effective therapeutic agents for HIV-1 infection. The present application therefore provides a construct (such as an isolated construct) comprising an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein. The construct can be, for example, a full-length anti-RTMC antibody, a multispecific anti-RTMC molecule (such as a bispecific anti-RTMC antibody), an anti-RTMC chimeric antigen receptor ("CAR"), or an anti-RTMC immunoconjugate. In another aspect, a nucleic acid encoding an anti-RTMC construct or a portion of an anti-RTMC antibody portion of the construct is provided. In another aspect, a composition comprising an anti-RTMC construct is provided, the construct comprising an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein. The composition may be a pharmaceutical composition comprising anti-RTMC constructs or effector cells exhibiting anti-RTMC constructs or associated with anti-RTMC constructs (eg T cells exhibiting anti-RTMC CAR or anti-RTMC abTCR). Also provided are methods for manufacturing and using anti-RTMC constructs (or cells expressing anti-RTMC constructs or cells related thereto) for therapeutic or diagnostic purposes, as well as kits and products suitable for such methods. Definitions As used herein, "treatment (treating)" is a method for obtaining beneficial or desired results (including clinical results). For the purposes of the present invention, beneficial or desired clinical results include (but are not limited to) one or more of the following: alleviate one or more symptoms arising from the disease, reduce the degree of the disease, stabilize the disease (eg, prevent or delay the disease) Exacerbate), prevent or delay the spread of the disease, prevent or delay the recurrence of the disease, delay or slow the progression of the disease, improve the condition of the disease, provide disease remission (partial or complete), reduce the dose of one or more other drugs required to treat the disease, delay the disease Progress, improve or improve quality of life, increase weight gain and / or prolong survival. "Treatment" also covers the reduction of the pathological results of the disease. The methods of the present invention encompass any one or more of these treatment modalities. The term "refractory" or "tolerability" refers to a disease that does not respond to treatment. As used herein with regard to CD3 expressing cells, "activation" refers to the state of detectably elevated cells that have been sufficiently stimulated to induce downstream effector functions of CD3 signaling pathways, including but not limited to cell proliferation and interleukin production. The term "antibody portion" includes full-length antibodies and antigen-binding fragments thereof. A full-length antibody contains two heavy chains and two light chains. The variable regions of the light and heavy chains are responsible for antigen binding. The variable regions in both chains generally contain three highly variable loops called complementarity determining regions (CDRs) (light chain (LC) CDRs include LC-CDR1, LC-CDR2 and LC-CDR3, heavy chain (HC ) CDR includes HC-CDR1, HC-CDR2 and HC-CDR3). The CDR boundaries of the antibodies and antigen-binding fragments disclosed herein can be defined or identified by the Kabat, Chothia, or Al-Lazikani conventions (Al-Lazikani 1997; Chothia 1985; Chothia 1987; Chothia 1989; Kabat 1987; Kabat 1991). The three CDRs of the heavy or light chain are inserted between the lateral extensions called the framework regions (FR). These lateral extensions are more conservative than CDRs and form a framework that supports hypervariable loops. The constant regions of the heavy and light chains do not participate in antigen binding, but exhibit various effector functions. Antibodies are assigned to various classes based on the amino acid sequence of the constant region of their heavy chains. The five main classes or isotypes of antibodies are IgA, IgD, IgE, IgG, and IgM, which are characterized by the presence of α, δ, ε, γ, and μ heavy chains, respectively. Several major antibody classes are divided into subcategories, such as lgG1 (γ1 heavy chain), lgG2 (γ2 heavy chain), lgG3 (γ3 heavy chain), lgG4 (γ4 heavy chain), lgA1 (α1 heavy chain), or lgA2 (α2 heavy chain) . The term "antigen-binding fragment" as used herein refers to antibody fragments, including, for example, bifunctional antibodies, Fab, Fab ', F (ab') 2, Fv fragments, disulfide stabilized Fv fragments (dsFv), (dsFv) 2 , Bispecific dsFv (dsFv-dsFv '), disulfide-stabilized bifunctional antibody (ds bifunctional antibody), single chain antibody molecule (scFv), scFv dimer (bivalent bifunctional antibody), consisting of one or Part of an antibody of multiple CDRs forms a multispecific antibody, camel's single domain antibody, nanobody antibody, domain antibody, bivalent domain antibody, or any other antibody fragment that binds to an antigen but does not contain the entire antibody structure. The antigen-binding fragment can bind to the same antigen as the parent antibody or parent antibody fragment (eg, parent scFv). In some embodiments, the antigen-binding fragment may comprise one or more CDRs from a specific human antibody grafted to the framework regions from one or more different human antibodies. The term "epitope" as used herein refers to a specific atom or group of amino acids on the antigen to which the antibody or antibody portion is bound. If two antibodies or antibody portions exhibit competitive binding to an antigen, they can bind the same epitope within the antigen. "Fab-like antigen binding module" refers to an antibody portion comprising a first polypeptide chain and a second polypeptide chain, wherein the first and second polypeptide chains comprise V_L Antibody domain, C_L Antibody domain, V_H Antibody domain and C_H 1 Antibody domain. V_L And C_L The antibody domain can be on one chain, and V_H And C_H 1 The antibody domain is on another chain; or V_L And C_H 1 Antibody domain can be located on a chain, and V_H And C_L The antibody domain is on another chain. In some embodiments, the first and second polypeptide chains are linked such as by peptide bonds or by another chemical bond (such as a disulfide bond). As used herein, the first antibody portion inhibits target RTMC binding of the second antibody portion by at least about 50% (such as at least about 55%, 60%, 65%) when the first antibody portion is at an equal molarity , 70%, 75%, 80%, 85%, 90%, 95%, 98% or 99%), the first antibody part and the second antibody part "compete" to bind to the target RTMC, Or vice versa. The high-throughput process of "binning" antibodies based on their cross-competition is described in PCT Publication No. WO 03/48731. As used herein, the term "specific binding" or "specific to" refers to a measurable and reproducible interaction, such as the binding between a target and an antibody or antibody portion, which is in a heterogeneous molecule The presence of a population (including biomolecules) determines the presence of targets. For example, an antibody or antibody portion that specifically binds to a target (which can be an epitope) is more affinity, affinity, easiness, and / or duration of binding to this target than it is to bind to other targets The antibody or antibody part. In some embodiments, an antibody or antibody portion that specifically binds to an antigen has one or more antigenic determinants (eg, HIV-1) with at least about 10 times its binding affinity for other targets and one or more antigenic determinants of the antigen RT peptide / MHC class I protein complex) reaction. The term "T cell receptor" or "TCR" refers to a heterodimeric receptor composed of paired αβ or γδ chains on the surface of T cells. Each α, β, γ, and δ chain is composed of two Ig-like domains: a variable domain (V) conferred by the complementarity determining region (CDR) for antigen recognition, followed by an anchoring by a linking peptide and a transmembrane (TM) region To the constant domain of the cell membrane (C). The TM area is combined with a constant subunit of the CD3 signal transmission device. Each of the V domains has three CDRs. Complex interactions between these CDRs and antigen peptides bound to proteins encoded by the major histocompatibility complex (pMHC) (Davis and Bjorkman (1988) Nature, 334, 395-402; Davis et al. (1998 ) Annu Rev Immunol, 16, 523-544; Murphy (2012), xix, p. 868). The term "TCR-related signaling molecule" refers to a molecule having an activation motif (ITAM) based on the cytoplasmic immune receptor tyrosine, which is part of the TCR-CD3 complex. TCR-related signaling molecules include CD3γε, CD3δε, and ζζ, and are necessary for TCR's signaling ability. The term "module" when referring to a part of a protein is meant to include structurally and / or functionally related parts that constitute one or more polypeptides of the protein. For example, the transmembrane module of the dimeric receptor may refer to the transmembrane portion of each polypeptide chain of the receptor. Module can also refer to the relevant part of a single polypeptide chain. For example, the transmembrane module of the monomeric receptor may refer to the transmembrane portion of the single polypeptide chain of the receptor. The module may also include only a single part of the polypeptide. As used herein, the "isolated" anti-RTMC construction system refers to (1) not related to proteins found in nature, (2) free of other proteins from the same source, (3) expressed by cells from different species, or ( 4) Anti-RTMC constructs that do not exist in nature. The term "isolated nucleic acid" as used herein is intended to mean genomic nucleic acid, cDNA, or a nucleic acid of synthetic origin or some combination thereof, with the aid of which source, "isolated nucleic acid" (1) is not found in "isolated nucleic acid" All or part of the polynucleotides in nature are related, (2) are operably linked to polynucleotides that are not linked to them in nature, or (3) do not exist as part of a larger sequence in nature. As used herein, the terms "CDR" or "complementarity determining region" are intended to mean non-contiguous antigen combination sites found within the variable regions of both heavy and light chain polypeptides. These specific areas have been described by: Kabat et al., J. Biol. Chem. 252: 6609-6616 (1977); Kabat et al., US Dept. of Health and Human Services, "Sequences of proteins of immunological interest" ( 1991); Chothia et al., J. Mol. Biol. 196: 901-917 (1987); and MacCallum et al., J. Mol. Biol. 262: 732-745 (1996), where these definitions are compared with each other Includes overlaps or subsets of amino acid residues. Nevertheless, the use of any definition to refer to the CDR of an antibody or grafted antibody or variants thereof is intended to fall within the scope of the term as defined and used herein. The amino acid residues covering the CDRs defined by each of the references cited above are set forth in Table 1 as a comparison as follows.table 1 : CDR definition ¹ Numbering of residues follows the nomenclature previously described by Kabat et al.² The residue numbering follows the nomenclature described by Chothia et al.³ The residue numbers follow the nomenclature of MacCallum et al. The term "chimeric antibody" refers to the following antibodies and fragments of such antibodies, in which part of the heavy chain and / or light chain is derived from a specific species or belongs to a specific antibody class or The corresponding sequence in a class of antibodies is identical or homologous, and the remainder of the chain (s) is identical or homologous to the corresponding sequence in an antibody derived from another species or belonging to another antibody class or subclass, as long as the Such antibodies or fragments can exhibit the biological activity of the present invention (see US Patent No. 4,816,567; and Morrison et al.,Proc . Natl . Acad . Sci . USA , 81: 6851-6855 (1984)). The term "semi-synthetic" with respect to an antibody or antibody portion means that the antibody or antibody portion has one or more naturally occurring sequences and one or more non-naturally occurring (ie, synthetic) sequences. "Fv" is the smallest antibody fragment that contains complete antigen recognition and antigen binding sites. This fragment consists of a dimer of a heavy chain variable region and a light chain variable region that are tightly and non-covalently associated. From the folding of these two domains, six hypervariable circuits (each from three circuits of the heavy chain and the light chain) are issued, which promote the antigen binding of amino acid residues and confer antigen binding specificity to the antibody. However, even if a single variable domain (or one-half of an Fv containing only three CDRs specific for an antigen) can recognize and bind the antigen, the affinity is lower than the entire binding site. `` Single-chain Fv '' (also abbreviated as `` sFv '' or `` scFv '') includes V linked to a single polypeptide chain<sub>H</sub> And V<sub>L</sub> Antibody fragments of the antibody domain. In some embodiments, the scFv polypeptide is at V<sub>H</sub> With V<sub>L</sub> A polypeptide linker is further included between the domains, which enables the scFv to form the desired structure for antigen binding. For comments on scFv, see Pluckthun,The Pharmacology of Monoclonal Antibodies , Volume 113, edited by Rosenburg and Moore, Springer-Verlag, New York, pages 269-315 (1994). The term "bifunctional antibody" refers to small antibody fragments prepared as follows: usually V<sub>H</sub> With V<sub>L</sub> Short linkers between domains (such as about 5 to about 10 residues) construct scFv fragments (see previous paragraphs) so that inter-chain rather than intra-chain pairing of V domains is achieved, resulting in bivalent fragments, that is Fragments of two antigen binding sites. Bispecific bifunctional antibodies are heterodimers of two "crossover" scFv fragments, of which the V of two antibodies<sub>H</sub> And V<sub>L</sub> Domains exist on different polypeptide chains. Bifunctional antibodies are more fully described in, for example, EP 404,097; WO 93/11161; and Hollinger et al.,Proc . Natl . Acad . Sci . USA , 90: 6444-6448 (1993). "Humanized" forms of non-human (eg, rodent) antibodies are chimeric antibodies that contain minimal sequences derived from non-human antibodies. To a great extent, humanized antibodies are human immunoglobulins (recipient antibodies), in which the residues from the hypervariable region (HVR) of the recipient are derived from such Replacement of residues in hypervariable regions of non-human species (donor antibodies) of rats, rabbits or non-human primates. In some cases, framework region (FR) residues of human immunoglobulin are replaced by corresponding non-human residues. In addition, the humanized antibody may contain residues not found in the recipient antibody or the donor antibody. These modifications are made to further improve antibody performance. In general, a humanized antibody will comprise at least one and usually two variable domains of substantially all variable domains, wherein all or substantially all hypervariable circuits correspond to non-human immunoglobulin hypervariable circuits and all or Basically all FRs are FRs of human immunoglobulin sequences. The humanized antibody will also optionally include at least a portion of an immunoglobulin constant region (Fc), usually, at least a portion of a human immunoglobulin constant region. For other details, see Jones et al.,Nature 321: 522-525 (1986); Riechmann et al.,Nature 332: 323-329 (1988); and Presta,Curr . Op . Struct . Biol . 2: 593-596 (1992). The "amino acid sequence identity percentage (%)" or "homology" with respect to the polypeptide and antibody sequences identified herein is defined as the situation after considering any conservative substitutions as part of the sequence identity after sequence alignment Below, the percentage of amino acid residues in the candidate sequence that are identical to the amino acid residues in the compared polypeptide. Alignment for the purpose of determining the percent amino acid sequence identity can be achieved in various ways within the skill in the art, for example using publicly available computer software such as BLAST, BLAST-2, ALIGN, Megalign (DNASTAR) Or MUSCLE software. Those skilled in the art can determine appropriate parameters for measuring alignment, including any algorithms needed to achieve maximum alignment over the full length of the compared sequences. However, for the purposes of this article, the sequence comparison computer program MUSCLE was used to generate the amino acid sequence identity% value (Edgar, R.C.,Nucleic Acids Research 32 (5): 1792-1797, 2004; Edgar, R.C.,BMC Bioinformatics 5 (1): 113, 2004). The term "Fc receptor" or "FcR" is used to describe a receptor that binds to the Fc region of an antibody. In some embodiments, the FcR of the present invention is an FcR that binds an IgG antibody (gamma receptor) and includes receptors of the FcγRI, FcγRII, and FcγRIII subclasses (including dual gene variants and alternate splicing forms of these receptors). FcγRII receptors include FcγRIIA (“activated receptor”) and FcγRIIB (“inhibited receptor”), both of which have similar amino acid sequences that differ mainly in their cytoplasmic domain. The activated receptor FcyRIIA contains an immunoreceptor tyrosine-based activation motif (ITAM) in its cytoplasmic domain. The inhibitory receptor FcγRIIB contains an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic domain (see review M. in Daëron,Annu . Rev . Immunol . 15: 203-234 (1997)). The term includes allotypes, such as FcyRIIIA allotypes: FcyRIIIA-Phe158, FcyRIIIA-Val158, FcyRIIA-R131 and / or FcyRIIA-H131. FcR in Ravetch and Kinet,Annu . Rev . Immunol 9: 457-92 (1991); Capel et al.,Immunomethods 4: 25-34 (1994); and de Haas and others,J . Lab . Clin . Med . 126: 330-41 (1995). Other FcRs include those identified in the future and are covered by the term "FcR" herein. The term also includes the neonatal receptor FcRn, which is responsible for delivering maternal IgG to the fetus (Guyer et al.,J . Immunol .117: 587 (1976) and Kim et al.,J . Immunol . 24: 249 (1994)). The term "FcRn" refers to the neonatal Fc receptor (FcRn). FcRn is structurally similar to the major histocompatibility complex (MHC) and consists of an alpha chain non-covalently bound to β2-microglobulin. The various functions of neonatal Fc receptor FcRn are reviewed in Ghetie and Ward (2000)Annu . Rev . Immunol . 18, 739-766. FcRn plays a role in the passive transfer of immunoglobulin IgG and serum IgG content from the mother to the larvae. FcRn can act as a rescue receptor, which binds and transports a complete form of endocytotic IgG within and across cells, and rescues it from a predetermined degradation pathway. Human IgG Fc region "C<sub>H</sub> The "domain 1" (also known as "C1" of the "H1" domain) generally extends from about amino acid 118 to about amino acid 215 (EU numbering system). The `` hinge region '' is usually defined as extending from Glu216 of human IgG1 to Pro230 (Burton,Molec . Immunol .22: 161-206 (1985)). The hinge regions of other IgG isotypes can be aligned with the IgG1 sequence by placing the first and last cysteine residues forming the S-S bond between the heavy chains in the same position. The "CH2 domain" of the human IgG Fc region (also known as the "C2" domain of the "H2" domain) generally extends from about amino acid 231 to about amino acid 340. The CH2 domain is unique in that it is not closely paired with another domain. In fact, two N-linked branched-chain carbohydrate chains are inserted between the two CH2 domains of a complete natural IgG molecule. It has been speculated that carbohydrates can provide a substitute for domain-domain pairing and help stabilize the CH2 domain. Burton,Molec Immunol. 22: 161-206 (1985). The "CH3 domain" (also known as the "C2" or "H3" domain) contains the elongation from the C-terminus of the residue in the Fc region to the CH2 domain (ie, about amino acid residue 341 to the C-terminus of the antibody sequence, usually At amino acid residues 446 or 447 of IgG). The "functional Fc fragment" has the "effector function" of the native sequence Fc region. Exemplary "effector functions" include C1q binding; complement dependent cytotoxicity (CDC); Fc receptor binding; antibody-dependent cell-mediated cytotoxicity (ADCC); phagocytosis; down-regulation of cell surface receptors (eg B cells) Receptor; BCR), etc. These effector functions generally require the Fc region to be combined with a binding domain (eg, antibody variable domain) and can be evaluated using various analyses known in the art. Variant IgG Fc antibodies with "altered" FcR binding affinity or ADCC activity are enhanced or reduced FcR binding activity (eg, FcγR or FcRn) compared to the parent polypeptide or a polypeptide comprising a native sequence Fc region and / Or ADCC activity antibody. Variant Fc "showing increased binding to FcR" has a higher affinity (e.g. lower apparent K than parent polypeptide or native sequence IgG Fc_d Or IC₅₀ Value) binds at least one FcR. According to some embodiments, the binding increase compared to the parent polypeptide is about 3-fold (such as about any of 5, 10, 25, 50, 60, 100, 150, 200, or up to 500-fold, or about 25% Up to 1000%). Polypeptide variants that "show reduced binding to FcR" have a lower affinity (e.g. higher apparent K_d Or higher IC₅₀ Value) binds at least one FcR. The reduction in binding compared to the parent polypeptide may be about 40% or more. "Antibody-dependent cell-mediated cytotoxicity" or "ADCC" refers to the following cytotoxic forms: which bind to certain cytotoxic cells (eg, natural killer (NK) cells, neutrophils, and macrophages) The secreted Ig of the existing receptor (FcR) allows these cytotoxic effector cells to specifically bind to antigen-bearing target cells and subsequently kill the target cells with cytotoxin. Antibodies "arm" cytotoxic cells and are absolutely necessary for such killing. Primary cells used to regulate ADCC (NK cells) only express FcγRIII, while monocytes express FcγRI, FcγRII and FcγRIII. The performance of FcR on hematopoietic cells is summarized in Ravetch and Kinet,Annu . Rev . Immunol . 9: 457-92 (1991), page 464, table 3. To assess the ADCC activity of related molecules, an in vitro ADCC analysis can be performed, such as the analysis described in US Patent No. 5,500,362 or 5,821,337. Effector cells suitable for this type of analysis include peripheral blood mononuclear cells (PBMC) and natural killer (NK) cells. Alternatively or in addition, the ADCC activity of related molecules can be assessed in vivo, for example, as disclosed in Clynes et al.PNAS ( USA ) 95: 652-656 (1998) in the animal model. Polypeptides that contain "variable Fc regions that exhibit increased ADCC" or that mediate antibody-dependent cell-mediated cytotoxicity (ADCC) in the presence of human effector cells are more effective than those with wild-type IgG Fc or parent polypeptides When the amount of the polypeptide having a variant Fc region and the polypeptide (or parent polypeptide) having a wild-type Fc region in the analysis is substantially the same, a polypeptide that mediates ADCC substantially more effectively in vitro or in vivo. In general, such variants will be identified using any in vitro ADCC analysis known in the art, such as assays or methods used to determine ADCC activity in, for example, animal models. In some embodiments, the effectiveness of the variant-mediated ADCC is about 5 times to about 100 times (eg, about 25 to about 50 times) the wild-type Fc (or parent polypeptide). "Complement dependent cytotoxicity" or "CDC" refers to the lysis of target cells in the presence of complement. The activation of the classical complement pathway is initiated by the first component of the complement system (C1q) binding to (of the appropriate subclass) antibodies that bind to their cognate antigens. To assess complement activation, CDC analysis can be performed, such as Gazzano-Santoro et al.,J . Immunol . Methods 202: 163 (1996). Polypeptide variants with altered amino acid sequences in the Fc region and increased or decreased C1q binding ability are described in US Patent No. 6,194,551B1 and WO99 / 51642. The contents of their patent publications are specifically incorporated herein by reference. See also Idusogie et alJ . Immunol . 164: 4178-4184 (2000). Unless otherwise specified, "nucleotide sequences encoding amino acid sequences" includes all nucleotide sequences that are degenerate versions of each other and encode the same amino acid sequence. The phrase nucleotide sequence encoding protein or RNA may also include introns to the extent that the nucleotide sequence encoding protein may contain introns in some versions. The term "operably linked" refers to the functional bond between the regulatory sequence and the heterologous nucleic acid sequence, which results in the latter's performance. For example, when the first nucleic acid sequence and the second nucleic acid sequence are in a functional relationship, the first nucleic acid sequence is operably linked to the second nucleic acid sequence. For example, if the promoter affects the transcription or performance of the coding sequence, the promoter is operably linked to the coding sequence. Generally speaking, the operably linked DNA sequences are continuous, and when it is necessary to join two protein coding regions, they are in the same reading frame. "Homologous" refers to the sequence similarity or sequence identity between two polypeptides or between two nucleic acid molecules. When a position in the two compared sequences is occupied by the same base or amino acid monomer subunit, for example, if a position in each of the two DNA molecules is occupied by adenine, the molecules are located in the Same position. The% homology between two sequences is a function of the number of matching or homologous positions shared by the two sequences divided by the number of compared positions multiplied by 100. For example, if 6/10 of the two sequences match or are homologous, the two sequences are 60% homologous. For example, the DNA sequences ATTGCC and TATGGC share 50% homology. In general, comparisons are made when two sequences are aligned to produce the largest percentage of homology. The "effective amount" of the anti-RTMC construct or composition as disclosed herein is an amount sufficient for the specific stated purpose. The "effective amount" can be determined empirically and by known methods related to the stated purpose. The term "therapeutically effective amount" refers to an amount of an anti-RTMC construct or composition as disclosed herein that is effective to "treat" an individual's disease. In the case of HIV-1 infection, a therapeutically effective amount of an anti-RTMC construct or composition as disclosed herein can reduce the number of HIV-1 infected cells; reduce HIV-1 replication; inhibit (i.e. To some extent slows and preferably stops) the spread to infected uninfected cells; and / or to some extent relieves one or more of the symptoms associated with HIV-1 infection. To the extent that an anti-RTMC construct or composition as disclosed herein can kill existing HIV-1 infected cells, it can be cytotoxic. In some embodiments, the therapeutically effective amount is an amount that prolongs the survival of the patient. As used herein, "pharmacologically acceptable" or "pharmacologically compatible" means a substance that is not biologically or otherwise unsuitable, for example, the substance can be incorporated into a pharmaceutical composition administered to a patient Without causing any significant unsuitable biological effects or interacting with any other components of the composition containing them in a harmful manner. Pharmaceutically acceptable carriers or excipients preferably meet the required standards of toxicology and manufacturing testing and / or include guidelines for inactive ingredients developed by the US Food and Drug Administration ( Inactive Ingredient Guide). The term "label" when used herein refers to a detectable compound or composition that can be directly or indirectly bound to an anti-RTMC antibody moiety. The label itself can be detectable (for example, a radioisotope label or a fluorescent label), or in the case of an enzyme label, can catalyze a chemical change of the substrate compound or composition, which change is detectable. It should be understood that the embodiments of the present invention described herein include "consisting of embodiments" and / or "essentially consisting of embodiments". Herein, reference to "about" a value or parameter includes (and describes) changes to that value or parameter itself. For example, a reference to "about X" includes a description of "X". As used herein, the reference to "not" a value or parameter generally means and describes "except for a value or parameter." For example, the method is not used to treat type X infection means that the method is used to treat types of infections other than type X. Unless the context clearly indicates otherwise, the singular forms "a (an) (a / an)" and "the" include plural (species) indicators as used in this and the accompanying patent applications. In an aspect of the anti-RTMC construct, the present invention provides an HIV-1 RT / MHC class I complex-specific construct (anti-RTMC construct), which comprises a specific binding to an HIV-1 RT peptide and MHC class I The antibody portion of a protein complex ("HIV-1 RT / MHC class I complex" or "RTMC"). In some embodiments, the anti-RTMC construct is an isolated anti-RTMC construct. The specificity of the anti-RTMC construct is derived from the anti-RTMC antibody portion that specifically binds to RTMC, such as a full-length antibody or antigen-binding fragment thereof. In some embodiments, reference to a portion (such as an antibody portion) that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein means that the portion binds to RTMC as follows: a) is its response to full-length HIV -1 RT, no HIV-1 RT peptide, MHC class I protein that does not bind to the peptide, and / or MHC class I protein that binds to a non-HIV-1 RT peptide has a binding affinity of at least about 10 ( Contains, for example, at least about 10, 20, 30, 40, 50, 75, 100, 200, 300, 400, 500, 750, 1000, or greater than 1000 times any affinity); K of each of full-length HIV-1 RT, HIV-1 RT peptide-free, MHC class I protein that does not bind to the peptide, and / or MHC class I protein that binds to a non-HIV-1 RT peptide_d Of no more than about 1/10 400, 1/500, 1/750, 1/1000 or less than 1/1000) times K_d . Binding affinity can be determined by methods known in the art, such as ELISA, fluorescence activated cell sorting (FACS) analysis or radioimmunoprecipitation analysis (RIA). K_d It can be determined by methods known in the art, such as surface plasmon resonance (SPR) analysis using, for example, Biacore instruments, or kinetic exclusion analysis (KinExA) using, for example, Sapidyne instruments. Covered anti-RTMC constructs include, for example, full-length anti-RTMC antibodies, multispecific (such as bispecific) anti-RTMC molecules, anti-RTMC chimeric antigen receptors (CAR), and anti-RTMC immunoconjugates. For example, in some embodiments, an anti-RTMC construct (such as an isolated anti-RTMC construct) is provided that includes an anti-RTMC antibody that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein section. In some embodiments, the HIV-1 RT peptide comprises (such as consisting of) the amino acid sequence of any one of SEQ ID NOs: 5-18. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01 (Genbank deposit number: AAO20853). In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the anti-RTMC construct ranges from about 0.1 pM to about 500 nM (such as about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM, 50 nM, 100 nM or 500 nM, including any range between these values) K_d Combined with RTMC. In some embodiments, the anti-RTMC construct and at least one variant (such as at least 2, 3) of a variant of an HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC construct cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, there is provided an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and HLA-A * 02: 01, the HIV-1 RT peptide comprising SEQ ID NO: The amino acid sequence of any one of 5-18 (such as consisting of it). In some embodiments, the HIV1-RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7) ), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the anti-RTMC construct ranges from about 0.1 pM to about 500 nM (such as about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM, 50 nM, 100 nM or 500 nM, including any range between these values) K_d Combined with RTMC. In some embodiments, the anti-RTMC construct and at least one variant (such as at least 2, 3) of a variant of an HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC construct cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, an anti-RTMC construct is provided that includes an antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody portion includes: i) heavy chain A variable domain sequence comprising: the HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240, or a variant comprising at most about 3 (eg, any of about 1, 2 or 3) amino acid substitutions , HC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 241-244, or comprising at most about 3 (eg, about any of 1, 2, or 3) amino acid substitutions Variants, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246, or comprising up to about 3 (eg, about any of 1, 2, or 3) amino acids Variants thereof; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 247-249, or up to about 3 (eg about Any one of 1, 2 or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253, or containing up to about 3 (E.g. about any of 1, 2, or 3) Acid substituted variants thereof. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the anti-RTMC construct ranges from about 0.1 pM to about 500 nM (such as about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM, 50 nM, 100 nM or 500 nM, including any range between these values) K_d Combined with RTMC. In some embodiments, the anti-RTMC construct and at least one variant (such as at least 2, 3) of a variant of an HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC construct cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, an anti-RTMC construct is provided that includes an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody portion includes: i) heavy A chain variable domain sequence comprising: an HC-CDR1 comprising the amino acid sequence of any of SEQ ID NOs: 75-96 (and consisting of it in some embodiments); or comprising up to about 5 ( (Eg, any of about 1, 2, 3, 4, or 5) amino acid substituted variants thereof; comprising the amino acid sequence of any one of SEQ ID NOs: 97-124 (and in some embodiments HC-CDR2; or variants containing up to about 5 (eg, any of about 1, 2, 3, 4, or 5) amino acid substitutions; and SEQ ID NO: 125 -HC-CDR3 of the amino acid sequence of (and consisting of, in some embodiments) of any of 163; or comprising up to about 5 (eg, about any of 1, 2, 3, 4, or 5 The variant of amino acid substitution; and ii) the light chain variable domain sequence comprising: an amino acid sequence comprising any one of SEQ ID NO: 164-189 (and in some embodiments by Its composition) LC-CDR1; or contains More than about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; including the amino acid sequence of any one of SEQ ID NO: 190-207 ( And in some embodiments it consists of) LC-CDR2; or a variant comprising up to about 3 (eg, any of about 1, 2, 3) amino acid substitutions; and comprising SEQ ID NO: LC-CDR3 of the amino acid sequence of any of 208-239 (and consisting of it in some embodiments); or comprising up to about 5 (eg, about any of 1, 2, 3, 4, or 5 One) Amino acid substituted variants thereof. In some embodiments, an anti-RTMC construct is provided that includes an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody portion includes: i) heavy Chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any of SEQ ID NO: 75-96 (and consisting of it in some embodiments); comprising SEQ ID NO: 97- HC-CDR2 of the amino acid sequence of any of 124 (and consisting of it in some embodiments); and the amino acid sequence of any of SEQ ID NOs: 125-163 (and in some HC-CDR3 of the embodiment); or variants containing up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions in the HC-CDR sequence ; And ii) a light chain variable domain sequence comprising: LC-CDR1 comprising the amino acid sequence of (and consisting of, in some embodiments) any one of SEQ ID NO: 164-189; comprising SEQ ID NO: LC-CDR2 of the amino acid sequence of any one of 190-207 (and consisting of it in some embodiments); and an amino acid comprising any one of SEQ ID NO: 208-239 Sequence (and in some LC-CDR3 of which it consists of in the examples); or variants containing up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence . In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the anti-RTMC construct ranges from about 0.1 pM to about 500 nM (such as about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM, 50 nM, 100 nM or 500 nM, including any range between these values) K_d Combined with RTMC. In some embodiments, the anti-RTMC construct and at least one variant (such as at least 2, 3) of a variant of an HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC construct cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, there is provided an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody portion comprises: comprising SEQ ID NO: the heavy chain variable domain of the amino acid sequence of any of 19-46 (and consisting of it in some embodiments), or having at least about 95% (eg, at least about 96%, 97%, 98 % Or 99%) variants of sequence identity; and the amino acid sequence comprising (and consisting of, in some embodiments) any of SEQ ID NOs: 47-74 A chain variable domain, or a variant thereof that has at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the anti-RTMC construct ranges from about 0.1 pM to about 500 nM (such as about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM, 50 nM, 100 nM or 500 nM, including any range between these values) K_d Combined with RTMC. In some embodiments, the anti-RTMC construct and at least one variant (such as at least 2, 3) of a variant of an HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC construct cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, an anti-RTMC construct is provided that includes a second anti-RTMC antibody portion that competes for binding to a target HIV-1 RT / MHC class I according to any of the anti-RTMC antibody portions described herein The first anti-RTMC antibody portion of the complex. In some embodiments, the first anti-RTMC antibody portion and the second anti-RTMC antibody portion bind to the same, or substantially the same epitope. In some embodiments, the binding of the first anti-RTMC antibody portion to the target HIV-1 RT / MHC class I complex inhibits the binding of the second anti-RTMC antibody portion to the target HIV-1 RT / MHC class I complex At least about 70% (such as at least about any of 75%, 80%, 85%, 90%, 95%, 98%, or 99%), or vice versa. In some embodiments, the first anti-RTMC antibody portion and the second anti-RTMC antibody portion cross-competitively bind to the target HIV-1 RT / MHC class I complex, ie, each of the first and second antibody portions Compete with each other to bind to the target HIV-1 RT / MHC class I complex. For example, in some embodiments, an anti-RTMC construct is provided that includes an anti-RTMC antibody portion that competes with an antibody portion comprising the following for binding to a target HIV-1 RT / MHC class I complex: i) heavy chain Variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240, or a variant comprising up to about 3 (eg, any of about 1, 2 or 3) amino acid substitutions HC-CDR2 comprising the amino acid sequence of any one of SEQ ID NOs: 241-244, or containing up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions Variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg, any one of 1, 2, or 3) amino groups Acid-substituted variants thereof; and ii) a light chain variable domain comprising LC-CDR1 containing the amino acid sequence of any one of SEQ ID NO: 247-249, or up to about 3 (eg about Any one of 1, 2 or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253, or containing up to about 3 (E.g. about any of 1, 2, or 3) the amino acid is taken Its variant. In some embodiments, there is provided an anti-RTMC construct comprising an anti-RTMC antibody portion that competes with an antibody portion comprising the following for binding to a target HIV-1 RT / MHC class I complex: i) heavy chain variable domain sequence Which comprises: HC-CDR1 comprising the amino acid sequence of any of SEQ ID NO: 75-96 (and consisting of it in some embodiments); or comprising up to about 5 (eg about 1, 2 , Any of 3, 4 or 5) amino acid substituted variants thereof; comprising the amino acid sequence of any one of SEQ ID NO: 97-124 (and consisting of it in some embodiments) HC-CDR2; or variants containing up to about 5 (eg, any of about 1, 2, 3, 4, or 5) amino acid substitutions; and including any of SEQ ID NOs: 125-163 HC-CDR3 of one of the amino acid sequences (and consisting of it in some embodiments); or contains up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acids Variants thereof; and ii) a light chain variable domain sequence comprising: an LC comprising the amino acid sequence of any of SEQ ID NOs: 164-189 (and consisting of it in some embodiments) -CDR1; or contain up to about 5 (eg about 1, 2 , Any of 3, 4 or 5) amino acid substituted variants thereof; comprising the amino acid sequence of any one of SEQ ID NO: 190-207 (and consisting of it in some embodiments) LC-CDR2; or variants containing up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions; and amines including any of SEQ ID NO: 208-239 LC-CDR3 of an acid sequence (and consisting of it in some embodiments); or a variant containing up to about 5 (eg, any of about 1, 2, 3, 4, or 5) amino acid substitutions body. In some embodiments, there is provided an anti-RTMC construct comprising an anti-RTMC antibody portion that competes with an antibody portion comprising the following for binding to a target HIV-1 RT / MHC class I complex: i) heavy chain variable domain sequence Which comprises: HC-CDR1 comprising the amino acid sequence of any of SEQ ID NO: 75-96 (and consisting of it in some embodiments); comprising any of SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence of (and consisting of in some embodiments); and the amino acid sequence comprising any of SEQ ID NOs: 125-163 (and consisting of in some embodiments) Composition) of HC-CDR3; or variants containing up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions in the HC-CDR sequence; and ii) light Chain variable domain sequence comprising: LC-CDR1 comprising the amino acid sequence of any of SEQ ID NO: 164-189 (and consisting of it in some embodiments); comprising SEQ ID NO: 190- LC-CDR2 of the amino acid sequence of any of 207 (and consisting of it in some embodiments); comprising the amino acid sequence of any of SEQ ID NO: 208-239 (and in some implementations (In this case, it is composed of) LC- CDR3; or a variant comprising up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence. In some embodiments, there is provided an anti-RTMC construct comprising an anti-RTMC antibody portion that competes with an antibody portion comprising the following for binding to a target HIV-1 RT / MHC class I complex: comprising SEQ ID NO: 19-46 The heavy chain variable domain of the amino acid sequence of any of (and consisting of, in some embodiments), or having at least about 95% (eg, at least about 96%, 97%, 98%, or 99%) Any of them) a variant of sequence identity; a light chain variable domain comprising the amino acid sequence of (and consisting of, in some embodiments) any of SEQ ID NOs: 47-74, or Variants thereof having at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, there is provided an anti-RTMC construct comprising an anti-RTMC antibody portion that competes with an antibody portion comprising the following for binding to a target HIV-1 RT / MHC class I complex: comprising SEQ ID NO: 19-46 The heavy chain variable domain of the amino acid sequence of any of (and consisting of, in some embodiments), and the amino acid sequence of any of SEQ ID NOs: 47-74 (and in In some embodiments it consists of the light chain variable domain. In some embodiments, the anti-RTMC construct is stable in solution for at least about 1 month (such as at least about 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 Month, 8 months, 9 months, 10 months, 11 months, 1 year, 2 years, or greater than 2 years). Stability can be expressed as, for example, the retention of the effector function of anti-RTMC constructs (eg, target cell killing activity) in an aqueous formulation solution maintained at a storage temperature (eg, 4 ° C). For example, in some embodiments, the anti-RTMC construct is maintained at least 40% (such as at least about 45%, 50%, 55%, 60%, 65%, 70%) in the aqueous formulation solution maintained at the storage temperature , 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or greater than 99% of the effect function for at least about 1 month (such as at least about 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 1 year, 2 years or Greater than any of 2 years). In some embodiments, the storage temperature does not exceed about 25 ° C (such as not exceed about 20, 18, 16, 14, 12, 10, 8, 6, 5, 4, 3, 2, 1, or 0 ° C, or lower ). In some embodiments, the effector function is target cell killing activity. In some embodiments, the antibody portion of the anti-RTMC construct comprises HC-CDR and LC-CDR sequences, and the tandem two scFv bispecific anti-RTMC antibodies comprising the HC-CDR and LC CDR sequences are formulated at a temperature maintained At least 40% (such as at least about 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99% or greater than 99%) of the effect function for at least about 1 month (such as at least about 1 month, 2 months, 3 months, 4 months, 5 months, 6 Month, 7 months, 8 months, 9 months, 10 months, 11 months, 1 year, 2 years or more than 2 years), where the tandem two scFv bispecific anti-RTMC antibodies contain a ) A first scFv that specifically binds to a complex containing HIV-1 RT 181 peptide and MHC class I protein and includes HC-CDR and LC-CDR sequences, and b) a second scFv that specifically binds to CD3ε. In some embodiments, the storage temperature does not exceed about 25 ° C (such as not exceed about 20, 18, 16, 14, 12, 10, 8, 6, 5, 4, 3, 2, 1, or 0 ° C, or lower ). In some embodiments, the effector function is target cell killing activity. The different aspects are discussed in more detail in the following sections. Anti-RTMC antibody portion The anti-RTMC construct includes an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein. In some embodiments, the anti-RTMC antibody portion specifically binds to RTMC present on the cell surface. In some embodiments, the cell is a T cell. In some embodiments, the T cell is CD4⁺ T cells. In some embodiments, the HIV-1 RT peptide is an MHC class I restricted peptide. In some embodiments, the HIV-1 RT peptide is about 8 to about 12 (such as about any of 8, 9, 10, 11, or 12) amino acids in length. In some embodiments, the HIV-1 RT peptide comprises the amino acid sequence of any of SEQ ID NOs: 5-18 (and consists of it in some embodiments). In some embodiments, the HIV-1 RT peptide comprises the sequence of amino acids 181-189 HIV-1 RT (YQYMDDLYV, SEQ ID NO: 5; also referred to herein as "HIV-1 RT 181") (and In some embodiments it consists of). In some embodiments, the MHC class I protein is HLA-A, HLA-B, HLA-C, HLA-E, HLA-F, or HLA-G. In some embodiments, the MHC class I protein is HLA-A. In some embodiments, HLA-A is HLA-A02. In some embodiments, HLA-A02 is HLA-A * 02: 01. In some embodiments, the anti-RTMC antibody portion is a full-length antibody. In some embodiments, the anti-RTMC antibody portion is an antigen-binding fragment, for example, an antigen-binding fragment selected from the group consisting of: Fab, Fab ', F (ab') 2, Fv fragment, disulfide bond stability Fv fragment ( dsFv) and single chain antibody molecules (scFv). In some embodiments, the anti-RTMC antibody portion is scFv. In some embodiments, the anti-RTMC antibody portion is human, humanized, or semi-synthetic. In some embodiments, the anti-RTMC antibody portion specifically binds to the N-terminal portion of the HIV-1 RT peptide in the complex. In some embodiments, the anti-RTMC antibody portion specifically binds to the C-terminal portion of the HIV-1 RT peptide in the complex. In some embodiments, the anti-RTMC antibody portion specifically binds to the middle portion of the HIV-1 RT peptide in the complex. In some embodiments, the anti-RTMC antibody portion (or anti-RTMC construct comprising the anti-RTMC antibody portion) binds with an affinity to a complex comprising HIV-1 RT peptide and MHC class I protein, the affinity of which is The binding affinity of each of the full-length HIV-1 RT, no HIV-1 RT peptide, MHC class I protein that does not bind to the peptide, and / or MHC class I protein that binds to a non-HIV-1 RT peptide is at least about 10 (including, for example, at least about any of 10, 20, 30, 40, 50, 75, 100, 200, 300, 400, 500, 750, 1000, or greater than 1000) times. In some embodiments, the anti-RTMC antibody portion (the anti-RTMC construct comprising the anti-RTMC antibody portion) is_d Bound to a complex containing HIV-1 RT peptide and MHC class I protein, the K_d K for each of its binding to full-length HIV-1 RT, no HIV-1 RT peptide, MHC class I protein that does not bind to the peptide, and / or MHC class I protein that binds to non-HIV-1 RT peptide_d Of no more than about 1/10 (such as no more than about 1/10, 1/20, 1/30, 1/40, 1/50, 1/75, 1/100, 1/200, 1/300, 1 / 400, 1/500, 1/750, 1/1000 or less than 1/1000) times. In some embodiments, the anti-RTMC antibody portion (or anti-RTMC construct comprising the anti-RTMC antibody portion) is_d Bound to a complex containing HIV-1 RT peptide and MHC class I protein, the K_d Between about 0.1 pM to about 500 nM (such as any of about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM, 50 nM, 100 nM, or 500 nM , Including any range between these values). In some embodiments, the anti-RTMC antibody portion (or anti-RTMC construct comprising the anti-RTMC antibody portion) is_d Bound to a complex containing HIV-1 RT peptide and MHC class I protein, the K_d Between about 1 pM to about 250 pM (such as any of about 1, 10, 25, 50, 75, 100, 150, 200, or 250 pM, including any range between these values). In some embodiments, the anti-RTMC antibody portion (or anti-RTMC construct comprising the anti-RTMC antibody portion) is_d Bound to a complex containing HIV-1 RT peptide and MHC class I protein, the K_d Between about 1 nM and about 500 nM (such as any of about 1, 10, 25, 50, 75, 100, 150, 200, 250, 300, 350, 400, 450, or 500 nM, inclusive Any range between values). In some embodiments, the anti-RTMC antibody portion specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody portion is altered from the dual gene comprising HIV-1 RT peptide and MHC class I protein At least one compound of the body cross-reacts. In some embodiments, the dual gene variant has at most about 10 (such as about any of 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 when compared to MHC class I protein The) amino acid substitution. In some embodiments, the dual gene variant is the same serotype as the MHC class I protein. In some embodiments, the dual gene variant is a serotype different from the MHC class I protein. In some embodiments, the anti-RTMC antibody portion does not cross-react with any complexes that include the HIV-1 RT peptide and the dual gene variant of the MHC class I protein. In some embodiments, the anti-RTMC antibody portion cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, the anti-RTMC antibody portion specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody portion comprises MHC class I protein and has an amino acid substitution (such as conservative At least one complex of a variant of the HIV-1 RT peptide that is substituted by an amino acid). In some embodiments, the anti-RTMC antibody portion does not cross-react with any complexes comprising variants of MHC class I protein and HIV-1 RT peptide. For example, in some embodiments, the anti-RTMC antibody portion specifically binds to an amino acid sequence comprising HIV-1 RT peptide (including any of SEQ ID NO: 5-9 (SEQ ID NO: 5) (Such as consisting of)) and a complex of MHC class I proteins (such as HLA-A02, for example HLA-A * 02: 01), wherein the anti-RTMC antibody portion further binds to at least one of the following (including at least about 2 , Any of 3, 4 or 5): containing alanine substituted SEQ ID NO: 10 HIV-1 RT peptide and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) Complex; a complex containing alanine substituted HIV-1 RT peptide of SEQ ID NO: 11 and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); a complex containing SEQ ID NO: 12 Complex of acid-substituted HIV-1 RT peptide and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01); comprising alanine substituted HIV-1 RT peptide of SEQ ID NO: 13 and MHC class I Complexes of proteins (such as HLA-A02, such as HLA-A * 02: 01); and alanine-substituted HIV-1 RT peptides of SEQ ID NO: 15 and MHC class I proteins (such as HLA-A02, such as HLA-A02 A * 02: 01). In some embodiments, the antibody portion of anti-RTMC specifically binds to: an HIV-1 RT peptide comprising an amino acid sequence containing any of SEQ ID NOs: 5-9 and an MHC class I protein (such as HLA- A02, for example the complex of HLA-A * 02: 01); comprising the alanine substituted HIV-1 RT peptide of SEQ ID NO: 10 and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01) Complex; and a complex comprising alanine substituted HIV-1 RT peptide of SEQ ID NO: 11 and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: an HIV-1 RT peptide comprising an amino acid sequence containing any of SEQ ID NO: 6-9 and an MHC class I protein (such as HLA-A02 , For example, a complex of HLA-A * 02: 01); containing alanine-substituted HIV-1 RT peptide of SEQ ID NO: 10 and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) Complex; and a complex comprising alanine substituted HIV-1 RT peptide of SEQ ID NO: 12 and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: an HIV-1 RT peptide comprising an amino acid sequence containing any of SEQ ID NOs: 5-9 and an MHC class I protein (such as HLA-A02 , For example, a complex of HLA-A * 02: 01); containing alanine-substituted HIV-1 RT peptide of SEQ ID NO: 10 and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) Complex; a complex comprising alanine substituted HIV-1 RT peptide of SEQ ID NO: 11 and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); and a complex comprising SEQ ID NO: 13 Alanine replaces the complex of HIV-1 RT peptide and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: an HIV-1 RT peptide comprising an amino acid sequence containing any of SEQ ID NOs: 5-9 and an MHC class I protein (such as HLA-A02 , For example, a complex of HLA-A * 02: 01); containing alanine-substituted HIV-1 RT peptide of SEQ ID NO: 10 and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) Complex; a complex containing alanine substituted HIV-1 RT peptide of SEQ ID NO: 11 and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); a complex containing SEQ ID NO: 12 Complex of acid-substituted HIV-1 RT peptide and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); and alanine-substituted HIV-1 RT peptide and MHC I comprising SEQ ID NO: 13 A complex of protein-like proteins such as HLA-A02, for example HLA-A * 02: 01. In some embodiments, the anti-RTMC antibody portion specifically binds to: an HIV-1 RT peptide comprising the amino acid sequence SEQ ID NO: 6 or 7 and an MHC class I protein (such as HLA-A02, such as HLA-A * 02:01); a complex comprising the alanine substituted HIV-1 RT peptide of SEQ ID NO: 11 and an MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01); comprising SEQ ID NO: 12 Alanine substituted HIV-1 RT peptide and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) complex; including SEQ ID NO: 13 Alanine substituted HIV-1 RT A complex of peptides and MHC class I proteins (such as HLA-A02, such as HLA-A * 02: 01); and alanine substituted HIV-1 RT peptides including SEQ ID NO: 15 and MHC class I proteins (such as HLA- A02, for example the complex of HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: an HIV-1 RT peptide comprising an amino acid sequence containing any of SEQ ID NOs: 5-9 and an MHC class I protein (such as HLA-A02 , For example, a complex of HLA-A * 02: 01); containing alanine-substituted HIV-1 RT peptide of SEQ ID NO: 10 and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) Complex; a complex containing alanine substituted HIV-1 RT peptide of SEQ ID NO: 11 and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); a complex containing SEQ ID NO: 12 Complex of acid-substituted HIV-1 RT peptide and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01); comprising alanine substituted HIV-1 RT peptide of SEQ ID NO: 13 and MHC class I Complexes of proteins (such as HLA-A02, such as HLA-A * 02: 01); and alanine-substituted HIV-1 RT peptides of SEQ ID NO: 15 and MHC class I proteins (such as HLA-A02, such as HLA-A02 A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to a complex comprising an HIV-1 RT peptide containing the amino acid sequence of any of SEQ ID NOs: 5-9 and HLA-A * 02: 01 , Where the anti-RTMC antibody portion cross-reacts with at least one of the following (including at least about 2, 3, 4, 5, or 6): comprising HIV-1 RT peptide and HLA-A * 02: 02 ( GenBank deposit number: AFL91480) complex, including HIV-1 RT peptide and HLA-A * 02: 03 (GenBank deposit number: AAA03604) complex, including HIV-1 RT peptide and HLA-A * 02: 05 ( GenBank deposit number: AAA03603) complex, including HIV-1 RT peptide and HLA-A * 02: 06 (GenBank deposit number: CCB78868) complex, including HIV-1 RT peptide and HLA-A * 02: 07 ( GenBank deposit number: ACR55712) complex, and a complex containing HIV-1 RT peptide and -A * 02: 11 (GenBank deposit number: CAB56609). In some embodiments, the anti-RTMC antibody portion specifically binds to one or more of the following: comprising HIV-1 RT 181 (SEQ ID NO: 5) and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) complex; comprising HIV-1 RT 181 variant with amino acid sequence YQYVDDLYV (SEQ ID NO: 6) and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01 ); A complex containing an HIV-1 RT 181 variant with the amino acid sequence YQYIDDLYV (SEQ ID NO: 7) and a MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) ; A complex comprising an HIV-1 RT 181 variant having the amino acid sequence CQYMDDLYV (SEQ ID NO: 8) and a MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01); and comprising A complex of the HIV-1 RT 181 variant of the amino acid sequence CQYVDDLYV (SEQ ID NO: 9) and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: a complex comprising HIV-1 RT peptide of SEQ ID NO: 5 and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01) ; A complex comprising an HIV-1 RT 181 variant with the amino acid sequence YQYVDDLYV (SEQ ID NO: 6) and a MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); and comprising A complex of the HIV-1 RT 181 variant of the amino acid sequence YQYIDDLYV (SEQ ID NO: 7) and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: a complex comprising HIV-1 RT peptide of SEQ ID NO: 5 and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01) ; A complex comprising an HIV-1 RT 181 variant with the amino acid sequence YQYVDDLYV (SEQ ID NO: 6) and an MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); containing a complex with an amine Complex of HIV-1 RT 181 variant of amino acid sequence YQYIDDLYV (SEQ ID NO: 7) and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01); contains CQYMDDLYV with amino acid sequence (SEQ ID NO: 8) A complex of HIV-1 RT 181 variant and MHC class I protein (such as HLA-A02, for example HLA-A * 02: 01); and comprising CQYVDDLYV (SEQ ID NO: 9) A complex of HIV-1 RT 181 variant and MHC class I protein (such as HLA-A02, eg HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: comprises an HIV-1 RT 181 variant having the amino acid sequence YQYVDDLYV (SEQ ID NO: 6) and an MHC class I protein (such as HLA-A02, such as HLA -A * 02: 01) complex; comprising HIV-1 RT 181 variant with amino acid sequence YQYIDDLYV (SEQ ID NO: 7) and MHC class I protein (such as HLA-A02, for example HLA-A * 02 : 01); containing HIV-1 RT 181 variant with amino acid sequence CQYMDDLYV (SEQ ID NO: 8) and MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01) Complex; and a complex comprising an HIV-1 RT 181 variant having the amino acid sequence CQYVDDLYV (SEQ ID NO: 9) and a MHC class I protein (such as HLA-A02, such as HLA-A * 02: 01). In some embodiments, the anti-RTMC antibody portion specifically binds to: comprises an HIV-1 RT 181 variant having the amino acid sequence YQYVDDLYV (SEQ ID NO: 6) and an MHC class I protein (such as HLA-A02, such as HLA -A * 02: 01); and contains HIV-1 RT 181 variant with amino acid sequence YQYIDDLYV (SEQ ID NO: 7) and MHC class I protein (such as HLA-A02, such as HLA-A * 02:01). In some embodiments, the anti-RTMC antibody portion is a semi-synthetic antibody portion comprising fully human sequences and one or more synthetic regions. In some embodiments, the anti-RTMC antibody portion is a semi-synthetic antibody portion comprising a fully human light chain variable domain and a semi-synthetic heavy chain variable domain, the semi-synthetic heavy chain variable domain comprising fully human FR1, HC-CDR1 FR2, HC-CDR2, FR3 and FR4 regions and synthetic HC-CDR3. In some embodiments, the semi-synthetic heavy chain variable domain comprises a fully synthetic HC-CDR3 having a length of about 5 to about 25 (such as about 5, 6, 7, 8, 9, 10, 11, 12, 13, Any of 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25) amino acid sequences. In some embodiments, the semi-synthetic heavy chain variable domain or synthetic HC-CDR3 is obtained from a semi-synthetic library (such as a semi-synthetic human library), which comprises a length of about 5 to about 25 (such as about 5, 6, 7, (8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25) total synthesis of amino acid sequences HC-CDR3, where each amino acid in the sequence is randomly selected from standard human amino acids, minus cysteine. In some embodiments, the length of the synthetic HC-CDR3 is about 7 to about 15 (such as about any of 7, 8, 9, 10, 11, 12, 13, 14, or 15) amino acids. In some embodiments, the anti-RTMC antibody portion comprises a specific sequence or certain variants of such sequences. In some embodiments, amino acid substitution in the variant sequence does not substantially reduce the ability of the anti-RTMC antibody portion to bind to RTMC. For example, changes can be made that do not substantially reduce RTMC binding affinity. It also covers changes that substantially improve RTMC binding affinity or affect some other characteristics, such as specificity and / or cross-reactivity with related variants of RTMC. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or at most about 3 (eg, any of about 1, 2, or 3) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: including any of SEQ ID NO: 250-253 LC-CDR3 of the amino acid sequence of the amino acid sequence, or a variant thereof containing up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) light A chain variable domain comprising: LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240 or comprising up to about 3 (eg, about 1, 2 or Any one of 3) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 241-244, or up to about 3 (eg, about 1, Any one of 2 or 3) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246, or comprising up to about 3 (eg Any one of about 1, 2 or 3) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: an amino acid comprising any of SEQ ID NO: 247-249 LC-CDR1 of the sequence, or variants containing up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions, and any of SEQ ID NO: 250-253 The LC-CDR3 of the amino acid sequence, or a variant thereof containing up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240, or up to about 3 (eg, about 1, 2 Or any of 3) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any of SEQ ID NO: 241-244, or up to about 3 (eg, about 1 , Any of 2 or 3) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246; and ii) light chain variable Domain, comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 247-249, or comprising up to about 3 (eg, any of about 1, 2 or 3) amino groups Acid-substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240, comprising any of SEQ ID NO: 241-244 HC-CDR2 of the amino acid sequence of the above, and HC-CDR3 comprising the amino acid sequence of any of SEQ ID NO: 245-246; or up to about 3 (such as about Any one of 1, 2 or 3) an amino acid substituted variant thereof; and ii) a light chain variable domain comprising: an amino acid sequence comprising any one of SEQ ID NO: 247-249 LC-CDR1, and LC-CDR3 containing the amino acid sequence of any one of SEQ ID NO: 250-253; or the LC-CDR sequence contains up to about 3 (such as about 1, 2 or 3 Either) Amino acid substituted variants thereof. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240, comprising any of SEQ ID NO: 241-244 HC-CDR2 of the amino acid sequence of the above, and HC-CDR3 comprising the amino acid sequence of any of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: comprising SEQ ID NO: LC-CDR1 of the amino acid sequence of any one of 247-249, and LC-CDR3 including the amino acid sequence of any one of SEQ ID NO: 250-253. The sequences of the CDRs mentioned herein are provided in Table 2 below.table 2 In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163, or at most about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: including SEQ ID NO: 208-239 LC-CDR3 of the amino acid sequence of any of them, or a variant thereof containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising HC-CDR3 containing the amino acid sequence of any one of SEQ ID NOs: 125-163; and ii) a light chain A variable domain comprising LC-CDR3 containing the amino acid sequence of any one of SEQ ID NO: 208-239. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96, or at most about Variants of 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including the HC- of the amino acid sequence of any of SEQ ID NO: 97-124 CDR2, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, and any of SEQ ID NOs: 125-163 HC-CDR3 of the amino acid sequence, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions; and ii) light chain variable domains Which comprises: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189, or up to about 5 (such as about any of 1, 2, 3, 4 or 5 ) Amino acid substituted variants thereof, including the LC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 190-207, or up to about 3 (such as about any of 1, 2, or 3) One) Amino acid substituted variants thereof, and amino acid sequences comprising any of SEQ ID NO: 208-239 LC-CDR3, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96, or at most about Variants of 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including the HC- of the amino acid sequence of any of SEQ ID NO: 97-124 CDR2, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, and any of SEQ ID NOs: 125-163 HC-CDR3 of the amino acid sequence; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189, or up to about 5 (Such as any of about 1, 2, 3, 4, or 5) amino acid substituted variants thereof, including LC-CDR2 of the amino acid sequence of any of SEQ ID NO: 190-207, Or a variant comprising up to about 3 (such as about any of 1, 2, or 3) amino acid substitutions, and an LC comprising the amino acid sequence of any one of SEQ ID NO: 208-239 -CDR3. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising SEQ ID NO: HC-CDR2 of the amino acid sequence of any one of 97-124; and HC-CDR3 containing the amino acid sequence of any one of SEQ ID NO: 125-163; or in the HC-CDR sequence Contains up to about 5 (such as about any of 1, 2, 3, 4 or 5) amino acid substituted variants thereof; and ii) a light chain variable domain sequence comprising: comprising SEQ ID NO : LC-CDR1 of the amino acid sequence of any one of 164-189; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and comprising SEQ ID NO: 208- LC-CDR3 of the amino acid sequence of any of 239; or containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence Its variant. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising SEQ ID NO: HC-CDR2 of the amino acid sequence of any one of 97-124; and HC-CDR3 containing the amino acid sequence of any one of SEQ ID NO: 125-163; or containing up to about 5 (Such as any of about 1, 2, 3, 4, or 5) variants of amino acid substitutions, wherein the amino acid substitutions are in HC-CDR1 or HC-CDR2; and ii) the light chain variable domain Sequence comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189; LC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 190-207 ; And LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 208-239; or comprising up to about 5 (such as about any of 1, 2, 3, 4, or 5) amines; A variant of the amino acid substitution, in which the amino acid substitution is in HC-CDR1 or HC-CDR2. In some embodiments, the anti-RTMC antibody portion comprises: i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising SEQ ID NO: HC-CDR2 of the amino acid sequence of any one of 97-124; and HC-CDR3 including the amino acid sequence of any one of SEQ ID NO: 125-163; and ii) the light chain may Variable domain sequence comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189; LC comprising the amino acid sequence of any one of SEQ ID NO: 190-207 -CDR2; and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 208-239. The sequences of HC-CDRs from putative anti-RTMC antibody pure lines are provided in Table 3 below, and the sequences of LC-CDRs from these pure lines are provided in Table 4 below.table 3 table 4 In some embodiments, the anti-RTMC antibody portion comprises: a heavy chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 19-46, or has at least about 95% (including, for example, at least about 96% , 97%, 98%, or 99%) variants of sequence identity, and the light chain variable domain comprising the amino acid sequence of any one of SEQ ID NO: 47-74, or Variants thereof having at least about 95% (including, for example, at least about 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, the anti-RTMC antibody portion comprises: a heavy chain variable domain comprising the amino acid sequence of any one of SEQ ID NO: 19-46 and any one of SEQ ID NO: 47-74 The light chain variable domain of the amino acid sequence. The heavy and light chain variable domains can be combined in various pairs to generate multiple anti-RTMC antibody portions. For example, in some embodiments, the anti-RTMC antibody portion includes heavy and light chain variable domains that include HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1 , LC-CDR2 and LC-CDR3, which contain the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, respectively And 209, SEQ ID NO: 77, 99, 127, 164, 192, and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193, and 211, SEQ ID NO: 79, 101, 129, respectively , 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80 , 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218 , Respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ I D NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222 , Respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178 , 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116 , 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO : 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 And 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238; Or SEQ ID NOs: 96, 124, 163, 189, 207, and 239, respectively; or individually contain up to about 5 in HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, and / or LC-CDR3 (E.g., any of about 1, 2, 3, 4, or 5) amino acid substitution and / or include up to about 3 (e.g., about any of 1, 2, or 3) amines in the LC-CDR2 Variants of the base acid substitution. For example, in some embodiments, the heavy chain comprises: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 75, HC-CDR2 comprising the amino acid sequence SEQ ID NO: 97, and comprising the amino acid sequence HC-CDR3 of SEQ ID NO 125, and the light chain comprises: LC-CDR1 comprising the amino acid sequence SEQ ID NO: 164, LC-CDR2 comprising the amino acid sequence SEQ ID NO: 190, and comprising the amino acid sequence LC-CDR3 of SEQ ID NO: 208. In some embodiments, the anti-RTMC antibody portion includes heavy chain and light chain variable domains that include HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 And LC-CDR3, which contains the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 And 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132 , 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83 , 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, SEQ ID NO: 81, 117, 148, 169, 191, and 218, SEQ ID NO: 82, 118, 149, 180, 199, and 228, respectively, SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 18 5, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively, SEQ ID NO: 95, 123, 162, 188, 200 and 238, or SEQ respectively ID NO: 96, 124, 163, 189, 207, and 239; or include up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the HC-CDR sequence and And / or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence. In some embodiments, the anti-RTMC antibody portion includes heavy chain and light chain variable domains that include HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 And LC-CDR3, which contains the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 And 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132 , 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83 , 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102 , 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO : 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 And 227, SEQ ID NO: 81, 117, 148, 169, 191, and 218, SEQ ID NO: 82, 118, 149, 180, 199, and 228, respectively, SEQ ID NO: 82, 114, 150 , 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80 , 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 1 85, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238; or SEQ respectively ID NO: 96, 124, 163, 189, 207 and 239. In some embodiments, the anti-RTMC antibody portion comprises: heavy chain and light chain variable domains, the heavy chain and light chain variable domains comprising the following amino acid sequences: SEQ ID NO: 19 and 47, respectively, respectively SEQ ID NO: 20 and 48, respectively SEQ ID NO: 21 and 49, respectively SEQ ID NO: 22 and 50, respectively SEQ ID NO: 23 and 51, respectively SEQ ID NO: 24 and 52, respectively SEQ ID NO: 25 and 53, SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, SEQ ID NO: 28 and 56 respectively, SEQ ID NO: 29 and 57 respectively SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, respectively SEQ ID NO: 35 and 63, respectively SEQ ID NO: 36 and 64, respectively SEQ ID NO: 37 and 65, respectively SEQ ID NO: 38 and 66, respectively SEQ ID NO: 39 and 67, respectively SEQ ID NO: 40 and 68, respectively SEQ ID NO: 41 and 69, respectively SEQ ID NO: 42 and 70, respectively SEQ ID NO: 43 and 71, respectively SEQ ID NO: 44 and 72, respectively SEQ ID NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively; or individually have Variants of at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, the anti-RTMC antibody portion includes heavy and light chain variable domains that include the following amino acid sequences: SEQ ID NOs: 19 and 47, and SEQ, respectively ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, SEQ ID NO: 23 and 51, SEQ ID NO: 24 and 52, SEQ, respectively ID NO: 25 and 53, respectively SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, respectively SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, SEQ respectively ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID NO: 38 and 66, SEQ ID NO: 39 and 67, SEQ, respectively ID NO: 40 and 68, respectively SEQ ID NO: 41 and 69, respectively SEQ ID NO: 42 and 70, respectively SEQ ID NO: 43 and 71, respectively SEQ ID NO: 44 and 72, respectively SEQ ID NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively. The sequences of the heavy chain variable domain and light chain variable domain from the putative anti-RTMC antibody pure line are provided in Table 5 below.table 5 In some embodiments, the anti-RTMC antibody portion comprises heavy and light chain variable domains comprising amino acid sequences SEQ ID NOs: 27 and 55, or individually has at least about 95% (eg, at least about 96%, 97 %, 98% or 99%) variants of sequence identity. In some embodiments, the anti-RTMC antibody portion comprises heavy and light chain variable domains, which comprise the amino acid sequences SEQ ID NO: 27 and 55, respectively. In some embodiments, the anti-RTMC antibody portion comprises heavy and light chain variable domains comprising amino acid sequences SEQ ID NOs: 30 and 58, respectively, or individually has at least about 95% (eg, at least about 96%, 97 %, 98% or 99%) variants of sequence identity. In some embodiments, the anti-RTMC antibody portion comprises heavy and light chain variable domains, which comprise the amino acid sequences SEQ ID NO: 30 and 58, respectively. In some embodiments, the anti-RTMC antibody portion competes with the second anti-RTMC antibody portion according to any of the anti-RTMC antibody portions described herein to bind to the target HIV-1 RT / MHC class I complex. In some embodiments, the anti-RTMC antibody portion and the second anti-RTMC antibody portion bind to the same, or substantially the same epitope. In some embodiments, the binding of the anti-RTMC antibody portion to the target HIV-1 RT / MHC class I complex inhibits the binding of the second anti-RTMC antibody portion to the target HIV-1 RT / MHC class I complex by at least about 70% (such as at least about any of 75%, 80%, 85%, 90%, 95%, 98%, or 99%), or vice versa. In some embodiments, the anti-RTMC antibody portion and the second anti-RTMC antibody portion cross-compete to bind to the target HIV-1 RT / MHC class I complex, that is, each of these antibody portions competes with each other for binding to the target Target HIV-1 RT / MHC class I complex. For example, in some embodiments, an anti-RTMC antibody portion competes with an antibody portion comprising the following for binding to a target HIV-1 RT / MHC class I complex: i) a heavy chain variable domain sequence comprising: comprising an amine HC-CDR1 of the acid sequence SEQ ID NO: 240, or a variant thereof containing up to about 3 (eg, any of about 1, 2 or 3) amino acid substitutions, including SEQ ID NO: 241-244 HC-CDR2 of the amino acid sequence of any of them, or a variant thereof containing up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions, and comprising SEQ ID NO: HC-CDR3 of the amino acid sequence of any one of 245-246; or a variant thereof comprising at most about 3 (eg, about any of 1, 2, or 3) amino acid substitutions; and ii) Light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 247-249, or up to about 3 (eg, any of about 1, 2 or 3 The variant of the amino acid substitution, and the LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 250-253, or up to about 3 (eg, about 1, 2 or 3) Either) Amino acid substituted variants thereof. In some embodiments, the anti-RTMC antibody portion competes with an antibody portion comprising the following for binding to the target HIV-1 RT / MHC class I complex: i) heavy chain variable domain sequence comprising: comprising SEQ ID NO: 75 -The HC-CDR1 of the amino acid sequence of (and consisting of, in some embodiments) of any of 96; or up to about 5 (eg, about any of 1, 2, 3, 4, or 5 ) -Amino acid substituted variants thereof; HC-CDR2 comprising the amino acid sequence of any of SEQ ID NOs: 97-124 (and consisting of it in some embodiments); or comprising up to about 5 (Eg, about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and the amino acid sequence comprising any of SEQ ID NO: 125-163 (and in HC-CDR3 in some embodiments); or variants containing up to about 5 (eg, any of about 1, 2, 3, 4, or 5) amino acid substitutions; and ii) light Chain variable domain sequence comprising: LC-CDR1 comprising the amino acid sequence of any of SEQ ID NO: 164-189 (and consisting of it in some embodiments); or comprising up to about 5 ( (E.g. about any of 1, 2, 3, 4 or 5) amino acid substitution Variants thereof; LC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 190-207 (and consisting of it in some embodiments); or comprising up to about 3 (eg about 1, 2 or 3) an amino acid substituted variant thereof; and an LC comprising the amino acid sequence of any one of SEQ ID NO: 208-239 (and consisting of it in some embodiments) -CDR3; or a variant comprising up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions. In some embodiments, the anti-RTMC antibody portion competes with an antibody portion comprising the following for binding to the target HIV-1 RT / MHC class I complex: i) heavy chain variable domain sequence comprising: comprising SEQ ID NO: 75 -HC-CDR1 of the amino acid sequence of any of (and consisting of in some embodiments); comprising the amino acid sequence of any of SEQ ID NO: 97-124 (and in some HC-CDR2; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163 (and in some embodiments); or in HC -Up to about 5 (e.g., about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof are included in the CDR sequence; and ii) light chain variable domain sequence comprising: comprising LC-CDR1 of the amino acid sequence of any of SEQ ID NO: 164-189 (and consisting of it in some embodiments); comprising the amino acid of any of SEQ ID NO: 190-207 LC-CDR2 of the sequence (and consisting of it in some embodiments); and LC- comprising the amino acid sequence of any of SEQ ID NO: 208-239 (and consisting of it in some embodiments) CDR3; or include at most in the LC-CDR sequence There are about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof. In some embodiments, the anti-RTMC antibody portion competes with an antibody portion comprising the following for binding to the target HIV-1 RT / MHC class I complex: comprising the amino acid sequence of any one of SEQ ID NO: 19-46 (And in some embodiments thereof) a heavy chain variable domain, or one having at least about 95% (e.g., at least about any of 96%, 97%, 98%, or 99%) sequence identity Variants, and a light chain variable domain comprising the amino acid sequence of any of SEQ ID NOs: 47-74 (and consisting of it in some embodiments), or having at least about 95% (eg, at least about 96%, 97%, 98% or 99%) variants of sequence identity. In some embodiments, the anti-RTMC antibody portion competes with an antibody portion comprising heavy and light chain variable domains for binding to a target HIV-1 RT / MHC class I complex, the heavy and light chain variable domains comprising HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3, which include the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191 and 209 respectively, SEQ ID NO: 77, 99, 127, 164, 192 and 210 respectively, SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, SEQ ID NO: 88, 113, 144, 178, 201, and 224, respectively, SEQ ID NO: 82, 114, 145, 179, 202, and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively, SEQ ID NO: 80, 102 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200, and 238, or SEQ ID NO: 96, 124, 163, 189, 207, and 239, respectively; or individually in HC-CDR1, HC-CDR2, HC-CDR3 , LC-CDR1 and / or LC-CDR3 contain up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions and / or up to about 3 in LC-CDR2 (Eg, about any of 1, 2, or 3) amino acid substituted variants thereof. In some embodiments, the anti-RTMC antibody portion competes with an antibody portion comprising heavy and light chain variable domains for binding to a target HIV-1 RT / MHC class I complex, the heavy and light chain variable domains comprising HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3, which include the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191 and 209 respectively, SEQ ID NO: 77, 99, 127, 164, 192 and 210 respectively, SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, SEQ ID NO: 88, 113, 144, 178, 201, and 224, respectively, SEQ ID NO: 82, 114, 145, 179, 202, and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively, SEQ ID NO: 80, 102 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200, and 238, or SEQ ID NO: 96, 124, 163, 189, 207, and 239, respectively, or up to about 5 (such as about Any of 1, 2, 3, 4 or 5) amino acid substitutions and / or up to about 5 (such as about any of 1, 2, 3, 4 or 5 in the LC-CDR sequence ) Amino acid substituted variants thereof. In some embodiments, the anti-RTMC antibody portion competes with an antibody portion comprising heavy and light chain variable domains for binding to a target HIV-1 RT / MHC class I complex, the heavy and light chain variable domains comprising HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3, which include the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191 and 209 respectively, SEQ ID NO: 77, 99, 127, 164, 192 and 210 respectively, SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, SEQ ID NO: 88, 113, 144, 178, 201, and 224, respectively, SEQ ID NO: 82, 114, 145, 179, 202, and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively, SEQ ID NO: 80, 102 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200, and 238, or SEQ ID NO: 96, 124, 163, 189, 207, and 239, respectively. In some embodiments, the anti-RTMC antibody portion comprises at least about 95% (e.g., at least about any of 96%, 97%, 98%, or 99%) sequence of heavy chain and light chain variable domains or individually Consistently, the antibody portion of its variant competes for binding to the target HIV-1 RT / MHC class I complex. The heavy and light chain variable domains contain the following amino acid sequences: SEQ ID NO: 19 and 47, SEQ ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, SEQ ID NO: 23 and 51, SEQ ID NO: 24 and 47, respectively 52, SEQ ID NO: 25 and 53, respectively, SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, SEQ ID NO: 30 and 58, respectively, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and respectively 62, SEQ ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID NO: 38 and 66, SEQ ID NO: 39 and 62, respectively 67, SEQ ID NO: 40 and 68, respectively, SEQ ID NO: 41 and 69, respectively SEQ ID NO: 42 and 70, SEQ ID NO: 43 and 71, SEQ ID NO: 44 and 72, SEQ ID NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively . In some embodiments, the anti-RTMC antibody portion competes with an antibody portion comprising heavy and light chain variable domains for binding to a target HIV-1 RT / MHC class I complex, the heavy and light chain variable domains comprising The following amino acid sequences: SEQ ID NO: 19 and 47, SEQ ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, SEQ ID, respectively NO: 23 and 51, respectively SEQ ID NO: 24 and 52, respectively SEQ ID NO: 25 and 53, respectively SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, SEQ ID NO: 29 and 57, respectively SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59 respectively, SEQ ID NO: 32 and 60 respectively, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, SEQ ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID, respectively NO: 38 and 66, SEQ ID NO: 39 and 67, SEQ ID NO: 40 and 68, SEQ ID NO: 41 and 69, SEQ ID NO: 42 and 70, SEQ ID, respectively NO: 43 and 71, respectively SEQ ID NO: 44 and 72, respectively SEQ ID NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively.Full length anti RTMC antibody In some embodiments, the anti-RTMC construct is a full-length antibody comprising an anti-RTMC antibody portion (also referred to herein as "full-length anti-RTMC antibody"). In some embodiments, the full-length antibody is a monoclonal antibody. In some embodiments, the full-length anti-RTMC antibody comprises Fc sequences from immunoglobulins, such as IgA, IgD, IgE, IgG, and IgM. In some embodiments, the full-length anti-RTMC antibody comprises the Fc sequence of any of IgG (such as IgG1, IgG2, IgG3, or IgG4). In some embodiments, the full-length anti-RTMC antibody comprises the Fc sequence of human immunoglobulin. In some embodiments, the full-length anti-RTMC antibody comprises the Fc sequence of mouse immunoglobulin. In some embodiments, the full-length anti-RTMC antibody comprises an Fc sequence that has been altered or otherwise altered to have enhanced antibody-dependent cytotoxicity (ADCC) or complement-dependent cytotoxicity (CDC) effector functions. Thus, for example, in some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) Fc region. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) specific binding to HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9) peptide and HLA-A * 02 : The anti-RTMC antibody portion of the complex of 01, and b) the Fc region. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. In some embodiments, the anti-RTMC antibody portion and at least one variant (such as at least 2, 3) of a variant of HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC antibody portion cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the anti-RTMC antibody portion comprising: i ) Heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240, or comprising up to about 3 (eg, any of about 1, 2 or 3) amino acid substitutions Variants thereof, comprising HC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 241-244, or containing up to about 3 (eg, about any of 1, 2, or 3) amino groups Acid-substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg, any of about 1, 2 or 3 ) An amino acid substituted variant thereof; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 247-249, or up to about 3 (For example, about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any of SEQ ID NO: 250-253, or comprising Up to about 3 (e.g. about 1, 2 or 3 of One) amino acid substituted variants thereof; and b) Fc region. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the anti-RTMC antibody portion comprising: i ) Heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence SEQ ID NO: 240, HC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 241-244, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: an amine comprising any one of SEQ ID NO: 247-249 LC-CDR1 of the acid sequence, and LC-CDR3 including the amino acid sequence of any one of SEQ ID NO: 250-253; and b) Fc region. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the anti-RTMC antibody portion comprising: i ) A heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96, or up to about 5 (such as about 1, 2, 3, 4 or Any of 5) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any of SEQ ID NO: 97-124, or containing up to about 5 (such as about 1, (Any of 2, 3, 4 or 5) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 125-163, or comprising at most about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: comprising SEQ ID NO: 164-189 LC-CDR1 of the amino acid sequence of any of them, or a variant thereof containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including SEQ ID NO: LC-CDR2 of amino acid sequence of any one of 190-207, or package Up to about 3 (such as about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any of SEQ ID NO: 208-239 , Or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the anti-RTMC antibody portion comprising: i ) Heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising the amine group of any one of SEQ ID NO: 97-124 HC-CDR2 of the acid sequence; and HC-CDR3 including the amino acid sequence of any one of SEQ ID NO: 125-163 in the HC-CDR sequence; or up to about 5 (such as about 1, 2, Any of 3, 4 or 5) amino acid substituted variants thereof; and ii) light chain variable domain sequence comprising: an amino acid comprising any of SEQ ID NO: 164-189 LC-CDR1 of the sequence; LC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 190-207; and LC comprising the amino acid sequence of any one of SEQ ID NO: 208-239 -CDR3; or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence; and b) Fc region. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the anti-RTMC antibody portion comprising: i ) Heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising the amine group of any one of SEQ ID NO: 97-124 HC-CDR2 of the acid sequence; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163; and ii) a light chain variable domain sequence comprising: comprising SEQ ID NO: 164 -LC-CDR1 of the amino acid sequence of any one of 189; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and including SEQ ID NO: 208-239 LC-CDR3 of the amino acid sequence of any one; and b) Fc region. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the anti-RTMC antibody portion comprising: comprising The heavy chain variable domain of the amino acid sequence of any one of SEQ ID NO: 19-46, or has at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99% ) A variant of sequence identity, and a light chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 47-74, or having at least about 95% (including, for example, at least about 96%, 97 Any of%, 98%, or 99%) variants of sequence identity; and b) Fc region. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. In some embodiments, a full-length anti-RTMC antibody is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the anti-RTMC antibody portion comprising: comprising The heavy chain variable domain of the amino acid sequence of any one of SEQ ID NO: 19-46 and the light chain variable domain comprising the amino acid sequence of any one of SEQ ID NO: 47-74; and b) Fc region. In some embodiments, the Fc region comprises IgG1 Fc sequence. In some embodiments, the Fc region comprises human IgG1 Fc sequence. In some embodiments, the Fc region comprises mouse IgG1 Fc sequence. For example, in some embodiments, the full-length anti-RTMC antibody portion includes heavy and light chain variable domains that include HC-CDR1, HC-CDR2, HC-CDR3, LC- CDR1, LC-CDR2 and LC-CDR3, which include the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191 and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, SEQ ID NO: 85, 108, 137, 169, 191 and SEQ respectively 218, SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, SEQ ID NO: 88, 113, 144, respectively 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, SEQ ID NO: 80, 102, 153, 164, 192, and 232, SEQ ID NO: 93, 121, 154, 183, 204, and 233, respectively, SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO : 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, 173, 206, and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 And 238; or SEQ ID NO: 96, 124, 163, 189, 207 and 239, respectively; or individually included up to HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1 and / or LC-CDR3 About 5 (e.g., any of about 1, 2, 3, 4, or 5) amino acid substitutions and / or up to about 3 (e.g., about any of 1, 2, or 3) included in the LC-CDR2 The variant of amino acid substitution. In some embodiments, the full-length anti-RTMC antibody portion comprises heavy and light chain variable domains, and these heavy and light chain variable domains comprise HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC- CDR2 and LC-CDR3, which include the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, and 209, SEQ ID NO: 77, 99, 127, 164, 192 and 210 respectively, SEQ ID NO: 78, 100, 128, 166, 193 and 211 respectively, SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, SEQ ID NO: 82, 114, 145, 179, 202 and 225 respectively, SEQ ID NO: 89, 115, 146, 175, 200 and 226 respectively, SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 15 7, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238; or respectively SEQ ID NO: 96, 124, 163, 189, 207, and 239; or individually contain up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amines in the HC-CDR sequence Amino acid substitutions and / or variants containing up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence. In some embodiments, the full-length anti-RTMC antibody portion comprises heavy and light chain variable domains, and these heavy and light chain variable domains comprise HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC- CDR2 and LC-CDR3, which include the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, and 209, SEQ ID NO: 77, 99, 127, 164, 192 and 210 respectively, SEQ ID NO: 78, 100, 128, 166, 193 and 211 respectively, SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80 , 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224 , SEQ ID NO: 82, 114, 145, 179, 202, and 225, respectively, SEQ ID NO: 89, 115, 146, 175, 200, and 226, respectively SEQ ID NO: 90, 116, 147, 169 , 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114 , 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO : 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 1 57, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238; or respectively SEQ ID NO: 96, 124, 163, 189, 207 and 239. In some embodiments, the full-length anti-RTMC antibody portion comprises: heavy chain and light chain variable domains, the heavy chain and light chain variable domains comprising the following amino acid sequences: SEQ ID NOs: 19 and 47, respectively, SEQ ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, SEQ ID NO: 23 and 51, SEQ ID NO: 24 and 52, respectively, SEQ ID NO: 25 and 53, SEQ ID NO: 26 and 54 respectively, SEQ ID NO: 27 and 55 respectively, SEQ ID NO: 28 and 56 respectively, SEQ ID NO: 29 and 57 respectively SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, respectively, SEQ ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID NO: 38 and 66, SEQ ID NO: 39 and 67, respectively, SEQ ID NO: 40 and 68, SEQ ID NO: 41 and 69, SEQ ID NO: 42 and 70, SEQ ID NO: 43 and 71, SEQ ID NO: 44 and 72, respectively, SEQ ID NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively; or individually Variants thereof having at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, the full-length anti-RTMC antibody portion comprises heavy and light chain variable domains, and these heavy and light chain variable domains comprise the following amino acid sequences: SEQ ID NOs: 19 and 47, respectively, respectively SEQ ID NO: 20 and 48, respectively SEQ ID NO: 21 and 49, respectively SEQ ID NO: 22 and 50, respectively SEQ ID NO: 23 and 51, respectively SEQ ID NO: 24 and 52, respectively SEQ ID NO: 25 and 53, SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, SEQ ID NO: 28 and 56 respectively, SEQ ID NO: 29 and 57 respectively SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, respectively SEQ ID NO: 35 and 63, respectively SEQ ID NO: 36 and 64, respectively SEQ ID NO: 37 and 65, respectively SEQ ID NO: 38 and 66, respectively SEQ ID NO: 39 and 67, respectively SEQ ID NO: 40 and 68, respectively SEQ ID NO: 41 and 69, respectively SEQ ID NO: 42 and 70, respectively SEQ ID NO: 43 and 71, respectively SEQ ID NO: 44 and 72, respectively SEQ ID NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively. In some embodiments, the full-length anti-RTMC antibody portion comprises heavy and light chain variable domains comprising amino acid sequences SEQ ID NOs: 27 and 55, or individually has at least about 95% (eg, at least about 96%, Any of 97%, 98%, or 99%) variants of sequence identity. In some embodiments, the full-length anti-RTMC antibody portion comprises heavy and light chain variable domains, which comprise the amino acid sequences SEQ ID NO: 27 and 55, respectively. In some embodiments, the full-length anti-RTMC antibody portion comprises heavy and light chain variable domains comprising amino acid sequences SEQ ID NO: 30 and 58, respectively, or individually has at least about 95% (eg, at least about 96%, Any of 97%, 98%, or 99%) variants of sequence identity. In some embodiments, the full-length anti-RTMC antibody portion comprises heavy and light chain variable domains, which comprise the amino acid sequences SEQ ID NO: 30 and 58, respectively. In some embodiments, the full-length anti-RTMC antibody_d Bound to a complex containing HIV-1 RT peptide and MHC class I protein, the K_d Between about 0.1 pM to about 500 nM (such as any of about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM, 50 nM, 100 nM, or 500 nM , Including any range between these values). In some embodiments, the full-length anti-RTMC antibody_d Bound to a complex containing HIV-1 RT peptide and MHC class I protein, the K_d Between about 1 pM to about 250 pM (such as any of about 1, 10, 25, 50, 75, 100, 150, 200, or 250 pM, including any range between these values).Multispecific anti RTMC molecule In some embodiments, the anti-RTMC construct includes a multispecific anti-RTMC molecule that includes an anti-RTMC antibody portion and a second binding portion (such as a second antigen binding portion). In some embodiments, the multispecific anti-RTMC molecule includes an anti-RTMC antibody portion and a second antigen binding portion. Multispecific molecules are molecules that have binding specificities for at least two different antigens or epitopes (eg, bispecific antibodies have binding specificities for two antigens or epitopes). Multispecific molecules with more than two valencies and / or specificities are also covered. For example, trispecific antibodies can be prepared. Tutt et alJ . Immunol . 147: 60 (1991). It should be understood that those skilled in the art can select appropriate characteristics of the individual multispecific molecules described herein to combine with each other to form the multispecific anti-RTMC molecules of the present invention. Thus, for example, in some embodiments, a multispecific (e.g., bispecific) anti-RTMC molecule is provided, comprising: a) an antibody that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein RTMC antibody portion, and b) a second binding portion (such as an antigen binding portion). In some embodiments, the second binding moiety specifically binds to a complex comprising different HIV-1 RT peptides bound to MHC class I protein. In some embodiments, the second scFv specifically binds to a complex comprising HIV-1 RT peptides bound to different MHC class I proteins. In some embodiments, the second binding moiety specifically binds to different epitopes on a complex comprising HIV-1 RT peptide and MHC class I protein. In some embodiments, the second binding moiety specifically binds to different antigens. In some embodiments, the second binding moiety specifically binds to an antigen on the surface of cells (such as cytotoxic cells). In some embodiments, the second binding moiety specifically binds to an antigen on the surface of lymphocytes (such as T cells, NK cells, neutrophils, monocytes, macrophages, or dendritic cells). In some embodiments, the second binding moiety specifically binds to effector T cells, such as cytotoxic T cells (also known as cytotoxic T lymphocytes (CTL) or T killer cells). In some embodiments, a multispecific anti-RTMC molecule is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) specific binding The second antigen binding portion of CD3. In some embodiments, the second antigen-binding portion specifically binds to CD3ε. In some embodiments, the second antigen-binding portion specifically binds to the agonistic epitope of CD3ε. As used herein, the term "promoting epitope" means (a) after binding to a multispecific molecule, optionally allowing it to activate T after binding to a number of multispecific molecules on the same cell The epitope of cell receptor (TCR) signaling and inducing T cell activation, and / or (b) consists only of amino acid residues in the epsilon chain of CD3 and exists in its natural state on T cells (also That is, an epitope that can be bound by multispecific molecules when surrounded by TCR, CD3γ chain, and / or (c) an epitope that cannot stabilize the spatial position of CD3ε relative to CD3γ after binding the multispecific molecule. In some embodiments, a multispecific anti-RTMC molecule is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) specific binding In effector cells, this includes, for example, CD3γ, CD3δ, CD3ε, CD3ζ, CD28, CD16a, CD56, CD68 and the second antigen-binding portion of the antigen on the surface of GDS2D. In some embodiments, a multispecific anti-RTMC molecule is provided that includes a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) specifically binds to Components of the complement system, such as the second antigen-binding portion of Clq. C1q is the subunit of the C1 enzyme complex that activates the serum complement system. In some embodiments, the second antigen-binding portion specifically binds to Fc receptors. In some embodiments, the second antigen binding portion specifically binds to Fcγ receptor (FcγR). FcγR may be FcγRIII present on the surface of natural killer (NK) cells or FcγRI, FcγRIIA, FcγRIIBI, FcγRIIB2 and FcγRIIIB present on the surface of macrophages, monocytes, neutrophils and / or dendritic cells. The one. In some embodiments, the second antigen binding portion is an Fc region or a functional fragment thereof. "Functional fragment" as used in this context means still able to bind to FcR with sufficient specificity and affinity, especially to FcγR to allow FcγR carrying effector cells, specifically macrophages, monocytes, tropism Neutral leukocytes and / or dendritic cells kill fragments of the antibody Fc region of target cells by cytotoxin lysis or phagocytosis. Functional Fc fragments can competitively inhibit the binding of the initial, full-length Fc portion to FcR such as activated FcγRI. In some embodiments, the functional Fc fragment retains at least 30%, 40%, 50%, 60%, 70%, 80%, 90%, or 95% of its affinity for activated FcyR. In some embodiments, the Fc region or functional fragment thereof is an enhanced Fc region or functional fragment thereof. As used herein, the term "enhanced Fc region" refers to modified to enhance Fc receptor-mediated effector functions, specifically antibody-dependent cell-mediated cytotoxicity (ADCC), complement-dependent cytotoxicity (ADC CDC) and antibody-mediated bacteriophage Fc region. This can be achieved as known in the art, for example by causing increased affinity for activated receptors (such as FcγRIIIA (CD16A) expressed on natural killer (NK) cells) and / or with inhibitory receptors (such as FcγRIIB1 / B2 (CD32B)) The reduced binding modifies the Fc region. In still other embodiments, the second antigen-binding portion is an antibody or antigen-binding fragment thereof, which binds specifically to FcR with sufficient specificity and affinity, especially to FcγR to allow effector cells carrying FcγR, specifically Macrophages, monocytes, neutrophils and / or dendritic cells kill target cells by cytotoxic lysis or phagocytosis. In some embodiments, multispecific anti-RTMC molecules allow killing of RTMC presenting target cells and / or can effectively redirect CTL to lyse RTMC presenting target cells. In some embodiments, multispecific (eg, bispecific) anti-RTMC molecules of the invention display in vitro EC in the range of 10 to 500 ng / ml₅₀ And can induce about 50% of target cells to pass through CTL at a ratio of CTL to target cells of about 1: 1 to about 50: 1 (such as about 1: 1 to about 15: 1, or about 2: 1 to about 10: 1) It's redirected to crack. In some embodiments, multispecific (e.g., bispecific) anti-RTMC molecules are capable of cross-linking stimulated or unstimulated CTL and target cells, in such a way that the target cells are lysed. This provides the advantage that no target-specific T-cell pure lines are generated or that common antigen presentation by dendritic cells is not required to allow the multispecific anti-RTMC molecules to exert their desired activity. In some embodiments, the multispecific anti-RTMC molecules of the invention can redirect CTL to lyse target cells in the absence of other activation signals. In some embodiments, the second antigen binding portion of the multispecific anti-RTMC molecule specifically binds to CD3 (eg, specifically binds to CD3ε) and does not require C28 and / or IL-2 signaling to redirect CTL To lyse the target cells. It is within the normal ability of those skilled in the art to measure the preference of a multispecific anti-RTMC molecule to simultaneously bind to two antigens (eg, antigens on two different cells). For example, when the second binding moiety specifically binds to CD3, the multispecific anti-RTMC molecule can interact with CD3⁺ / HIV-1 RT^- Cells and CD3^- / HIV-1 RT⁺ Contact the mixture of cells. The number of multispecific anti-RTMC molecule positive single cells and the number of cells cross-linked by the multispecific anti-RTMC molecule can then be evaluated by microscopy or fluorescence activated cell sorting (FACS) known in the art . For example, in some embodiments, a multispecific anti-RTMC molecule is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b ) Second antigen binding portion. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, the second antigen-binding portion specifically binds to a complex comprising different HIV-1 RT peptides bound to MHC class I protein. In some embodiments, the second antigen-binding portion specifically binds to a complex comprising HIV-1 RT peptides bound to different MHC class I proteins. In some embodiments, the second antigen-binding portion specifically binds to different epitopes on a complex comprising HIV-1 RT peptide and MHC class I protein. In some embodiments, the second antigen binding portion specifically binds to another antigen. In some embodiments, the second antigen binding moiety specifically binds to cells, such as RTMC presenting antigen on the cell surface. In some embodiments, the second antigen-binding portion specifically binds to an antigen on the cell surface that does not express HIV-1 RT. In some embodiments, the second antigen-binding portion specifically binds to antigens on the surface of cytotoxic cells. In some embodiments, the second antigen binding moiety specifically binds to lymphocytes, such as antigens on the surface of T cells, NK cells, neutrophils, monocytes, macrophages, or dendritic cells. In some embodiments, the second antigen binding moiety specifically binds to effector T cells, such as antigens on the surface of cytotoxic T cells. In some embodiments, the second antigen binding moiety specifically binds to effector cells, including, for example, CD3γ, CD3δ, CD3ε, CD3ζ, CD28, CD16a, CD56, CD68, and antigens on the surface of GDS2D. In some embodiments, the anti-RTMC antibody portion is human, humanized, or semi-synthetic. In some embodiments, the second antigen binding portion is an antibody portion. In some embodiments, the second antigen-binding portion is a human, humanized, or semi-synthetic antibody portion. In some embodiments, the multispecific anti-RTMC molecule further comprises at least one (such as at least about any of 2, 3, 4, 5, or more) additional antigen binding moieties. In some embodiments, the anti-RTMC antibody portion and at least one variant (such as at least 2, 3) of a variant of HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC antibody portion cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, a multispecific anti-RTMC molecule is provided, which comprises a) an anti-RTMC antibody portion that specifically binds to a complex comprising: HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9) Peptide and HLA-A * 02: 01, and b) second antigen binding portion. In some embodiments, a multispecific anti-RTMC molecule is provided, comprising a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising: i) Heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, or comprising up to about 3 (eg, any of about 1, 2 or 3) amino acid substitutions Variants thereof, HC-CDR2 comprising the amino acid sequence of any one of SEQ ID NOs: 241-244, or up to about 3 (eg, about any one of 1, 2, or 3) amino groups Acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg, any of about 1, 2 or 3 ) An amino acid substituted variant thereof; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 247-249, or comprising up to about 3 (Eg, any of about 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253, or comprising Up to about 3 (e.g. about any of 1, 2, or 3 One) amino acid substituted variants, and b) a second antigen binding portion. In some embodiments, a multispecific anti-RTMC molecule is provided, comprising a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising: i) Heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, HC-CDR2 comprising the amino acid of any of SEQ ID NO: 241-244, and comprising HC-CDR3 of the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: comprising an amino group of any one of SEQ ID NO: 247-249 The LC-CDR1 of the acid sequence, and the LC-CDR3 including the amino acid sequence of any one of SEQ ID NOs: 250-253, and b) the second antigen binding portion. In some embodiments, a multispecific anti-RTMC molecule is provided, comprising a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising: i) Heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96, or up to about 5 (such as about 1, 2, 3, 4 or 5 Any one of them) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 97-124, or containing up to about 5 (such as about 1, 2 , Any of 3, 4 or 5) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163, or comprising up to about 5 (Such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: comprising SEQ ID NO: 164-189 LC-CDR1 of the amino acid sequence of any one, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including SEQ ID NO : LC-CDR2 of the amino acid sequence of any one of 190-207, or containing More than three (such as about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 208-239 , Or comprise up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and b) a second antigen binding moiety. In some embodiments, a multispecific anti-RTMC molecule is provided, comprising a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising i) heavy Chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising the amino acid sequence of any one of SEQ ID NO: 97-124 HC-CDR2; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163; or up to about 5 (such as about 1, 2, 3, Any one of 4 or 5) amino acid substituted variants thereof; and ii) a light chain variable domain sequence comprising: an amino acid sequence comprising any of SEQ ID NO: 164-189 LC-CDR1; LC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 190-207; and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 208-239 Or, in the LC-CDR sequence, up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and b) a second antigen binding portion. In some embodiments, a multispecific anti-RTMC molecule is provided, comprising a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising i) heavy Chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising the amino acid sequence of any one of SEQ ID NO: 97-124 HC-CDR2; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 125-163; and ii) a light chain variable domain sequence comprising: comprising SEQ ID NO: 164-189 LC-CDR1 of the amino acid sequence of any one of them; LC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 190-207; and any of SEQ ID NO: 208-239 LC-CDR3 of the amino acid sequence of one; and b) the second antigen binding portion. In some embodiments, a multispecific anti-RTMC molecule is provided that includes a) an anti-RTMC antibody portion that includes a heavy chain variable domain that includes the amine of any one of SEQ ID NOs: 19-46 Base acid sequence or a variant thereof having at least about 95% (e.g., at least about any of 96%, 97%, 98%, or 99%) sequence identity, and a light chain variable domain comprising SEQ ID NO : An amino acid sequence of any of 47-74 or a variant thereof having at least about 95% (including, for example, at least about 96%, 97%, 98%, or 99%) sequence identity; And b) a second scFv. In some embodiments, a multispecific anti-RTMC molecule is provided that includes a) an anti-RTMC antibody portion that includes a heavy chain variable domain containing the amino acid sequence of any one of SEQ ID NO: 19-46 , And a light chain variable domain comprising the amino acid sequence of any one of SEQ ID NO: 47-74; and b) a second antigen binding portion. In some embodiments, the multispecific anti-RTMC molecules are, for example, bifunctional antibodies (Db), single chain bifunctional antibodies (scDb), tandem scDb (Tandab), linear dimerization scDb (LD-scDb), circular dimerization scDb (CD-scDb), bi-bifunctional antibody, tandem scFv, tandem bi-scFv (e.g. bispecific T cell junction molecule), tandem tri-scFv, trifunctional antibody, bispecific Fab2, bi-minibody, Four-functional antibody, scFv-Fc-scFv fusion, dual affinity retargeting (DART) antibody, dual variable domain (DVD) antibody, IgG-scFab, scFab-ds-scFv, Fv2-Fc, IgG-scFv fusion Antibody, dock and lock (DNL) antibody, knob-into-hole (KiH) antibody (bispecific IgG prepared by KiH technology), DuoBody (bispecific prepared by Duobody technology) IgG), heteromultimeric antibodies or heteroconjugate antibodies. In some embodiments, the multispecific anti-RTMC molecule is a tandem scFv (eg, tandem di-scFv, such as a bispecific T cell junction molecule).Tandem scFv In some embodiments, the multispecific anti-RTMC molecule is a tandem scFv, which includes a first scFv and a second scFv containing an anti-RTMC antibody portion (also referred to herein as "tandem scFv multispecific anti-RTMC antibody"). In some embodiments, the tandem scFv multispecific anti-RTMC antibody further comprises at least one (such as at least about any of 2, 3, 4, 5, or more) additional scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, And b) a second scFv. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, the second scFv specifically binds to a complex comprising different HIV-1 RT peptides bound to MHC class I protein. In some embodiments, the second scFv specifically binds to a complex comprising HIV-1 RT peptides bound to different MHC class I proteins. In some embodiments, the second scFv specifically binds to different epitopes on a complex comprising HIV-1 RT peptide and MHC class I protein. In some embodiments, the second scFv specifically binds to another antigen. In some embodiments, the second scFv specifically binds to a cell, such as RTMC presenting an antigen on the cell surface. In some embodiments, the second scFv specifically binds to an antigen on the cell surface that does not express HIV-1 RT. In some embodiments, the second scFv specifically binds to an antigen on the surface of cytotoxic cells. In some embodiments, the second scFv specifically binds to an antigen on the surface of lymphocytes, such as T cells, NK cells, neutrophils, monocytes, macrophages, or dendritic cells. In some embodiments, the second scFv specifically binds to effector T cells, such as antigens on the surface of cytotoxic T cells. In some embodiments, the second scFv specifically binds to effector cells, including, for example, CD3γ, CD3δ, CD3ε, CD3ζ, CD28, CD16a, CD56, CD68, and antigens on the surface of GDS2D. In some embodiments, the first scFv is human, humanized, or semi-synthetic. In some embodiments, the second scFv is human, humanized, or semi-synthetic. In some embodiments, both the first scFv and the second scFv are human, humanized, or semi-synthetic. In some embodiments, the tandem scFv multispecific anti-RTMC antibody further comprises at least one (such as at least about any of 2, 3, 4, 5, or more) additional scFv. In some embodiments, the anti-RTMC antibody portion and at least one variant (such as at least 2, 3) of a variant of HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC antibody portion cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising: HIV-1 RT 181 (SEQ ID NO : 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9) peptide and HLA-A * 02: 01; and b) second scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, The first scFv comprises: i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, or up to about 3 (eg, about 1, 2 or 3 of Any one) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NOs: 241-244, or up to about 3 (eg, about 1, 2 or 3) Any one of them) amino acid substituted variants thereof, and the HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg about 1, Any one of 2 or 3) an amino acid substituted variant thereof; and ii) a light chain variable domain comprising: LC comprising the amino acid sequence of any one of SEQ ID NO: 247-249 -CDR1, or a variant thereof containing up to about 3 (eg, any of about 1, 2, or 3) amino acid substitutions, and an amino acid comprising any of SEQ ID NO: 250-253 LC-CDR3 of the sequence, or contains up to about 3 (eg about Any one of 1, 2 or 3) an amino acid substituted variant thereof, and b) a second scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, The first scFv comprises i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, comprising the amino acid of any one of SEQ ID NO: 241-244 HC-CDR2 of the sequence, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: comprising SEQ ID NO: 247-249 LC-CDR1 of the amino acid sequence of any one, and LC-CDR3 including the amino acid sequence of any one of SEQ ID NOs: 250-253, and b) the second scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, The first scFv comprises i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96, or up to about 5 (such as about 1, Any of 2, 3, 4 or 5) amino acid substituted variants thereof; HC-CDR2 comprising the amino acid sequence of any one of SEQ ID NOs: 97-124, or comprising up to about 5 (Such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and HC- comprising the amino acid sequence of any one of SEQ ID NO: 125-163 CDR3, or variants comprising up to about 5 (such as about any of 1, 2, 3, 4 or 5) amino acid substitutions; and ii) light chain variable domains comprising: comprising SEQ ID NO: LC-CDR1 of the amino acid sequence of any one of 164-189, or it contains up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions Variant; LC-C comprising the amino acid sequence of any one of SEQ ID NO: 190-207 DR2, or a variant comprising at most about 3 (such as about any of 1, 2, or 3) amino acid substitutions; and an amino acid sequence comprising any of SEQ ID NO: 208-239 LC-CDR3, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions; and b) a second scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, The first scFv comprises i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence of any one; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163, or up to about 5 in the HC-CDR sequence ( Such as any of about 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and ii) light chain variable domain sequence comprising: including any of SEQ ID NO: 164-189 LC-CDR1 of the amino acid sequence of one; LC-CDR2 including the amino acid sequence of any of SEQ ID NO: 190-207; and of any one of SEQ ID NO: 208-239 LC-CDR3 of the amino acid sequence, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC CDR sequence; and b) Second scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, The first scFv comprises i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence of any one; and HC-CDR3 including the amino acid sequence of any one of SEQ ID NOs: 125-163; and ii) the light chain variable domain sequence, comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189; LC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 190-207; and comprising SEQ ID NO: LC-CDR3 of the amino acid sequence of any one of 208-239; and b) the second scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv, the first scFv comprising a heavy chain variable domain comprising SEQ ID NO: 19- The amino acid sequence of any one of 46 or a variant thereof having at least about 95% (eg, at least about 96%, 97%, 98%, or 99%) sequence identity, and the light chain may A variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 47-74, or having at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) Variants of sequence identity; and b) a second scFv. In some embodiments, a tandem scFv multispecific (eg bispecific) anti-RTMC antibody is provided, which comprises a) a first scFv, the first scFv comprising a heavy chain variable domain comprising SEQ ID NO: 19- The amino acid sequence of any one of 46, and the light chain variable domain, which includes the amino acid sequence of any one of SEQ ID NOs: 47-74; and b) a second scFv. In some embodiments, a tandem scFv multispecific (eg, bispecific) anti-RTMC antibody is provided, which comprises: a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein , And b) a second scFv, wherein the tandem scFv multispecific anti-RTMC antibody is tandem two-scFv or tandem three-scFv. In some embodiments, the tandem scFv multispecific anti-RTMC antibody is tandem di-scFv. In some embodiments, the tandem scFv multispecific anti-RTMC antibody is a bispecific T cell junction molecule. For example, in some embodiments, a tandem bi-scFv bispecific anti-RTMC antibody is provided, which comprises: a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein , And b) a second scFv that specifically binds to an antigen on the surface of T cells. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, the second scFv specifically binds to effector T cells, such as antigens on the surface of cytotoxic T cells. In some embodiments, the second scFv specifically binds to an antigen selected from the group consisting of, for example, CD3γ, CD3δ, CD3ε, CD3ζ, CD28, OX40, GITR, CD137, CD27, CD40L, and HVEM. In some embodiments, the second scFv specifically binds to an agonistic epitope on an antigen on the surface of the T cell, wherein the binding of the second scFv to the antigen enhances T cell activation. In some embodiments, the first scFv is human, humanized, or semi-synthetic. In some embodiments, the second scFv is human, humanized, or semi-synthetic. In some embodiments, both the first scFv and the second scFv are human, humanized, or semi-synthetic. In some embodiments, a tandem bi-scFv bispecific anti-RTMC antibody is provided, comprising: a) specifically binding to a first scFv comprising the following complex: HIV-1 RT 181 (SEQ ID NO: 5) , HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9) peptide and HLA-A * 02: 01, and b) a second scFv that specifically binds to an antigen on the surface of T cells. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, or up to about 3 (eg, any of about 1, 2 or 3) amines Variants of the amino acid substitution, including the HC-CDR2 of the amino acid sequence of any of SEQ ID NO: 241-244, or up to about 3 (eg, any of about 1, 2, or 3) ) Amino acid substituted variants thereof, and the HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg, about 1, 2 or 3) Any one) an amino acid substituted variant thereof; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 247-249, or comprising Up to about 3 (eg, about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253 , Or contain up to about 3 (such as about any of 1, 2, or 3 One) amino acid substituted variants, and b) a second scFv that specifically binds to an antigen on the surface of T cells. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, HC- comprising the amino acid sequence of any of SEQ ID NO: 241-244 CDR2, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: comprising any one of SEQ ID NO: 247-249 LC-CDR1 of the amino acid sequence of the above, and LC-CDR3 including the amino acid sequence of any of SEQ ID NO: 250-253, and b) the first specific binding to the antigen on the surface of the T cell Two scFv. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 75-96, or up to about 5 (such as about 1, 2, 3, Any one of 4 or 5) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 97-124, or containing up to about 5 (such as about Any one of 1, 2, 3, 4 or 5) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 125-163, or comprising Up to about 5 (such as about any of 1, 2, 3, 4 or 5) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: comprising SEQ ID NO: 164- LC-CDR1 of the amino acid sequence of any one of 189, or a variant containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including LC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 190-207, or comprising More than three (such as about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 208-239 , Or a variant containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions; and b) a second antigen that specifically binds to an antigen on the surface of T cells scFv. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising any one of SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence; and HC-CDR3 containing the amino acid sequence of any one of SEQ ID NOs: 125-163; or up to about 5 (such as about 1, such as about 1, in the HC-CDR sequence) Any one of 2, 3, 4 or 5) amino acid substituted variants thereof; and ii) light chain variable domain sequence comprising: an amine comprising any of SEQ ID NO: 164-189 LC-CDR1 of the acid sequence; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and amino acid sequence of any one of SEQ ID NO: 208-239 LC-CDR3; or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence; and b) specific binding The second scFv of the antigen on the surface of T cells. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising any one of SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163; and ii) light chain variable domain sequence comprising: comprising SEQ ID NO : LC-CDR1 of the amino acid sequence of any one of 164-189; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and comprising SEQ ID NO: 208- LC-CDR3 of the amino acid sequence of any of 239; and b) a second scFv that specifically binds to an antigen on the surface of T cells. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, comprising: a) a first scFv, the first scFv comprising: a heavy chain variable domain comprising SEQ ID NO: 19-46 Any one of the amino acid sequences, or a variant having at least about 95% (eg, at least about 96%, 97%, 98%, or 99%) sequence identity, and the light chain is variable Domain, which comprises the amino acid sequence of any one of SEQ ID NOs: 47-74, or has a sequence of at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) Consistent with its variants, and b) a second scFv that specifically binds to an antigen on the surface of T cells. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, comprising: a) a first scFv, the first scFv comprising: a heavy chain variable domain comprising SEQ ID NO: 19-46 The amino acid sequence of any one, and the light chain variable domain, including the amino acid sequence of any one of SEQ ID NO: 47-74, and b) the first specific binding to the antigen on the surface of the T cell Two scFv. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, comprising: a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) It specifically binds to the second scFv of CD3ε. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, the first scFv is fused to the second scFv via a link to the peptide linker. In some embodiments, the length of the peptide linker is between about 5 to about 20 (such as any of about 5, 10, 15, or 20, including any range between these equivalents) amino acids. In some embodiments, the peptide linker comprises (and in some embodiments consists of the following) the amino acid sequence SRGGGGSGGGGSGGGGSLEMA (SEQ ID NO: 276). In some embodiments, the first scFv is human, humanized, or semi-synthetic. In some embodiments, the second scFv is human, humanized, or semi-synthetic. In some embodiments, both the first scFv and the second scFv are human, humanized, or semi-synthetic. In some embodiments, a tandem bi-scFv bispecific anti-RTMC antibody is provided, comprising: a) specifically binding to a first scFv comprising the following complex: HIV-1 RT 181 (SEQ ID NO: 5) , HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, The M184V (SEQ ID NO: 9) peptide and HLA-A * 02: 01, and b) specifically bind to the second scFv of CD3ε. In some embodiments, the first scFv is fused to the second scFv via a link to the peptide linker. In some embodiments, the length of the peptide linker is between about 5 to about 20 (such as any of about 5, 10, 15, or 20, including any range between these equivalents) amino acids. In some embodiments, the peptide linker comprises (and in some embodiments consists of the following) the amino acid sequence of SEQ ID NO: 276. In some embodiments, the first scFv is human, humanized, or semi-synthetic. In some embodiments, the second scFv is human, humanized, or semi-synthetic. In some embodiments, both the first scFv and the second scFv are human, humanized, or semi-synthetic. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Contains: i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, or up to about 3 (eg, any of about 1, 2 or 3) Amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NOs: 241-244, or up to about 3 (eg, about any of 1, 2, or 3 The variant of the amino acid substitution, and the HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg, about 1, 2 or 3) Any one) an amino acid substituted variant thereof; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 247-249, or Variants comprising up to about 3 (eg, any of about 1, 2 or 3) amino acid substitutions, and LC- comprising the amino acid sequence of any of SEQ ID NO: 250-253 CDR3, or contain up to about 3 (eg, about 1, 2 or 3 of Either) an amino acid substituted variant thereof, and b) a second scFv that specifically binds to CD3ε. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Contains: i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, HC comprising the amino acid sequence of any one of SEQ ID NO: 241-244 -CDR2 and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: comprising any one of SEQ ID NO: 247-249 LC-CDR1 of the amino acid sequence of the above, and LC-CDR3 including the amino acid sequence of any one of SEQ ID NOs: 250-253, and b) the second scFv that specifically binds to CD3ε. In some embodiments, the first scFv is fused to the second scFv via a link to the peptide linker. In some embodiments, the length of the peptide linker is between about 5 to about 20 (such as any of about 5, 10, 15, or 20, including any range between these equivalents) amino acids. In some embodiments, the peptide linker comprises (and in some embodiments consists of the following) the amino acid sequence of SEQ ID NO: 276. In some embodiments, the first scFv is human, humanized, or semi-synthetic. In some embodiments, the second scFv is human, humanized, or semi-synthetic. In some embodiments, both the first scFv and the second scFv are human, humanized, or semi-synthetic. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 75-96, or up to about 5 (such as about 1, 2, 3, Any one of 4 or 5) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 97-124, or containing up to about 5 (such as about Any one of 1, 2, 3, 4 or 5) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 125-163, or comprising Up to about 5 (such as about any of 1, 2, 3, 4 or 5) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: comprising SEQ ID NO: 164- LC-CDR1 of the amino acid sequence of any one of 189, or a variant containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including LC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 190-207, or comprising More than three (such as about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 208-239 Or a variant comprising up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, and b) a second scFv that specifically binds to CD3ε. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising any one of SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence; and HC-CDR3 containing the amino acid sequence of any one of SEQ ID NOs: 125-163; or up to about 5 (such as about 1, such as about 1, in the HC-CDR sequence) Any one of 2, 3, 4 or 5) amino acid substituted variants thereof; and ii) light chain variable domain sequence comprising: an amine comprising any of SEQ ID NO: 164-189 LC-CDR1 of the acid sequence; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and amino acid sequence of any one of SEQ ID NO: 208-239 LC-CDR3; or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence, and b) specific binding In the second scFv of CD3ε. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the first scFv Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising any one of SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163; and ii) light chain variable domain sequence comprising: comprising SEQ ID NO : LC-CDR1 of the amino acid sequence of any one of 164-189; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and comprising SEQ ID NO: 208- LC-CDR3 of the amino acid sequence of any of 239; and b) specifically binds to the second scFv of CD3ε. In some embodiments, the first scFv is fused to the second scFv via a link to the peptide linker. In some embodiments, the length of the peptide linker is between about 5 to about 20 (such as any of about 5, 10, 15, or 20, including any range between these equivalents) amino acids. In some embodiments, the peptide linker comprises (and in some embodiments consists of the following) the amino acid sequence of SEQ ID NO: 276. In some embodiments, the first scFv is human, humanized, or semi-synthetic. In some embodiments, the second scFv is human, humanized, or semi-synthetic. In some embodiments, both the first scFv and the second scFv are human, humanized, or semi-synthetic. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv, the first scFv comprising: a heavy chain variable domain comprising SEQ ID NO: 19-46 The amino acid sequence of any one, or a variant thereof having at least about 95% (eg, at least about 96%, 97%, 98%, or 99%) sequence identity, and the light chain variable domain , Which contains the amino acid sequence of any one of SEQ ID NO: 47-74, or has at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity Variants thereof, and b) a second scFv that specifically binds to CD3ε. In some embodiments, a tandem di-scFv bispecific anti-RTMC antibody is provided, which comprises a) a first scFv, the first scFv comprising: an amino acid comprising any one of SEQ ID NOs: 19-46 The heavy chain variable domain of the sequence, and the light chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 47-74, and b) a second scFv that specifically binds to CD3ε. In some embodiments, the first scFv is fused to the second scFv via a link to the peptide linker. In some embodiments, the length of the peptide linker is between about 5 to about 20 (such as any of about 5, 10, 15, or 20, including any range between these equivalents) amino acids. In some embodiments, the peptide linker comprises (and in some embodiments consists of the following) the amino acid sequence of SEQ ID NO: 276. In some embodiments, the first scFv is human, humanized, or semi-synthetic. In some embodiments, the second scFv is human, humanized, or semi-synthetic. In some embodiments, both the first scFv and the second scFv are human, humanized, or semi-synthetic. In some embodiments, the tandem bi-scFv bispecific anti-RTMC antibody ranges from about 0.1 pM to about 500 nM (such as about 0.1 pM, 1.0 pM, 10 pM, 50 pM, 100 pM, 500 pM, 1 nM, 10 nM , 50 nM, 100 nM, or 500 nM, including any range between these values) K_d Binding to a complex containing HIV-1 RT peptide and MHC class I protein. In some embodiments, the tandem bi-scFv bispecific anti-RTMC antibody ranges from about 1 nM to about 500 nM (such as about 1, 10, 25, 50, 75, 100, 150, 200, 250, 300, 350, 400 , 450 or 500 nM, including any range between these values) K_d Binding to a complex containing HIV-1 RT peptide and MHC class I protein. In some embodiments, the tandem bi-scFv bispecific anti-RTMC antibody is stable in solution for at least about 1 month (such as at least about 1 month, 2 months, 3 months, 4 months, 5 months, 6 Any of months, 7 months, 8 months, 9 months, 10 months, 11 months, 1 year, 2 years or longer). Stability can be expressed, for example, by preserving the activity of killing target cells by maintaining tandem di-scFv bispecific anti-RTMC antibodies in an aqueous formulation maintained at a storage temperature, such as 4 ° C. For example, in some embodiments, the tandem bi-scFv bispecific anti-RTMC antibody is maintained at storage temperature for at least about 1 month (such as at least about 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, 1 year, 2 years or more) at least 40% (such as at least About 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or greater Either) Kill target cell activity. In some embodiments, the storage temperature does not exceed about 25 ° C (such as not exceed about 20, 18, 16, 14, 12, 10, 8, 6, 5, 4, 3, 2, 1, or 0 ° C, or lower ). In some embodiments, the tandem bi-scFv bispecific anti-RTMC antibody maintains at least 60% of the target cell-killing activity in an aqueous formulation maintained at a storage temperature of 4 for at least about 2 years. In some embodiments, the tandem bi-scFv bispecific anti-RTMC antibody comprises a) a first scFv that specifically binds to a complex comprising HIV-1 RT 181 peptide and MHC class I protein, and b) specifically binds to The second scFv of CD3ε. For example, in some embodiments, a multispecific anti-RTMC molecule (such as di-scFv) includes an anti-RTMC antibody portion that contains heavy and light chain variable domains that include the following HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2, and LC-CDR3 of the amino acid sequence of SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, respectively SEQ ID NO: 76, 98, 126, 165, 191 and 209, SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 And 211, SEQ ID NO: 79, 101, 129, 167, 194, and 212, respectively, SEQ ID NO: 80, 102, 130, 168, 192, and 213, SEQ ID NO: 81, 103, 131, respectively , 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82 , 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, SEQ ID NO: 88, 113, 144, 178, 201, and 224, SEQ ID NO: 82, 114, 145, 179, 202, and 225, respectively, SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200, and 238, or SEQ ID NO: 96, 124, 163, 189, 207, and 239, respectively; or in HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1 And / or LC-CDR3 individually contains up to about 5 (e.g., any of about 1, 2, 3, 4, or 5) amino acid substitutions and / or up to about 3 in LC-CDR2 ( For example, about any of 1, 2, or 3) amino acid substituted variants thereof. In some embodiments, the multispecific anti-RTMC molecule (such as di-scFv) comprises an anti-RTMC antibody portion comprising HC-CDR1, HC-CDR2, HC-CDR3, LC- CDR1, LC-CDR2 and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191 and 209, SEQ ID respectively NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, SEQ ID NO: 80, 102, 130, 168, 192 and 213 respectively, SEQ ID NO: 81, 103, 131, 169, 191 and 214 respectively, SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, SEQ ID NO: 81, 117, 148, 169, 191, and 218, SEQ ID NO: 82, 118, 149, 180, 199, and 228, respectively, SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185 , 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108 , 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, 173, 206, and 237, respectively, SEQ ID NO: 95, 123, 162, 188, 200, and 238, or SEQ ID, respectively NO: 96, 124, 163, 189, 207, and 239, or include up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the HC-CDR sequence and / Or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence. In some embodiments, the multispecific anti-RTMC molecule (such as di-scFv) comprises an anti-RTMC antibody portion comprising HC-CDR1, HC-CDR2, HC-CDR3, LC- CDR1, LC-CDR2 and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191 and 209, SEQ ID respectively NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, SEQ ID NO: 80, 102, 130, 168, 192 and 213 respectively, SEQ ID NO: 81, 103, 131, 169, 191 and 214 respectively, SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, SEQ ID NO: 81, 117, 148, 169, 191, and 218, SEQ ID NO: 82, 118, 149, 180, 199, and 228, respectively, SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185 , 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108 , 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, 173, 206, and 237, respectively, SEQ ID NO: 95, 123, 162, 188, 200, and 238, or SEQ ID, respectively NO: 96, 124, 163, 189, 207 and 239. In some embodiments, a multispecific anti-RTMC molecule (such as di-scFv) includes an anti-RTMC antibody portion that includes heavy and light chain variable domains that include the following amino acid sequences : SEQ ID NO: 19 and 47 respectively, SEQ ID NO: 20 and 48 respectively, SEQ ID NO: 21 and 49 respectively, SEQ ID NO: 22 and 50 respectively, SEQ ID NO: 23 and 51 respectively , Respectively SEQ ID NO: 24 and 52, respectively SEQ ID NO: 25 and 53, respectively SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56 , SEQ ID NO: 29 and 57, respectively SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61 respectively , SEQ ID NO: 34 and 62, SEQ ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID NO: 38 and 66, respectively , SEQ ID NO: 39 and 67, SEQ ID NO: 40 and 68, SEQ ID NO: 41 and 69, SEQ ID NO: 42 and 70, SEQ ID NO: 43 and 71, respectively , Respectively SEQ ID NO: 44 and 72, respectively SEQ ID NO: 45 and 73, or points To SEQ ID NO: 46 and 74, individually or at least about 95% (e.g. at least about 96%, 97%, 98%, or of any one of 99%) sequence identity to a variant thereof. In some embodiments, the multispecific anti-RTMC molecule comprises an anti-RTMC antibody portion containing heavy and light chain variable domains, the heavy and light chain variable domains comprising the following amino acid sequences: SEQ ID NO, respectively : 19 and 47, respectively SEQ ID NO: 20 and 48, respectively SEQ ID NO: 21 and 49, respectively SEQ ID NO: 22 and 50, respectively SEQ ID NO: 23 and 51, respectively SEQ ID NO : 24 and 52, respectively SEQ ID NO: 25 and 53, respectively SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO : 29 and 57, respectively SEQ ID NO: 30 and 58, respectively SEQ ID NO: 31 and 59, respectively SEQ ID NO: 32 and 60, respectively SEQ ID NO: 33 and 61, respectively SEQ ID NO : 34 and 62, respectively SEQ ID NO: 35 and 63, respectively SEQ ID NO: 36 and 64, respectively SEQ ID NO: 37 and 65, respectively SEQ ID NO: 38 and 66, respectively SEQ ID NO : 39 and 67, respectively SEQ ID NO: 40 and 68, respectively SEQ ID NO: 41 and 69, respectively SEQ ID NO: 42 and 70, respectively SEQ ID NO: 43 and 71, respectively SEQ ID NO : 44 and 72, respectively SEQ ID NO: 45 and 73, or respectively SEQ ID NO: 46 and 74. In some embodiments, a multispecific anti-RTMC molecule (such as di-scFv) comprises an anti-RTMC antibody portion containing heavy and light chain variable domains, which heavy chain and light chain variable domains comprise SEQ ID NO: Amino acid sequences of 27 and 55, or variants thereof that individually have at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, a multispecific anti-RTMC molecule (such as di-scFv) comprises an anti-RTMC antibody portion comprising heavy and light chains containing amino acid sequences of SEQ ID NOs: 27 and 55, respectively Variable domain. In some embodiments, a multispecific anti-RTMC molecule (such as di-scFv) comprises an anti-RTMC antibody portion containing heavy and light chain variable domains, which heavy chain and light chain variable domains comprise SEQ ID NO: The amino acid sequences of 30 and 58, or variants thereof that individually have at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, a multispecific anti-RTMC molecule (such as di-scFv) comprises an anti-RTMC antibody portion comprising heavy and light chains containing amino acid sequences of SEQ ID NOs: 30 and 58, respectively Variable domain.Chimeric receptors and effector cells In some embodiments, the anti-RTMC construct is a chimeric antigen receptor comprising an anti-RTMC antibody portion (also referred to herein as "anti-RTMC chimeric receptor"). Also provided is an effector cell (eg, T cell) containing a chimeric receptor, which contains an anti-RTMC antibody portion (also referred to herein as "anti-RTMC chimeric receptor effector cell", such as "anti-RTMC Chimeric receptor T cells ").Chimeric antigen receptor In some embodiments, Chimeric receptors are chimeric antigen receptors (CAR), And the anti-RTMC chimeric receptor is anti-RTMC CAR. In some embodiments, Anti-RTMC CAR contains: a) an extracellular domain that contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein and b) an intracellular signaling domain. The transmembrane domain may exist between the extracellular domain and the intracellular domain.  Between the extracellular domain and transmembrane domain of anti-RTMC CAR, Or between the intracellular domain and transmembrane domain of anti-RTMC CAR, There may be a spacer field. The spacer domain may be any oligopeptide or polypeptide used to link the transmembrane domain in the polypeptide chain to the extracellular domain or intracellular domain. The spacer domain may contain up to about 300 amino acids, Including, for example, about 10 to about 100, Or about 25 to about 50 amino acids.  The transmembrane domain can be derived from natural or synthetic sources. When the source is natural, This domain can be derived from any membrane-bound protein or transmembrane protein. The transmembrane region specifically used in the present invention may be derived from (ie, at least include the following transmembrane region) T cell receptors, CD28, CD3ε, CD3ζ, CD45, CD4, CD5, CD8, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD134, CD137, CD154 of α, β, δ, γ or ξ chain. In some embodiments, The transmembrane domain can be synthetic, In this situation, It may mainly contain hydrophobic residues, Such as leucine and valine. In some embodiments, Amphetamine acid can be found at each end of the synthetic transmembrane domain, Triad of tryptophan and valine. In some embodiments, Having for example a length between about 2 and about 10 (such as about 2, 3. 4. 5. 6. 7. 8, Either 9 or 10) a short oligopeptide or polypeptide linker between amino acids can form a bond between the transmembrane domain of the anti-RTMC CAR and the intracellular signaling domain. In some embodiments, The linker is glycine-serine dimer.  In some embodiments, Use a transmembrane domain that naturally binds to one of the sequences in the intracellular domain of anti-RTMC CAR (for example, if the anti-RTMC CAR intracellular domain contains a CD28 costimulatory sequence, The anti-RTMC CAR transmembrane domain is derived from the CD28 transmembrane domain). In some embodiments, The transmembrane domains can be selected or modified by amino acid substitution to avoid binding of such domains to the transmembrane domains of the same or different surface membrane proteins to minimize interaction with other members of the receptor complex.  The intracellular signaling domain of anti-RTMC CAR is responsible for activating at least one of the normal effector functions of immune cells in which anti-RTMC CAR has been placed. The effector function of T cells can be, for example, cytolytic activity or auxiliary activity, Including secretion of cytokines. therefore, The term "intracellular signaling domain" refers to a portion of a protein that transduces effector function signals and guides cells to perform specific functions. Although generally all intracellular signaling domains can be used, But in most cases, It is not necessary to use the entire chain. As for the extent to which the truncated part of the intracellular signaling domain is used, Such truncated parts can be used to replace the complete chain as long as they transduce the effect signal. The term "intracellular signaling sequence" is therefore intended to include any truncated portion of the intracellular signaling domain sufficient to transduce effector functional signals.  Examples of intracellular signaling domains used in the anti-RTMC CAR of the present invention include cytoplasmic sequences of T cell receptors (TCR) and co-receptors that work together to initiate signal transduction after antigen receptor conjugation, And any derivatives or variants of these sequences and any synthetic sequences with the same functional capabilities.  It is known that signals generated via TCR alone are not sufficient to fully activate T cells and also require secondary or co-stimulatory signals. therefore, T cell activation can be said to be mediated by two distinct classes of intracellular signaling sequences: Those that trigger antigen-dependent primary activation via TCR (primary signaling sequences) and those that function in an antigen-independent manner to provide secondary or costimulatory signals (costimulatory signaling sequences).  The primary signaling sequence regulates the primary activation of the TCR complex in a stimulatory or inhibitory manner. The first-level signaling sequence that functions in a stimulating manner may contain signaling primitives, It is called the immunoreceptor tyrosine-based activation motif or ITAM. In some embodiments, The RTMC CAR construct contains one or more ITAMs.  Examples of ITAMs containing primary signaling sequences specifically used in the invention include those derived from TCRζ, FcRγ, FcRβ, CD3γ, CD3δ, CD3ε, CD5, CD22, CD79a, CD79b and CD66d.  In some embodiments, The anti-RTMC CAR contains a first order signaling sequence derived from CD3ζ. For example, The intracellular signaling domain of the CAR may include the CD3ζ intracellular signaling sequence itself or in combination with any other desired intracellular signaling sequence suitable in the context of the anti-RTMC CAR of the present invention. For example, The intracellular domain of the anti-RTMC CAR may include CD3ζ intracellular signaling sequences and costimulatory signaling sequences. The co-stimulatory signaling sequence can be part of the intracellular domain of the co-stimulatory molecule, The costimulatory molecules include, for example, CD27, CD28, 4-1BB (CD137), OX40, CD30, CD40, PD-1, ICOS, Lymphocyte function related antigen-1 (LFA-1), CD2, CD7, LIGHT, NKG2C, B7-H3, Ligands and analogs that specifically bind CD83.  In some embodiments, The intracellular signaling domain of the anti-RTMC CAR includes the intracellular signaling sequence of CD3ζ and the intracellular signaling sequence of CD28. In some embodiments, The intracellular signaling domain of the anti-RTMC CAR includes the intracellular signaling sequence of CD3ζ and the intracellular signaling sequence of 4-1BB. In some embodiments, The intracellular signaling domain of the anti-RTMC CAR includes the intracellular signaling sequence of CD3ζ and the intracellular signaling sequences of CD28 and 4-1BB.  therefore, For example, in some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, The extracellular domain contains an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein; b) Transmembrane domain; And c) intracellular signaling domain. In some embodiments, The HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8) or HIV-1 RT 181 Y181C,  M184V (SEQ ID NO:  9). In some embodiments, The MHC class I protein is HLA-A02. In some embodiments, The MHC class I protein is HLA-A * 02: 01. In some embodiments, The intracellular signaling domain can activate immune cells. In some embodiments, The intracellular signaling domain includes primary signaling sequences and costimulatory signaling sequences. In some embodiments, The primary signaling sequence contains the CD3ζ intracellular signaling sequence. In some embodiments, Costimulatory signaling sequences include CD28 and / or 4-1BB intracellular signaling sequences. In some embodiments, The intracellular domain includes CD3ζ intracellular signaling sequences and CD28 and / or 4-1BB intracellular signaling sequences. In some embodiments, The anti-RTMC antibody portion and at least one variant (such as at least 2, 3. 4. Either 5 or 6) Complex cross reaction. In some embodiments, The anti-RTMC antibody portion is at least one of a different subtype (such as at least 2, 3. Either 4 or 5) Complex cross reaction.  In some embodiments, Provide an anti-RTMC CAR, It contains a) an extracellular domain that contains an anti-RTMC antibody portion that specifically binds to the following complexes: HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO:  9) Peptide and HLA-A * 02: 01; b) Transmembrane domain; And c) intracellular signaling domain. In some embodiments, The intracellular signaling domain can activate immune cells. In some embodiments, The intracellular signaling domain includes primary signaling sequences and costimulatory signaling sequences. In some embodiments, The primary signaling sequence contains the CD3ζ intracellular signaling sequence. In some embodiments, Costimulatory signaling sequences include CD28 and / or 4-1BB intracellular signaling sequences. In some embodiments, The intracellular domain includes CD3ζ intracellular signaling sequences and CD28 and / or 4-1BB intracellular signaling sequences.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody part that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of 240, Or contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any one of 241-244, Or contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any of 245-246, Or contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; And ii) light chain variable domain, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any of 247-249, Or contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 250-253, Or contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain. In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of 240, Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any one of 241-244, And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any of 245-246; And ii) light chain variable domain, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any of 247-249, And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 250-253; b) Intracellular signaling domain. In some embodiments, The intracellular signaling domain can activate immune cells. In some embodiments, The intracellular signaling domain includes primary signaling sequences and costimulatory signaling sequences. In some embodiments, The primary signaling sequence contains the CD3ζ intracellular signaling sequence. In some embodiments, Costimulatory signaling sequences include CD28 and / or 4-1BB intracellular signaling sequences. In some embodiments, The intracellular domain includes CD3ζ intracellular signaling sequences and CD28 and / or 4-1BB intracellular signaling sequences.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, The antibody part contains i) a heavy chain variable domain, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of any one of 75-96, Or contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any of 97-124, Or contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any one of 125-163, Or contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any one of 164-189, Or contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, Contains SEQ ID NO:  LC-CDR2 of the amino acid sequence of any one of 190-207, Or contains up to about 3 (such as about 1, Any of 2 or 3) amino acid substituted variants thereof, And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 208-239, Or contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain. In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of any one of 75-96; Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any of 97-124; And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any one of 125-163; Or contain up to about 5 (such as about 1, in the HC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain sequence, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any one of 164-189; Contains SEQ ID NO:  LC-CDR2 of the amino acid sequence of any one of 190-207; And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 208-239, Or include up to about 5 (such as about 1, in the LC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain. In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of any one of 75-96; Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any of 97-124; And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any one of 125-163; And ii) light chain variable domain sequence, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any one of 164-189; Contains SEQ ID NO:  LC-CDR2 of the amino acid sequence of any one of 190-207; And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 208-239; b) Intracellular signaling domain. In some embodiments, The intracellular signaling domain can activate immune cells. In some embodiments, The intracellular signaling domain includes primary signaling sequences and costimulatory signaling sequences. In some embodiments, The primary signaling sequence contains the CD3ζ intracellular signaling sequence. In some embodiments, Costimulatory signaling sequences include CD28 and / or 4-1BB intracellular signaling sequences. In some embodiments, The intracellular domain includes CD3ζ intracellular signaling sequences and CD28 and / or 4-1BB intracellular signaling sequences.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, Contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, This antibody part contains the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46, Or have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) variants of sequence identity, And the light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74, Or have at least about 95% (including for example at least about 96%, 97%, 98% or 99%) variants of sequence identity; b) Transmembrane domain; And c) intracellular signaling domain. In some embodiments, Provide an anti-RTMC CAR, It contains: a) extracellular domain, Contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, This antibody part contains the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46, And the light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74; b) Intracellular signaling domain. In some embodiments, The intracellular signaling domain can activate immune cells. In some embodiments, The intracellular signaling domain includes primary signaling sequences and costimulatory signaling sequences. In some embodiments, The primary signaling sequence contains the CD3ζ intracellular signaling sequence. In some embodiments, Costimulatory signaling sequences include CD28 and / or 4-1BB intracellular signaling sequences. In some embodiments, The intracellular domain includes CD3ζ intracellular signaling sequences and CD28 and / or 4-1BB intracellular signaling sequences.  In some embodiments, Provide an anti-RTMC CAR, It contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8) or HIV-1 RT 181 Y181C,  M184V (SEQ ID NO:  9). In some embodiments, The MHC class I protein is HLA-A02. In some embodiments, The MHC class I protein is HLA-A * 02: 01.  In some embodiments, Provide an anti-RTMC CAR, It contains: a) extracellular domain, Contains an anti-RTMC antibody portion that specifically binds to a complex comprising: HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO:  9) Peptide and HLA-A * 02: 01; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody part that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of 240, Or contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any one of 241-244, Or contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any of 245-246, Or contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; And ii) light chain variable domain, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any of 247-249, Or contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 250-253, Or contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody part that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of 240, Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any one of 241-244, And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any of 245-246; And ii) light chain variable domain, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any of 247-249, And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 250-253; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, The antibody part contains i) a heavy chain variable domain, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of any one of 75-96, Or contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any of 97-124, Or contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any one of 125-163, Or contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any one of 164-189, Or contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, Contains SEQ ID NO:  LC-CDR2 of the amino acid sequence of any one of 190-207, Or contains up to about 3 (such as about 1, Any of 2 or 3) amino acid substituted variants thereof, And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 208-239, Or contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of any one of 75-96; Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any of 97-124; And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any one of 125-163, Or contain up to about 5 (such as about 1, in the HC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain sequence, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any one of 164-189; Contains SEQ ID NO:  LC-CDR2 of the amino acid sequence of any one of 190-207; And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 208-239, Or include up to about 5 (such as about 1, in the LC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  In some embodiments, Provide an anti-RTMC CAR, It contains a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, The antibody part contains i) the heavy chain variable domain sequence, It contains: Contains SEQ ID NO:  HC-CDR1 of the amino acid sequence of any one of 75-96; Contains SEQ ID NO:  HC-CDR2 of the amino acid sequence of any of 97-124; And contains SEQ ID NO:  HC-CDR3 of the amino acid sequence of any one of 125-163; And ii) light chain variable domain sequence, It contains: Contains SEQ ID NO:  LC-CDR1 of the amino acid sequence of any one of 164-189; Contains SEQ ID NO:  LC-CDR2 of the amino acid sequence of any one of 190-207; And contains SEQ ID NO:  LC-CDR3 of the amino acid sequence of any one of 208-239; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  In some embodiments, Provide an anti-RTMC CAR, It contains: a) extracellular domain, Contains an anti-RTMC antibody portion that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein, This antibody part contains the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46, Or have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) variants of sequence identity, And the light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74, Or have at least about 95% (including for example at least about 96%, 97%, 98% or 99%) variants of sequence identity; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  In some embodiments, Provide an anti-RTMC CAR, It contains: a) extracellular domain, It contains an anti-RTMC antibody part that specifically binds to a complex containing HIV-1 RT peptide and MHC class I protein This antibody part contains the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46, And the light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence.  For example, In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239; Or in HC-CDR1 HC-CDR2, HC-CDR3, LC-CDR1 and / or LC-CDR3 individually include up to about 5 (e.g. about 1, 2, 3. Any of 4 or 5) amino acid substitutions and / or up to about 3 (e.g. Either 2 or 3) amino acid substituted variants thereof.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO: , 82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239, Or contain up to about 5 (such as about 1, in the HC-CDR sequence 2, 3. Any one of 4 or 5) amino acid substitutions and / or include up to about 5 (such as about 1, 2, 3. Either 4 or 5) amino acid substituted variants thereof.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains contain the following amino acid sequences: SEQ ID NO:  19 and 47, SEQ ID NO:  20 and 48, SEQ ID NO:  21 and 49, SEQ ID NO:  22 and 50, SEQ ID NO:  23 and 51, SEQ ID NO:  24 and 52, SEQ ID NO:  25 and 53, SEQ ID NO:  26 and 54, SEQ ID NO:  27 and 55, SEQ ID NO:  28 and 56, SEQ ID NO:  29 and 57, SEQ ID NO:  30 and 58, SEQ ID NO:  31 and 59, SEQ ID NO:  32 and 60, SEQ ID NO:  33 and 61, SEQ ID NO:  34 and 62, SEQ ID NO:  35 and 63, SEQ ID NO:  36 and 64, SEQ ID NO:  37 and 65, SEQ ID NO:  38 and 66, SEQ ID NO:  39 and 67, SEQ ID NO:  40 and 68, SEQ ID NO:  41 and 69, SEQ ID NO:  42 and 70, SEQ ID NO:  43 and 71, SEQ ID NO:  44 and 72, SEQ ID NO:  45 and 73, Or SEQ ID NO:  46 and 74, Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains contain the following amino acid sequences: SEQ ID NO:  19 and 47, SEQ ID NO:  20 and 48, SEQ ID NO:  21 and 49, SEQ ID NO:  22 and 50, SEQ ID NO:  23 and 51, SEQ ID NO:  24 and 52, SEQ ID NO:  25 and 53, SEQ ID NO:  26 and 54, SEQ ID NO:  27 and 55, SEQ ID NO:  28 and 56, SEQ ID NO:  29 and 57, SEQ ID NO:  30 and 58, SEQ ID NO:  31 and 59, SEQ ID NO:  32 and 60, SEQ ID NO:  33 and 61, SEQ ID NO:  34 and 62, SEQ ID NO:  35 and 63, SEQ ID NO:  36 and 64, SEQ ID NO:  37 and 65, SEQ ID NO:  38 and 66, SEQ ID NO:  39 and 67, SEQ ID NO:  40 and 68, SEQ ID NO:  41 and 69, SEQ ID NO:  42 and 70, SEQ ID NO:  43 and 71, SEQ ID NO:  44 and 72, SEQ ID NO:  45 and 73, Or SEQ ID NO:  46 and 74.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion includes the following heavy and light chain variable domains: SEQ ID NO:  Amino acid sequence of 27 and 55, Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion contains SEQ ID NO:  The heavy and light chain variable domains of the amino acid sequences of 27 and 55. In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion includes the following heavy and light chain variable domains: SEQ ID NO:  The amino acid sequence of 30 and 58, Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion contains SEQ ID NO:  The heavy and light chain variable domains of the amino acid sequences of 30 and 58.Chimeric antibody / T Cell receptor In some embodiments, the chimeric receptor is a chimeric antibody / T cell receptor construct (referred to herein as "abTCR"), and the anti-RTMC chimeric receptor is anti-RTMC abTCR. In some embodiments, the anti-RTMC abTCR comprises a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) is capable of recruiting at least one TCR-related T cell receptor module (TCRM) of signal transduction module. In some embodiments, the anti-RTMC abTCR comprises a first polypeptide chain and a second polypeptide chain. In some embodiments, the first and second polypeptide chains are linked, such as by covalent bonds (eg, peptide bonds or other chemical bonds) or non-covalent bonds. In some embodiments, the anti-RTMC abTCR is a heterodimer comprising a first polypeptide chain and a second polypeptide chain. In some embodiments, the first polypeptide chain and the second polypeptide chain are connected via at least one disulfide bond. The specificity of anti-RTMC abTCR is derived from the portion of the antibody that confers RTMC binding specificity. In some embodiments, the antibody portion is a Fab-like antigen binding module. In some embodiments, the antibody portion is an Fv-like antigen binding module. In some embodiments, the antibody portion is scFv. The ability of anti-RTMC abTCR to recruit TCR-related signaling modules originates from the T cell receptor module (TCRM). In some embodiments, the TCRM comprises a transmembrane module of TCR (such as αβTCR or γδTCR). In some embodiments, the TCRM further comprises one or both of TCR's linker peptide or fragments thereof. In some embodiments, the anti-RTMC abTCR further comprises at least one intracellular domain. In some embodiments, one or more of the at least one intracellular domain of anti-RTMC abTCR comprises a sequence from the intracellular domain of TCR. In some embodiments, one or more of the at least one intracellular domain of anti-RTMC abTCR comprises T cell co-stimulatory signaling sequences. The co-stimulatory signaling sequence may be part of the intracellular domain of the co-stimulatory molecule including, for example, CD27, CD28, 4-1BB (CD137), OX40, CD30, CD40, ICOS, lymphocyte function-related antigen-1 LFA-1), CD2, CD7, LIGHT, NKG2C, B7-H3, ligands that specifically bind CD83, and the like. In some embodiments, the antibody portion is contained in the extracellular domain of anti-RTMC abTCR. In some embodiments, the anti-RTMC abTCR further comprises one or more peptide linkers between the antibody portion and TCRM to optimize the length of the extracellular domain. In some embodiments, the antibody portion is a Fab-like antigen binding module, which comprises a) a first polypeptide chain, the first polypeptide chain comprises a first antigen binding domain, and the first antigen binding domain comprises V_H Antibody domain and C_H 1 an antibody domain; and b) a second polypeptide chain comprising a second antigen binding domain, the second antigen binding domain comprising V_L Antibody domain and C_L Antibody domain. In some embodiments, the first antigen binding domain comprises C_H 1V of amine terminal of antibody domain_H The antibody domain and / or the second antigen binding domain comprises C_L Antibody domain amine terminal V_L Antibody domain. In some embodiments, at V_L With C_L There are peptide linkers between antibody domains and / or in V_H With C_H 1 There is a peptide linker between antibody domains. In some embodiments, all V_L Antibody domain and V_H The antibody domain CDRs are all derived from the same antibody part. In some embodiments, V_L Antibody domain and V_H The antibody domain contains antibody CDRs derived from more than one antibody portion. In some embodiments, the first and second polypeptide chains are linked, such as by covalent bonds (eg, peptide bonds or other chemical bonds) or non-covalent bonds. In some embodiments, the first and second antigen binding domains are connected by disulfide bonds. In some embodiments, the first and second antigen binding domains are via C_H Residues in the 1 domain and C_L The disulfide bonds between the residues in the domain. In some embodiments, C_H The domain 1 is derived from the heavy chain of IgG (eg IgG1, IgG2, IgG3 or IgG4), and is optionally human. In some embodiments, C_H Domain 1 is a variant that contains one or more modifications (such as amino acid substitutions, insertions, and / or deletions) compared to the sequence from which it originated. In some embodiments, C_L The domain is derived from a kappa or lambda light chain, depending on the situation. In some embodiments, C_L A domain is a variant that contains one or more modifications (such as amino acid substitutions, insertions, and / or deletions) compared to the sequence from which it originated. In some embodiments, C_H 1 and / or C_L Domains contain one or more modifications that do not substantially change their binding affinity to each other. In some embodiments, C_H 1 and / or C_L Domains contain one or more modifications that increase their binding affinity to each other and / or introduce non-naturally occurring disulfide bonds. In some embodiments, the Fab-like antigen binding module is human, humanized, chimeric, semi-synthetic, or fully synthetic. In some embodiments, the antibody portion is a Fab-like antigen binding module, which comprises a) a first polypeptide chain, the first polypeptide chain comprises a first antigen binding domain, and the first antigen binding domain comprises V_L Antibody domain and C_H 1 an antibody domain; and b) a second polypeptide chain comprising a second antigen binding domain, the second antigen binding domain comprising V_H Antibody domain and C_L Antibody domain. In some embodiments, the first antigen binding domain is contained in C_H 1 V at the amine end of the antibody domain_L The antibody domain and / or second antigen binding domain is contained in C_L V at the amine end of the antibody domain_H Antibody domain. In some embodiments, at V_H With C_L There are peptide linkers between antibody domains and / or in V_L With C_H 1 There is a peptide linker between antibody domains. In some embodiments, all V_L Antibody domain and V_H The antibody domain CDRs are all derived from the same antibody part. In some embodiments, V_L Antibody domain and V_H The antibody domain contains antibody CDRs derived from more than one antibody portion. In some embodiments, the first and second polypeptide chains are linked, such as by covalent bonds (eg, peptide bonds or other chemical bonds) or non-covalent bonds. In some embodiments, the first and second antigen binding domains are connected by disulfide bonds. In some embodiments, the first and second antigen binding domains are via C_H Residues in the 1 domain and C_L The disulfide bonds between the residues in the domain. In some embodiments, C_H The domain 1 is derived from the heavy chain of IgG (eg IgG1, IgG2, IgG3 or IgG4), and is optionally human. In some embodiments, C_H Domain 1 is a variant that contains one or more modifications (such as amino acid substitutions, insertions, and / or deletions) compared to the sequence from which it originated. In some embodiments, C_L The domain is derived from a kappa or lambda light chain, depending on the situation. In some embodiments, C_L A domain is a variant that contains one or more modifications (such as amino acid substitutions, insertions, and / or deletions) compared to the sequence from which it originated. In some embodiments, C_H 1 and / or C_L Domains contain one or more modifications that do not substantially change their binding affinity to each other. In some embodiments, C_H 1 and / or C_L Domains contain one or more modifications that increase their binding affinity to each other and / or introduce non-naturally occurring disulfide bonds. In some embodiments, the Fab-like antigen binding module is human, humanized, chimeric, semi-synthetic, or fully synthetic. In some embodiments, the antibody portion is an Fv-like antigen binding module that includes a) a first polypeptide chain that includes a first antigen binding domain that includes V_H The antibody domain and optionally the first TCR constant domain from the T cell receptor subunit; and b) a second polypeptide chain, the second polypeptide chain comprising a second antigen binding domain, the second antigen binding domain comprising V_L The antibody domain and optionally the second TCR constant domain from the T cell receptor subunit. In some embodiments, the first antigen binding domain comprises a V at the amine end of the first TCR constant domain_H The antibody domain and / or the second antigen-binding domain contains the V at the amine end of the second TCR constant domain_L Antibody domain. In some embodiments, at V_L There is a peptide linker between the antibody domain and the first TCR constant domain and / or in the V_H There is a peptide linker between the antibody domain and the second TCR constant domain. In some embodiments, all V_L Antibody domain and V_H The antibody domain CDRs are all derived from the same antibody part. In some embodiments, V_L Antibody domain and V_H The antibody domain contains antibody CDRs derived from more than one antibody portion. In some embodiments, the first and second polypeptide chains are linked, such as by covalent bonds (eg, peptide bonds or other chemical bonds) or non-covalent bonds. In some embodiments, the first and second antigen binding domains are connected by disulfide bonds. In some embodiments, the first and second antigen binding domains are connected by a disulfide bond between the residue in the first TCR constant domain and the residue in the second TCR constant domain. In some embodiments, the first TCR constant domain is derived from the TCR alpha subunit, optionally human, and / or the second TCR constant domain is derived from the TCR beta subunit, optionally human. In some embodiments, the first TCR constant domain is derived from a TCR alpha subunit comprising the amino acid sequence of SEQ ID NO: 281, and / or the second TCR constant domain is derived from an amino acid comprising SEQ ID NO: 282 TCR β subunit of the sequence. In some embodiments, the first TCR constant domain is derived from TCR delta subunits, optionally human, and / or the second TCR constant domain is derived from TCR gamma subunits, optionally human. In some embodiments, the first TCR constant domain is derived from a TCR delta subunit comprising the amino acid sequence of SEQ ID NO: 283, and / or the second TCR constant domain is derived from an amino acid comprising SEQ ID NO: 282 TCR γ subunit of the sequence. In some embodiments, the first and / or second TCR constant domain is a variant that includes one or more modifications (eg, amino acid substitutions, insertions, and / or deletions) compared to the sequence from which it was derived. In some embodiments, the first and / or second TCR constant domains include one or more modifications that do not substantially change their binding affinity to each other. In some embodiments, the first and / or second TCR constant domains include one or more modifications that increase their binding affinity to each other and / or introduce non-naturally occurring disulfide bonds. In some embodiments, the Fv-like antigen binding module is human, humanized, chimeric, semi-synthetic, or fully synthetic. In some embodiments, the antibody portion is scFv, the scFv comprises a) a polypeptide chain, the polypeptide chain comprises V_H Antibody domain and V_L Antibody domain. In some embodiments, scFv is included in V_L V at the amine end of the antibody domain_H Antibody domain. In some embodiments, scFv is included in V_H V at the amine end of the antibody domain_L Antibody domain. In some embodiments, at V_L Antibody domain and V_H There are peptide linkers between antibody domains. In some embodiments, all V_L Antibody domain and V_H The antibody domain CDRs are all derived from the same antibody part. In some embodiments, V_L Antibody domain and V_H The antibody domain contains antibody CDRs derived from more than one antibody portion. In some embodiments, the scFv is human, humanized, chimeric, semi-synthetic, or fully synthetic. In some embodiments, TCRM comprises a) a first polypeptide chain comprising a first T cell receptor domain (TCRD) containing a first transmembrane domain; and b) a second polypeptide chain, The second polypeptide chain includes a second TCRD containing a second transmembrane domain. In some embodiments, the first transmembrane domain is the transmembrane domain of the first TCR subunit and / or the second transmembrane domain is the transmembrane domain of the second TCR subunit. In some embodiments, the first TCR subunit is the TCR α chain (eg, GenBank deposit number: CCI73895), and the second TCR subunit is the TCR β chain (eg, GenBank deposit number: CCI73893). In some embodiments, the first TCR subunit is a TCR β chain and the second TCR subunit is a TCR α chain. In some embodiments, the first TCR subunit is a TCR γ chain (for example, GenBank deposit number: AGE91788), and the second TCR subunit is a TCR delta chain (for example, GenBank deposit number: AAQ57272). In some embodiments, the first TCR subunit is a TCR delta chain, and the second TCR subunit is a TCR γ chain. In some embodiments, the first and / or second transmembrane domain individually comprises (such as consisting of) the transmembrane contained in any of the TCR subunit amino acid sequences of SEQ ID NO: 281-284 area. In some embodiments, the first and / or second transmembrane domain individually comprises (such as consisting of) any of the amino acid sequences of SEQ ID NO: 285-288. In some embodiments, the first TCRD further comprises a first connecting peptide at the amine end of the transmembrane domain and / or the second TCRD further comprises a second connecting peptide at the amine end of the transmembrane domain. In some embodiments, the first connecting peptide comprises all or part of the connecting peptide of the first TCR subunit and / or the second connecting peptide comprises all or part of the connecting peptide of the second TCR subunit. In some embodiments, the first and / or second linker peptide individually comprises (such as consisting of) all or part of any of the TCR subunit amino acid sequences of SEQ ID NO: 281-284 Linking peptides. In some embodiments, the first and / or second linker peptide individually comprises (such as consisting of) any one of the amino acid sequences of SEQ ID NO: 289-296. In some embodiments, the first TCRD further comprises a first TCR intracellular domain at the carboxy terminus of the first transmembrane domain and / or the second TCRD further comprises a second TCR intracellular domain at the carboxy terminus of the second transmembrane domain. In some embodiments, the first TCR intracellular domain includes all or a portion of the intracellular domain of the first TCR subunit and / or the second TCR intracellular domain includes all or a portion of the intracellular domain of the second TCR subunit. In some embodiments, the first and / or second TCR intracellular domain individually comprises (such as consisting of) all of the amino acid sequences contained in any of the TCR subunit amino acid sequences of SEQ ID NO: 281-284 Or part of the intracellular sequence. In some embodiments, the first and / or second TCR intracellular domain individually comprises (such as consisting of) any of the amino acid sequences of SEQ ID NO: 297-298. In some embodiments, the first TCRD is a fragment of the first TCR subunit and / or the second TCRD is a fragment of the second TCR chain. In some embodiments, the first and second polypeptide chains are linked, such as by covalent bonds (eg, peptide bonds or other chemical bonds) or non-covalent bonds. In some embodiments, the first and second TCRD are connected by disulfide bonds. In some embodiments, the first and second TCRD are connected by a disulfide bond between the residue in the first connecting peptide and the residue in the second connecting peptide. In some embodiments, TCRM can recruit at least one TCR-related signaling module selected from the group consisting of CD3δε, CD3γε, and ζζ. In some embodiments, TCRM is capable of recruiting each of CD3δε, CD3γε, and ζζ to form an octameric anti-RTMC abTCR-CD3 complex (ie, promote the formation of anti-RTMC abTCR-CD3 complex). In some embodiments, the anti-RTMC abTCR is a molecule comprising a fusion of an antibody portion and TCRM. In some embodiments, the anti-RTMC abTCR comprises a fusion of the first polypeptide chain of the Fab-like or Fv-like antigen binding module at the amine terminus of the first polypeptide chain of TCRM, thereby forming the first anti-RTMC abTCR A peptide chain; and a fusion of the second polypeptide chain of the Fab-like or Fv-like antigen binding module at the amine end of the second polypeptide chain of TCRM, thereby forming a second polypeptide chain that is anti-RTMC abTCR. In some embodiments, the anti-RTMC abTCR comprises a fusion of scFv at the amine terminus of the first or second polypeptide chain of TCRM. In some embodiments, the anti-RTMC abTCR further comprises a peptide linker between the first polypeptide chain of the Fab-like or Fv-like antigen binding module and the first polypeptide chain of the TCRM and / or the Fab-like or Fv-like A peptide linker between the second polypeptide chain of the antigen binding module and the second polypeptide chain of TCRM. In some embodiments, the anti-RTMC abTCR further comprises a peptide linker between the scFv of TCRM and the first or second polypeptide chain. In some embodiments, the length of the peptide linker is between about 5 to about 70 (such as about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, or 70) Any one, including any range between these values) amino acids. In some embodiments, the first polypeptide chain of anti-RTMC abTCR further includes an amine-terminal first signal peptide and / or the second polypeptide chain of anti-RTMC abTCR further includes an amine-terminal second signal peptide. In some embodiments, the first and / or second signal peptide comprises (such as consisting of the amino acid sequence of SEQ ID NO: 299. In some embodiments, the first polypeptide chain of the anti-RTMC abTCR further comprises the first accessory intracellular domain at the carboxyl terminus of the first transmembrane domain and / or the second polypeptide chain of the anti-RTMC abTCR further comprises the second span The second accessory intracellular domain at the carboxyl terminus of the membrane domain. In some embodiments, the first and / or second accessory intracellular domain comprises a TCR costimulatory domain. In some embodiments, the TCR costimulatory domain comprises all or part of the amino acid sequence of SEQ ID NO: 300. In some embodiments, the first and second polypeptide chains of the anti-RTMC abTCR are linked such as by covalent bonds (eg, peptide bonds or other chemical bonds) or non-covalent bonds. In some embodiments, the anti-RTMC abTCR is a heterodimer. Therefore, for example, in some embodiments, an anti-RTMC abTCR is provided, which comprises a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, And b) T cell receptor module (TCRM) capable of recruiting at least one TCR related signaling module. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the antibody portion is a Fab-like antigen binding module. In some embodiments, the antibody portion is an Fv-like antigen binding module. In some embodiments, the antibody portion is scFv. In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, the anti-RTMC antibody portion and at least one variant (such as at least 2, 3) of a variant of HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC antibody portion cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain, the extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising: HIV-1 RT 181 (SEQ ID NO: 5) , HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9) peptide and HLA-A * 02: 01, and b) T cell receptor module (TCRM) capable of recruiting at least one TCR related signaling module. In some embodiments, the antibody portion is a Fab-like antigen binding module. In some embodiments, the antibody portion is an Fv-like antigen binding module. In some embodiments, the antibody portion is scFv. In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, or up to about 3 (eg, any of about 1, 2 or 3) amines Variants of the amino acid substitution, including the HC-CDR2 of the amino acid sequence of any of SEQ ID NO: 241-244, or up to about 3 (eg, any of about 1, 2, or 3) ) Amino acid substituted variants thereof, and the HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg, about any of 1, 2, or 3) One) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 247-249, or comprising Up to about 3 (eg, about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253 , Or contain up to about 3 (eg About 2 or 3 according to any one of) the amino acid substituted variant thereof, and b) capable of raising at least one TCR signaling module associated T cell receptor module (TCRM). In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, HC- comprising the amino acid sequence of any of SEQ ID NO: 241-244 CDR2, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: comprising any one of SEQ ID NO: 247-249 LC-CDR1 of the amino acid sequence of the above, and LC-CDR3 containing the amino acid sequence of any one of SEQ ID NO: 250-253; and b) capable of recruiting at least one TCR-related signaling module T Cell Receptor Module (TCRM). In some embodiments, the antibody portion is a Fab-like antigen binding module. In some embodiments, the antibody portion is an Fv-like antigen binding module. In some embodiments, the antibody portion is scFv. In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion Comprising i) a heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NOs: 75-96, or up to about 5 (such as about 1, 2, 3, Any one of 4 or 5) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 97-124, or containing up to about 5 (such as about Any one of 1, 2, 3, 4 or 5) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 125-163, or comprising Up to about 5 (such as about any of 1, 2, 3, 4 or 5) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: comprising SEQ ID NO: 164- LC-CDR1 of the amino acid sequence of any one of 189, or a variant containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including SEQ ID NO: amino acid sequence of any one of 190-207 LC-CDR2, or variants containing up to about 3 (such as about any of 1, 2, or 3) amino acid substitutions, and amino groups containing any of SEQ ID NO: 208-239 LC-CDR3 of the acid sequence, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions; and b) capable of recruiting at least one TCR related signal The T cell receptor module (TCRM) of the conduction module. In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising any one of SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163, or up to about 5 (such as about 1, such as about 1, in the HC-CDR sequence) Any one of 2, 3, 4 or 5) amino acid substituted variants thereof; and ii) light chain variable domain sequence comprising: an amine comprising any of SEQ ID NO: 164-189 LC-CDR1 of the acid sequence; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and amino acid sequence of any one of SEQ ID NO: 208-239 LC-CDR3, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence; and b) capable of recruiting at least A TCR related signal conduction module T cell receptor module (TCRM). In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion Comprising i) a heavy chain variable domain sequence comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising any one of SEQ ID NO: 97-124 HC-CDR2 of the amino acid sequence; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163; and ii) light chain variable domain sequence comprising: comprising SEQ ID NO : LC-CDR1 of the amino acid sequence of any one of 164-189; LC-CDR2 including the amino acid sequence of any one of SEQ ID NO: 190-207; and comprising SEQ ID NO: 208- LC-CDR3 of the amino acid sequence of any one of 239; and b) T cell receptor module (TCRM) capable of recruiting at least one TCR related signaling module. In some embodiments, the antibody portion is a Fab-like antigen binding module. In some embodiments, the antibody portion is an Fv-like antigen binding module. In some embodiments, the antibody portion is scFv. In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion Comprising a heavy chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 19-46, or having at least about 95% (eg, at least about 96%, 97%, 98%, or 99% Any one) its variants of sequence identity, and the light chain variable domain, which comprise the amino acid sequence of any one of SEQ ID NOs: 47-74, or have at least about 95% (including, for example, at least about Any of 96%, 97%, 98% or 99%) variants of sequence identity; and b) a T cell receptor module (TCRM) capable of recruiting at least one TCR related signaling module. In some embodiments, there is provided an anti-RTMC abTCR comprising a) an extracellular domain comprising an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion Contains a heavy chain variable domain that includes the amino acid sequence of any one of SEQ ID NO: 19-46, and a light chain variable domain that includes the amine of any one of SEQ ID NO: 47-74 Acid sequence; and b) T cell receptor module (TCRM) capable of recruiting at least one TCR-related signaling module. In some embodiments, the antibody portion is a Fab-like antigen binding module. In some embodiments, the antibody portion is an Fv-like antigen binding module. In some embodiments, the antibody portion is scFv. For example, in some embodiments, the anti-RTMC abTCR includes an anti-RTMC antibody portion that contains heavy and light chain variable domains that include HC-CDR1 containing the following amino acid sequence , HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2, and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191 and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199, and 221, respectively, SEQ ID NO: 79, 110, 140, 164, 192, and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, SEQ ID NO: 80, 102, 153, 164, 192, and 232 respectively, SEQ ID NO: 93, 121, 154, 183, 204, and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, SEQ ID NO: 92, 108, 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, 173, 206, and 237, respectively, SEQ ID NO: 95, 123, 162, 188, 200 and 238, or SEQ ID NO: 96, 124, 163, 189, 207 and 239 respectively; or individually in HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1 and / or LC-CDR3 Include at most about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions and / or include at most about 3 (eg, about 1, 2 or 3) in the LC-CDR2 Either) Amino acid substituted variants thereof. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising HC-CDR1, HC-CDR2 containing the following amino acid sequence , HC-CDR3, LC-CDR1, LC-CDR2, and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, respectively And 209, SEQ ID NO: 77, 99, 127, 164, 192, and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193, and 211, SEQ ID NO: 79, 101, 129, respectively , 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80 , 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218 , Respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, SEQ ID NO: 85, 108, 142, 176, 192 and 208 respectively, SEQ ID NO: 80, 112, 143, 177, 191 and 223 respectively, SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 1 08, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238, Or SEQ ID NO: 96, 124, 163, 189, 207, and 239, respectively, or contain up to about 5 (such as about any of 1, 2, 3, 4, or 5) amines in the HC-CDR sequence Amino acid substitutions and / or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising HC-CDR1, HC-CDR2 containing the following amino acid sequence , HC-CDR3, LC-CDR1, LC-CDR2, and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, respectively And 209, SEQ ID NO: 77, 99, 127, 164, 192, and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193, and 211, SEQ ID NO: 79, 101, 129, respectively , 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80 , 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218 , Respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, SEQ ID NO: 85, 108, 142, 176, 192 and 208 respectively, SEQ ID NO: 80, 112, 143, 177, 191 and 223 respectively, SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191, and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191, and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199, and 228, respectively SEQ ID NO : 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192, and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204, and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238, or SEQ ID NO: 96, 124, 163, 189, 207, and 239, respectively. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising the following amino acid sequences: SEQ ID NO: 19 and 47, SEQ ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, SEQ ID NO: 23 and 51, SEQ ID NO: 24 and 47, respectively 52, SEQ ID NO: 25 and 53, respectively, SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, SEQ ID NO: 30 and 58, respectively, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and respectively 62, SEQ ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID NO: 38 and 66, SEQ ID NO: 39 and 62, respectively 67, SEQ ID NO: 40 and 68 respectively, SEQ ID NO: 41 and 69 respectively, SEQ ID NO: 42 and 70 respectively, SEQ ID NO: 43 and 71 respectively, SEQ ID NO: 44 and 72, SEQ ID NO: 45 and 73, respectively, or SEQ ID NO: 46 and 74, respectively Individually having at least about 95% (e.g. at least about 96%, 97%, 98%, or of any one of 99%) sequence identity to a variant thereof. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising the following amino acid sequences: SEQ ID NO: 19 and 47, SEQ ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, SEQ ID NO: 23 and 51, SEQ ID NO: 24 and 47, respectively 52, SEQ ID NO: 25 and 53, respectively, SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, SEQ ID NO: 30 and 58, respectively, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and respectively 62, SEQ ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID NO: 38 and 66, SEQ ID NO: 39 and 62, respectively 67, SEQ ID NO: 40 and 68 respectively, SEQ ID NO: 41 and 69 respectively, SEQ ID NO: 42 and 70 respectively, SEQ ID NO: 43 and 71 respectively, SEQ ID NO: 44 and 72, SEQ ID NO: 45 and 73, respectively, or SEQ ID NO: 46 and 74, respectively. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion comprising a heavy chain and light chain variable domain comprising: the amino acid sequences of SEQ ID NOs: 27 and 55 or individually having at least about 95 % (Eg, at least about any of 96%, 97%, 98%, or 99%) sequence variants thereof. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains comprising amino acid sequences of SEQ ID NOs: 27 and 55, respectively. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion containing heavy and light chain variable domains, the heavy and light chain variable domains comprising the amino acid sequences of SEQ ID NOs: 30 and 58, respectively Or a variant thereof that individually has at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, the anti-RTMC abTCR comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains comprising the amino acid sequences of SEQ ID NOs: 30 and 58, respectively. Also provided herein are effector cells (such as lymphocytes, such as T cells) that exhibit anti-RTMC chimeric receptors (such as anti-RTMC CAR or anti-RTMC abTCR). In addition, there is provided a method for preparing effector cells expressing anti-RTMC CAR or anti-RTMC abTCR, the method comprising introducing a vector containing a nucleic acid encoding anti-RTMC CAR or anti-RTMC abTCR into effector cells. In some embodiments, introducing the vector into the effector cell includes transducing the effector cell with the vector. In some embodiments, introducing the vector into the effector cell includes transfecting the effector cell with the vector. Vector transduction or transfection into effector cells can be performed using any method known in the art.Immunoconjugate In some embodiments, the anti-RTMC construct comprises an immunoconjugate containing an anti-RTMC antibody moiety attached to an effector molecule (also referred to herein as an "anti-RTMC immunoconjugate"). In some embodiments, the effector molecule is a therapeutic agent, such as a viral therapeutic agent, which is cytotoxic, cytostatic, or otherwise provides some therapeutic benefit. In some embodiments, the effector molecule is a label, which can directly or indirectly generate a detectable signal. In some embodiments, an anti-RTMC immunoconjugate (also referred to herein as an "antibody-drug conjugate" or "ADC") comprising an anti-RTMC antibody moiety and a therapeutic agent is provided. In some embodiments, the therapeutic agent is a toxin, which is cytotoxic, cytostatic, or otherwise prevents or reduces the ability of the target cell to divide. Use ADC to locally deliver cytotoxic agents or cell growth inhibitors, ie drugs that kill or inhibit tumor cells in cancer treatment (Syrigos and Epenetos, Anticancer Research 19: 605-614 (1999); Niculescu-Duvaz and Springer, Adv. Drg. Del. Rev. 26: 151 -172 (1997); U.S. Patent No. 4,975,278) allows partial delivery of drugs to target cells, and intracellular accumulation therein, in which systemic administration of these unconjugated therapeutic agents may Produces unacceptable levels of toxicity for normal cells and target cells that seek to eliminate (Baldwin et al., Lancet (March 15, 1986): 603-605 (1986); Thorpe, (1985) "Antibody Carriers Of Cytotoxic Agents In Cancer Therapy: A Review ", Monoclonal Antibodies '84: Biological And Clinical Applications, A. Pinchera et al. (Eds.), Pages 475-506). In order to seek the greatest efficacy and the least toxicity. Importantly, since most normal cells do not present RTMC on their surface, they cannot bind anti-RTMC immunoconjugates and are protected from the killing effect of toxins or other therapeutic agents. Therapeutic agents used in anti-RTMC immunoconjugates include, for example, daunomycin, doxorubicin, methotrexate, and vindesine (Rowland et al., Cancer Immunol. Immunother. 21: 183-187 (1986)). Toxins used in anti-RTMC immunoconjugates include bacterial toxins such as diphtheria toxin; plant toxins such as ricin; small molecule toxins such as geldanamycin (Mandler et al., J. Nat. Cancer Inst. 92 ( 19): 1573-1581 (2000); Mandler et al., Bioorganic & Med. Chem. Letters 10: 1025- 1028 (2000); Mandler et al., Bioconjugate Chem. 13: 786-791 (2002)) (EP 1391213; Liu et al., Proc. Natl. Acad. Sci. USA 93: 8618-8623 (1996)) and calicheamicin (Lode et al., Cancer Res. 58: 2928 (1998); Hinman et al. , Cancer Res. 53: 3336-3342 (1993)). Toxins can exert their cytotoxicity and cell growth inhibitory effects through mechanisms including tubulin binding, DNA binding, or topoisomerase inhibition. Some cytotoxic drugs tend to be inactive or weakly active when bound to larger antibodies or protein receptor ligands. Enzymatically active toxins and fragments thereof that can be used include, for example, diphtheria A chain, non-binding active fragments of diphtheria toxin, exotoxin A chain (from Pseudomonas aeruginosa), gabatoxin A chain, acacia toxin A chain, Modin A chain, α-sarcin, α-sarcin, Aleurites fordii protein, carnation protein, Phytolaca Americana protein (PAPI, PAPII and PAP-S), Momordica charantia inhibitor, curcin, crotin, sapaonaria officinalis inhibitor, gelonin, mitogellin, restrictedocin , Phenolmycin, inomycin (neomycin) and mycotoxin (tricothecene). See, for example, WO 93/21232 published on October 28, 1993. This article also covers anti-RTMC antibody parts and one or more small molecule toxins, such as calicheamicin, maytansinoids, dolastatin, aurostatin, crescent toxin and CC1065, and toxins Anti-RTMC immunoconjugates of derivatives of these active toxins. In some embodiments, an anti-RTMC immunoconjugate comprising a therapeutic agent having intracellular activity is provided. In some embodiments, the anti-RTMC immunoconjugate is internalized and the therapeutic agent is a cytotoxin that blocks cell protein synthesis, which causes cell death. In some embodiments, the therapeutic agent is a cytotoxin comprising a polypeptide having ribosome inactivating activity, including, for example, leukophyllin, bouganin, saporin, ricin, ricin A chain, Elemantin, diphtheria toxin, local aspergillin, Pseudomonas aeruginosa exotoxin A and its variants. In some embodiments, when the therapeutic agent is a cytotoxin comprising a polypeptide with ribosome inactivating activity, the anti-RTMC immunoconjugate must be internalized upon binding to the target cell to make the protein cytotoxic to the cell. In some embodiments, an anti-RTMC immunoconjugate comprising a therapeutic agent that acts to destroy DNA is provided. In some embodiments, the therapeutic agent that acts to destroy DNA is selected from the group consisting of enediynes (such as calicheamicin and esperamicin) and non-enediynes, for example. Molecular agents (eg bleomycin, methamphetyl-EDTA-Fe (II)). The invention further encompasses anti-RTMC immunoconjugates formed between anti-RTMC antibody moieties and compounds with nucleolytic activity (eg ribonuclease or DNA endonuclease, such as deoxyribonuclease; DNase). In some embodiments, the anti-RTMC immunoconjugate includes an agent that acts to disrupt tubulin. Such agents may include, for example, rhizostatin / maytansine, paclitaxel, vincristine and vinblastine, colchicine, auristatin poketoxin 10 MMAE, and peloruside A. In some embodiments, the anti-RTMC immunoconjugate comprises an alkylating agent, including, for example, Asaley NSC 167780, AZQ NSC 182986, BCNU NSC 409962, busulfan NSC 750, platinum carboxyphthalate NSC 271674, CBDCA NSC 241240, CCNU NSC 79037, CHIP NSC 256927, chlorambucil NSC 3088, chloramphenicol NSC 178248, cisplatin NSC 119875, chloroethene NSC 338947, cyano (N-morpholino) cranberry NSC 357704, plug Cyclodisone NSC 348948, Wecanol NSC 132313, Fludopan NSC 73754, Hepsulfam NSC 329680, Hydroxathion NSC 142982, Melphalan NSC 8806, Methyl CCNU NSC 95441, Mitosis Amycin C NSC 26980, Metazolamide NSC 353451, Nitrogen mustard NSC 762, PCNU NSC 95466, Piperazine NSC 344007, Piperazine dione NSC 135758, Piper bromide NSC 25154, Porferomycin NSC 56410, Spirohydantoin NSC 172112, teroxirone NSC 296934, tetraplatinum NSC 363812, thiotepa NSC 6396, triethylene melamine NSC 9706, uracil nitrogen mustard NSC 34462 and Yoshi-864 NSC 102627 . In some embodiments, the anti-RTMC immunoconjugate contains highly radioactive atoms. A variety of radioisotopes can be used to produce radioactively bound antibodies. Examples include²¹¹ At,¹³¹ I,¹²⁵ I,⁹⁰ Y,¹⁸⁶ Re,¹⁸⁸ Re,¹⁵³ Sm,²¹² Bi,³² P,²¹² Radioisotopes of Pb and Lu. In some embodiments, the anti-RTMC antibody portion may bind to a "receptor" (such as streptavidin) for use in where the antibody-receptor conjugate is administered to the patient to pre-target the tumor and then cleared using The agent removes unbound conjugate from circulation and then administers a "ligand" (eg, antibiotic protein) that binds to a cytotoxic agent (eg, radionucleotide). In some embodiments, the anti-RTMC immunoconjugate may comprise an anti-RTMC antibody moiety that binds to prodrug activating enzyme. In some such embodiments, the prodrug activating enzyme converts the prodrug into an active drug, such as an antiviral drug. In some embodiments, such anti-RTMC immunoconjugates are suitable for antibody-dependent enzyme-mediated prodrug therapy ("ADEPT"). Enzymes that can bind to antibodies include (but are not limited to) alkaline phosphatase, which is suitable for converting phosphate-containing prodrugs into free drugs; arylsulfatase, which is suitable for converting sulfate-containing prodrugs into free drugs ; Proteases, such as Serratia protease, thermolysin, protease, subtilisin, carboxypeptidase, and cathepsins (such as cathepsin B and L), which are suitable for converting peptide-containing prodrugs into free drugs; D-propylamine D-alanylcarboxypeptidases, which are suitable for the conversion of prodrugs containing D-amino acid substituents; carbohydrate-cleaving enzymes, such as β-galactose and neuraminidase, which are suitable for the conversion of sugar Basic prodrugs are converted into free drugs; β-lactamases, which are suitable for converting drugs derived from β-lactamase into free drugs; and penicillin acylases, such as penicillin V amidase and penicillin G amidase Aminase, which is suitable for the conversion of drugs derived from phenoxyacetyl or phenethylacetate on their amine nitrogen into free drugs. In some embodiments, the enzyme can be covalently bound to the antibody portion by recombinant DNA technology well known in the art. See, for example, Neuberger et al., Nature 312: 604-608 (1984). In some embodiments, the therapeutic portion of the anti-RTMC immunoconjugate can be a nucleic acid. Useful nucleic acids include, but are not limited to, antisense RNA, genes, or other polynucleotides, including nucleic acid analogs, such as thioguanine and thiopurine. The present application further provides an anti-RTMC immunoconjugate comprising an anti-RTMC antibody portion attached to an effector molecule, wherein the effector molecule is a label that can generate a detectable signal indirectly or directly. These anti-RTMC immunoconjugates can be used for research or diagnostic applications, such as for in vivo detection of cancer. The label preferably generates a detectable signal directly or indirectly. For example, the label may be radiopaque or radioisotope, such as³ H,¹⁴ C,³² P,³⁵ S,¹²³ I,¹²⁵ I,¹³¹ I; fluorescent (fluorophore) or chemiluminescent (chromophore) compounds, such as fluorescent isothiocyanate, rhodamine, or luciferin; enzymes, such as alkaline phosphatase, β-galactose, or spicy Root peroxidase; developer; or metal ion. In some embodiments, the label is a radioactive atom used for scintigraphy studies, for example⁹⁹ Tc or¹²³ I, or spin labels for nuclear magnetic resonance (NMR) imaging (also known as magnetic resonance imaging, MRI), such as zirconium-89, iodine-123, iodine-131, indium-111, fluorine-19, carbon-13 , Nitrogen-15, oxygen-17, gadolinium, manganese or iron. Zirconium-89 can be complexed with various metal chelating agents and bind to antibodies, for example for PET imaging (WO 2011/056983). In some embodiments, anti-RTMC immunoconjugates can be detected indirectly. For example, secondary antibodies specific for anti-RTMC immunoconjugates and containing detectable labels can be used to detect anti-RTMC immunoconjugates. Thus, for example, in some embodiments, an anti-RTMC immunoconjugate is provided that includes a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, and b) an effector molecule . In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, the effector molecule is covalently linked to the anti-RTMC antibody portion. In some embodiments, the effector molecule is a therapeutic agent selected from the group consisting of, for example, drugs, toxins, radioisotopes, proteins, peptides, and nucleic acids. In some embodiments, the effector molecule is a viral therapeutic agent. In some embodiments, the viral therapeutic agent is a highly radioactive atom selected from the group consisting of, for example:²¹¹ At,¹³¹ I,¹²⁵ I,⁹⁰ Y,¹⁸⁶ Re,¹⁸⁸ Re,¹⁵³ Sm,²¹² Bi,³² P and²¹² Pb. In some embodiments, the effector molecule is a label, which can directly or indirectly generate a detectable signal. In some embodiments, the label is a radioisotope selected from the group consisting of, for example:³ H,¹⁴ C,³² P,³⁵ S,¹²³ I,¹²⁵ I and¹³¹ I. In some embodiments, the anti-RTMC antibody portion is scFv. In some embodiments, the anti-RTMC antibody portion is human, humanized, or semi-synthetic. In some embodiments, the anti-RTMC antibody portion and at least one variant (such as at least 2, 3) of a variant of HIV-1 RT peptide comprising an MHC class I protein and an amino acid substitution (such as a conservative amino acid substitution) , Any of 4, 5, or 6) complex cross reaction. In some embodiments, the anti-RTMC antibody portion cross-reacts with at least one complex (such as at least any one of 2, 3, 4, or 5) of different isoforms including HIV-1 RT peptide and MHC class I protein. In some embodiments, there is provided an anti-RTMC immunoconjugate comprising a) an anti-RTMC antibody portion that specifically binds to a complex comprising: HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO : 9) Peptide and HLA-A * 02: 01, and b) effector molecule. In some embodiments, the effector molecule is covalently linked to the anti-RTMC antibody portion. In some embodiments, the effector molecule is a therapeutic agent selected from the group consisting of, for example, drugs, toxins, radioisotopes, proteins, peptides, and nucleic acids. In some embodiments, the effector molecule is a viral therapeutic agent. In some embodiments, the viral therapeutic agent is a highly radioactive atom selected from the group consisting of, for example:²¹¹ At,¹³¹ I,¹²⁵ I,⁹⁰ Y,¹⁸⁶ Re,¹⁸⁸ Re,¹⁵³ Sm,²¹² Bi,³² P and²¹² Pb. In some embodiments, the effector molecule is a label, which can directly or indirectly generate a detectable signal. In some embodiments, the label is a radioisotope selected from the group consisting of, for example:³ H,¹⁴ C,³² P,³⁵ S,¹²³ I,¹²⁵ I and¹³¹ I. In some embodiments, the anti-RTMC antibody portion is scFv. In some embodiments, the anti-RTMC antibody portion is human, humanized, or semi-synthetic. In some embodiments, a multispecific anti-RTMC immunoconjugate is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising : I) heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, or comprising up to about 3 (eg, about any of 1, 2, or 3) amines Variants of the amino acid substitution, including the HC-CDR2 of the amino acid sequence of any of SEQ ID NO: 241-244, or up to about 3 (eg, any of about 1, 2, or 3) ) Amino acid substituted variants thereof, and the HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 245-246, or up to about 3 (eg, about 1, 2 or 3) Any one) an amino acid substituted variant thereof; and ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 247-249, or comprising Up to about 3 (eg, about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 250-253 , Or contain up to about 3 (eg about 1, 2 Substituted to any one of 3) of amino acid variant thereof, and b) an effector molecule. In some embodiments, a multispecific anti-RTMC immunoconjugate is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising : I) heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of SEQ ID NO: 240, HC- comprising the amino acid sequence of any one of SEQ ID NO: 241-244 CDR2, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 245-246; and ii) a light chain variable domain comprising: comprising any one of SEQ ID NO: 247-249 LC-CDR1 of the amino acid sequence of the above, and LC-CDR3 including the amino acid sequence of any one of SEQ ID NO: 250-253, and b) the effector molecule. In some embodiments, an anti-RTMC immunoconjugate is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising: i) Heavy chain variable domain comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96, or up to about 5 (such as about 1, 2, 3, 4 or 5 Any one of them) amino acid substituted variants thereof, comprising the HC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 97-124, or containing up to about 5 (such as about 1, 2 , Any of 3, 4 or 5) amino acid substituted variants thereof, and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 125-163, or comprising up to about 5 (Such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and ii) a light chain variable domain comprising: comprising SEQ ID NO: 164-189 LC-CDR1 of the amino acid sequence of any one, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions, including SEQ ID NO : LC-CDR2 of the amino acid sequence of any one of 190-207, or containing More than 3 (such as about any of 1, 2, or 3) amino acid substituted variants thereof, and LC-CDR3 comprising the amino acid sequence of any of SEQ ID NO: 208-239 , Or contain up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substituted variants thereof; and b) effector molecules. In some embodiments, an anti-RTMC immunoconjugate is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising: i) Heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising the amino acid of any one of SEQ ID NO: 97-124 HC-CDR2 of the sequence; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 125-163, or up to about 5 (such as about 1, 2, 3) in the HC-CDR sequence , Any of 4 or 5) amino acid substituted variants thereof; and ii) light chain variable domain sequence comprising: an amino acid sequence comprising any of SEQ ID NO: 164-189 LC-CDR1; LC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 190-207; and LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 208-239 CDR3, or variants containing up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions in the LC-CDR sequence; and b) effector molecules. In some embodiments, an anti-RTMC immunoconjugate is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion comprising: i) Heavy chain variable domain sequence, comprising: HC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 75-96; comprising the amino acid of any one of SEQ ID NO: 97-124 HC-CDR2 of the sequence; and HC-CDR3 comprising the amino acid sequence of any one of SEQ ID NO: 125-163; and ii) a light chain variable domain sequence comprising: comprising SEQ ID NO: 164- LC-CDR1 of the amino acid sequence of any one of 189; LC-CDR2 of the amino acid sequence of any one of SEQ ID NO: 190-207; and of SEQ ID NO: 208-239 LC-CDR3 of the amino acid sequence of any one; and b) effector molecule. In some embodiments, an anti-RTMC immunoconjugate is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion includes a heavy chain A variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 19-46, or having at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) Variants of sequence identity, and light chain variable domains, which comprise the amino acid sequence of any one of SEQ ID NOs: 47-74, or have at least about 95% (including, for example, at least about 96%, 97 Any of%, 98%, or 99%) variants of sequence identity; and b) effector molecules. In some embodiments, an anti-RTMC immunoconjugate is provided, comprising: a) an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, the antibody portion includes a heavy chain The variable domain, which includes the amino acid sequence of any one of SEQ ID NO: 19-46, and the light chain variable domain, which includes the amino acid sequence of any one of SEQ ID NO: 47-74; And b) effector molecules. For example, in some embodiments, the anti-RTMC immunoconjugate includes an anti-RTMC antibody portion that includes HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC containing the following amino acid sequence -CDR2 and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190, and 208, respectively, SEQ ID NO: 76, 98, 126, 165, 191, and 209, SEQ ID NO: 77, respectively , 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215 , Respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169 , 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109 , 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139 , 174, 199 and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85 , 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227 , Respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176 , 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102 , 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO : 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 2 00 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, 173, 206, and 237, respectively, SEQ ID NO: 95, 123, 162, 188, 200, and 238, or SEQ ID NO, respectively : 96, 124, 163, 189, 207 and 239; or HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1 and / or LC-CDR3 individually contain up to about 5 (eg about 1, 2 , Any of 3, 4 or 5) amino acid substitutions and / or changes in the LC-CDR2 comprising up to about 3 (e.g. about any of 1, 2, or 3) amino acid substitutions body. In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising HC-CDR1, HC containing the following amino acid sequence -CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively, SEQ ID NO: 76, 98, 126, 165 respectively , 191 and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101 , 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO : 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 And 218, SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, SEQ ID NO: 88, 113, 144, respectively 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, SEQ ID NO: 80, 102, 153, 164, 192, and 232, SEQ ID NO: 93, 121, 154, 183, 204, and 233, respectively, SEQ ID NO: 92, 120, 155, 184, 191, and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192, and 234, respectively SEQ I D NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236 , SEQ ID NO: 92, 108, 160, 177, 191, and 218, respectively, SEQ ID NO: 94, 122, 161, 173, 206, and 237, respectively SEQ ID NO: 95, 123, 162, 188 , 200 and 238 or SEQ ID NO: 96, 124, 163, 189, 207 and 239, respectively, or up to about 5 (such as about any of 1, 2, 3, 4 or 5 in the HC-CDR sequence One) amino acid substitutions and / or variants comprising up to about 5 (such as about any of 1, 2, 3, 4 or 5) amino acid substitutions in the LC-CDR sequence. In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising HC-CDR1, HC containing the following amino acid sequence -CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively, SEQ ID NO: 76, 98, 126, 165 respectively , 191 and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101 , 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO : 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169, 191 And 218, SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, SEQ ID NO: 80, 102, 153, 164, 192, and 232, SEQ ID NO: 93, 121, 154, 183, 204, and 233, respectively, SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID N O: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, SEQ ID NO: 92, 108, 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, 173, 206, and 237, respectively, SEQ ID NO: 95, 123, 162, 188, 200 and 238, or SEQ ID NO: 96, 124, 163, 189, 207, and 239, respectively. In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising the following amino acid sequences: SEQ ID NO: respectively: 19 and 47, respectively SEQ ID NO: 20 and 48, respectively SEQ ID NO: 21 and 49, respectively SEQ ID NO: 22 and 50, respectively SEQ ID NO: 23 and 51, respectively SEQ ID NO: 24 and 52, SEQ ID NO: 25 and 53, respectively, SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, respectively SEQ ID NO: 30 and 58, respectively SEQ ID NO: 31 and 59, respectively SEQ ID NO: 32 and 60, respectively SEQ ID NO: 33 and 61, respectively SEQ ID NO: 34 and 62, respectively SEQ ID NO: 35 and 63, respectively SEQ ID NO: 36 and 64, respectively SEQ ID NO: 37 and 65, respectively SEQ ID NO: 38 and 66, respectively SEQ ID NO: 39 and 67, respectively SEQ ID NO: 40 and 68, respectively SEQ ID NO: 41 and 69, respectively SEQ ID NO: 42 and 70, respectively SEQ ID NO: 43 and 71, respectively SEQ ID NO: 44 and 72, SEQ ID NO: 45 and 73, respectively, or SEQ ID NO: 46, respectively 74, individually or at least about 95% (e.g. at least about 96%, 97%, 98%, or of any one of 99%) sequence identity to a variant thereof. In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising the following amino acid sequences: SEQ ID NO: respectively: 19 and 47, respectively SEQ ID NO: 20 and 48, respectively SEQ ID NO: 21 and 49, respectively SEQ ID NO: 22 and 50, respectively SEQ ID NO: 23 and 51, respectively SEQ ID NO: 24 and 52, SEQ ID NO: 25 and 53, respectively, SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, respectively SEQ ID NO: 35 and 63, respectively SEQ ID NO: 36 and 64, respectively SEQ ID NO: 37 and 65, respectively SEQ ID NO: 38 and 66, respectively SEQ ID NO: 39 and 67, respectively SEQ ID NO: 40 and 68, respectively SEQ ID NO: 41 and 69, respectively SEQ ID NO: 42 and 70, respectively SEQ ID NO: 43 and 71, respectively SEQ ID NO: 44 and 72, SEQ ID NO: 45 and 73, respectively, or SEQ ID NO: 46, respectively 74. In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion containing a heavy chain light chain variable domain, the heavy chain and light chain variable domains comprising the amino acid sequences of SEQ ID NOs: 27 and 55, respectively, Or a variant thereof that individually has at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising the amino acid sequences of SEQ ID NOs: 27 and 55, respectively . In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains, the heavy and light chain variable domains comprising the amino acid sequences of SEQ ID NOs: 30 and 58, respectively , Or variants thereof that individually have at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, the anti-RTMC immunoconjugate comprises an anti-RTMC antibody portion comprising heavy and light chain variable domains comprising amino acid sequences of SEQ ID NOs: 30 and 58, respectively.Nucleic acid Nucleic acid molecules encoding anti-RTMC constructs or anti-RTMC antibody portions are also covered. In some embodiments, nucleic acids (or nucleic acid collections) encoding full-length anti-RTMC antibodies are provided. In some embodiments, nucleic acids encoding multispecific anti-RTMC molecules (eg, multispecific anti-RTMC antibodies, bispecific anti-RTMC antibodies, or bispecific T cell junction molecule anti-RTMC antibodies) or polypeptide portions thereof are provided (or Nucleic acid collection). In some embodiments, a nucleic acid (or nucleic acid collection) encoding anti-RTMC CAR or anti-RTMC abTCR is provided. In some embodiments, a nucleic acid (or collection of nucleic acids) encoding an anti-RTMC immunoconjugate, or a polypeptide portion thereof is provided. This application also includes variants of these nucleic acid sequences. For example, variants include nucleotide sequences that hybridize to nucleic acid sequences encoding anti-RTMC constructs or anti-RTMC antibody portions of the present application under at least moderately stringent hybridization conditions. The present invention also provides a vector into which the nucleic acid of the present invention is inserted. In short, the expression of an anti-RTMC construct (eg, anti-RTMC CAR or anti-RTMC abTCR) or a polypeptide portion thereof by a natural or synthetic nucleic acid encoding an anti-RTMC construct or a polypeptide portion thereof can be performed by inserting the nucleic acid into an appropriate expression This is achieved in the vector so that the nucleic acid is operably linked to 5 'and 3' regulatory elements, including, for example, promoters (eg, lymphocyte-specific promoters) and 3 'untranslated regions (UTR). The vector may be suitable for replication and integration in eukaryotic host cells. Typical selection and expression vectors contain transcription and translation terminators, an initiation sequence, and a promoter suitable for regulating the expression of the desired nucleic acid sequence. The nucleic acid of the present invention can also be used for nucleic acid immunization and gene therapy using standard gene delivery protocols. Gene delivery methods are known in the art. See, for example, US Patent Nos. 5,399,346, 5,580,859, and 5,589,466, which are incorporated herein by reference in their entirety. In some embodiments, the present invention provides gene therapy vectors. Nucleic acids can be cloned into various types of vectors. For example, nucleic acids can be cloned into vectors including, but not limited to, plastids, phagemids, phage derivatives, animal viruses, and slime bodies. Vectors of particular interest include expression vectors, replication vectors, probe generation vectors, and sequencing vectors. In addition, the expression vector can be provided to the cell in the form of a viral vector. Viral vector technology is well known in the art and described in, for example, Sambrook et al. (2001, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, New York) and other manuals in virology and molecular biology. Viruses suitable as vectors include, but are not limited to, retroviruses, adenoviruses, adeno-associated viruses, herpes viruses, and lentiviruses. In general, suitable vectors contain an origin of replication that functions in at least one organism, a promoter sequence, a suitable restriction endonuclease site, and one or more selectable markers (see for example WO 01/96584; WO 01/29058; and US Patent No. 6,326,193). Several virus-based systems have been developed for gene transfer to mammalian cells. For example, retroviruses provide a suitable platform for gene delivery systems. The selected gene can be inserted into a vector and encapsulated in retroviral particles using techniques known in the art. The recombinant virus can then be isolated and delivered to the individual's cells in vivo or ex vivo. Many retrovirus systems are known in the art. In some embodiments, adenovirus vectors are used. Various adenovirus vectors are known in the art. In some embodiments, lentiviral vectors are used. Vectors derived from retroviruses (such as lentiviruses) are suitable tools for achieving long-term gene transfer because they allow long-term stable integration of transgenic genes and their propagation in daughter cells. Lentiviral vectors have the additional advantage over vectors derived from oncogenic retroviruses, such as murine leukemia viruses, because they can transduce non-proliferative cells, such as hepatocytes. It also has the additional advantage of low immunogenicity. Additional promoter elements (eg, enhancers) regulate the frequency of transcription initiation. Generally, these elements are located in the 30-110 bp region upstream of the start site, although multiple promoters have recently been shown to contain functional elements also downstream of the start site. The spacing between promoter elements is usually flexible so that the promoter function is preserved when the elements are inverted or moved relative to each other. In the thymidine kinase (tk) promoter, the spacing between promoter elements can be increased to 50 bp apart before activity begins to decline. An example of a suitable promoter is the immediate early cytomegalovirus (CMV) promoter sequence. This promoter sequence is a strong constitutive promoter sequence capable of driving a high performance level of any polynucleotide sequence operably linked thereto. Another example of a suitable promoter is elongation growth factor-1α (EF-1α). However, other constitutive promoter sequences may also be used, including (but not limited to) monkey virus 40 (SV40) early promoter, mouse mammary tumor virus (MMTV), human immunodeficiency virus (HIV) long terminal repeat sequence (LTR) ) Promoter, MoMuLV promoter, avian leukemia virus promoter, Epstein-Barr virus immediate early promoter, Rous sarcoma virus promoter, and human gene promoter, Such as (but not limited to) the actin promoter, myosin promoter, heme promoter and creatine kinase promoter. Furthermore, the invention should not be limited to the use of constitutive promoters. Inducible promoters are also covered as part of the invention. The use of an inducible promoter provides a molecular switch that can turn on the expression of the polynucleotide sequence to which it is operably linked when such expression is needed or turn off the expression when expression is not needed. Examples of inducible promoters include, but are not limited to, metallothionein promoter, glucocorticoid promoter, progesterone promoter, and tetracycline promoter. In order to assess the performance of the polypeptide or part thereof, the expression vector to be introduced into the cell may also contain selectable marker genes or reporter genes or both to facilitate identification and selection of expression cells from the cell population managed to be transfected or infected with the viral vector. In other aspects, selectable markers can be carried on separate DNA segments and used in co-transfection procedures. Both selectable markers and reporter genes can be flanked by appropriate regulatory sequences to enable expression in host cells. Useful selectable markers include, for example, antibiotic resistance genes, such as neo and the like. Reporter genes are used to identify potential transfected cells and assess the function of regulatory sequences. In general, a reporter gene is a gene that does not exist or is present in the recipient organism or tissue and encodes a polypeptide that is manifested by some easily detectable characteristics (such as enzymatic activity). The performance of the reporter gene is analyzed at a suitable time after the DNA has been introduced into the recipient cell. Suitable reporter genes may include genes encoding luciferase, β-galactose, chloramphenicol acetyltransferase, secreted alkaline phosphatase or green fluorescent protein genes (e.g. Ui-Tel et al., 2000 FEBS Letters 479 : 79-82). Suitable performance systems are well known and can be prepared using known techniques or commercially available. In general, the construct with the smallest 5 'flanking region displaying the highest performance level of the reporter gene is identified as a promoter. Such a promoter region can be linked to a reporter gene and used to assess reagents that regulate the ability of promoter-driven transcription. Methods for introducing and expressing genes into cells are known in the art. In the context of expression vectors, vectors can be easily introduced into host cells, such as mammalian, bacterial, yeast, or insect cells, by any method in the art. For example, the expression vector can be transferred to the host cell by physical, chemical or biological means. Physical methods for introducing polynucleotides into host cells include calcium phosphate precipitation, liposome transfection, particle bombardment, microinjection, electroporation, and similar methods. Methods for manufacturing cells containing vectors and / or exogenous nucleic acids are well known in the art. See, for example, Sambrook et al. (2001, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, New York). In some embodiments, the introduction of the polynucleotide into the host cell is performed by calcium phosphate transfection. Biological methods for introducing polynucleotides of interest into host cells include the use of DNA and RNA vectors. Viral vectors and especially retroviral vectors have become the most widely used method for inserting genes into mammalian (eg, human) cells. Other viral vectors may be derived from lentivirus, poxvirus, herpes simplex virus type 1, adenovirus and adeno-associated virus and similar viruses. See, for example, US Patent Nos. 5,350,674 and 5,585,362. Chemical methods used to introduce polynucleotides into host cells include colloidal dispersion systems, such as macromolecular complexes, nanocapsules, microspheres, beads, and lipid-based systems, including oil-in-water emulsions, microspheres Cells, mixed microcells and liposomes. An exemplary colloidal system for delivery in vitro and in vivo is a liposome (eg, artificial membrane vesicle). In the case of using a non-viral delivery system, an exemplary delivery vehicle is a liposome. The use of lipid formulations is expected to introduce nucleic acids into host cells (in vitro, ex vivo, or in vivo). In another aspect, the nucleic acid can bind to the lipid. The nucleic acid bound to the lipid can be encapsulated in the aqueous interior of the liposome, interspersed in the lipid bilayer of the liposome, attached to the liposome via a linking molecule combined with the liposome and the oligonucleotide, and coated with Liposomes, complexed with liposomes, dispersed in a solution containing lipids, mixed with lipids, combined with lipids, contained in lipids in the form of a suspension, containing or complexed with microcells, or otherwise combined with lipid phase Combine. The combination of lipid, lipid / DNA or lipid / expression carrier is not limited to any specific structure in solution. For example, it can exist in a double-layer structure, in the form of microcells or have a "collapsed" structure. It can also be simply interspersed in the solution, possibly forming aggregates that are not uniform in size or shape. Lipids are fatty substances that can be naturally occurring lipids or synthetic lipids. For example, lipids include fat droplets that naturally occur in the cytoplasm and classes of compounds containing long-chain aliphatic hydrocarbons and their derivatives (such as fatty acids, alcohols, amines, amino alcohols, and aldehydes). Regardless of the method used to introduce the exogenous nucleic acid into the host cell or otherwise expose the cell to the inhibitor of the present invention, various analyses can be performed to confirm the presence of the recombinant DNA sequence in the host cell. Such analysis includes, for example, "molecular biology" analysis known to those skilled in the art, such as southern and northern blotting, RT-PCR, and PCR; "biochemical" analysis, such as detecting the presence or absence of specific peptides, for example Reagents within the scope of the present invention are identified by immunological means (ELISA and Western blotting) or by the analysis described herein.MHC I Protein-like MHC class I proteins are one of two major classes of major histocompatibility complex (MHC) molecules (the other is MHC class II) and are found on almost every nucleated cell in the body. Its function is to display protein fragments from cells to T cells; healthy cells will be ignored, and cells containing foreign proteins will be attacked by the immune system. Since MHC class I proteins present peptides derived from cytosolic proteins, the MHC class I presentation pathway is often referred to as the cytosolic or endogenous pathway. Class I MHC molecules bind peptides mainly produced by the degradation of cytosolic proteins (via proteasomes). The MHC I: peptide complex is then inserted into the plasma membrane of the cell. The peptide binds to the extracellular part of the MHC class I molecule. Therefore, the function of Class I MHC is to present intracellular proteins to cytotoxic T cells (CTL). However, MHC class I can also present peptides produced from foreign proteins in a method called cross-presentation. MHC class I protein consists of two polypeptide chains: α and β2-microglobulin (β2M). The two chains are non-covalently connected via the interaction of b2m and α3 domains. Only the alpha chain is polymorphic and encoded by the HLA gene, while the b2m subunit is not polymorphic and is encoded by the beta-2 microglobulin gene. The α3 domain spans the plasma membrane and interacts with the CD8 co-receptor of T cells. The α3-CD8 interaction keeps the MHC I molecule in place, while the T cell receptor (TCR) on the surface of the cytotoxic T cell binds to its α1-α2 heterodimer ligand and checks the antigenicity of the coupled peptide . The α1 and α2 domains fold to form grooves for peptide binding. MHC class I proteins bind peptides with a length of 8-10 amino acids. The human leukocyte antigen (HLA) gene is a human type of MHC gene. The three main MHC class I proteins in the human body are HLA-A, HLA-B and HLA-C, and the three minor MHC class I proteins are HLA-E, HLA-F and HLA-G. HLA-A is among the genes with the fastest evolutionary coding sequences in humans. As of December 2013, there were 2,432 known HLA-A alleles encoding 1,740 active proteins and 117 knockout proteins. The HLA-A gene is located on the short arm of chromosome 6 and encodes the larger alpha chain component of HLA-A. Changes in the HLA-A α-chain are essential for HLA function. This change promotes genetic diversity in the population. Because each HLA has different affinity for certain structural peptides, more HLA means more antigens are "presented" on the cell surface, increasing the likelihood that the population subgroup will be resistant to any given foreign invader. This reduces the possibility that a single pathogen has the ability to eliminate the entire human population. Individuals can express up to two types of HLA-A, each from their parents. Some individuals will inherit the same HLA-A from their parents, reducing their individual HLA diversity; however, most individuals will receive two different copies of HLA-A. All HLA groups follow this same pattern. In other words, an individual may only express one or both of the 2432 known HLA-A alleles. All alleles are classified with at least four digit codes, such as HLA-A * 02: 12. A represents the HLA gene to which the dual gene belongs. Because there are many HLA-A alleles, the classification is simplified by serotype classification. The next pair of numbers indicates the result of this allocation. For example, HLA-A * 02: 02, HLA-A * 02: 04 and HLA-A * 02: 324 are all members of the A2 serotype (denoted by the prefix * 02). This group is the main factor responsible for HLA compatibility. All the following figures cannot be delineated by genetic sequencing by serotyping. The second set of numbers represents what HLA protein is produced. These are designated in the order of discovery and as of December 2013, there are 456 different known HLA-A02 proteins (designated names HLA-A * 02: 01 to HLA-A * 02: 456). The shortest possible HLA name includes all two of these details, and each extension beyond the name indicates that the nucleotide changes may or may not change the protein. In some embodiments, the anti-RTMC antibody portion specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, wherein the MHC class I protein is HLA-A, HLA-B, HLA-C, HLA-E , HLA-F or HLA-G. In some embodiments, the MHC class I protein is HLA-A, HLA-B, or HLA-C. In some embodiments, the MHC class I protein is HLA-A. In some embodiments, the MHC class I protein is HLA-B. In some embodiments, the MHC class I protein is HLA-C. In some embodiments, the MHC class I protein is HLA-A01, HLA-A02, HLA-A03, HLA-A09, HLA-A10, HLA-A11, HLA-A19, HLA-A23, HLA-A24, HLA-A25 , HLA-A26, HLA-A28, HLA-A29, HLA-A30, HLA-A31, HLA-A32, HLA-A33, HLA-A34, HLA-A36, HLA-A43, HLA-A66, HLA-A68, HLA -A69, HLA-A74 or HLA-A80. In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is any one of HLA-A * 02: 01-555, such as HLA-A * 02: 01, HLA-A * 02: 02, HLA-A * 02: 03 , HLA-A * 02: 04, HLA-A * 02: 05, HLA-A * 02: 06, HLA-A * 02: 07, HLA-A * 02: 08, HLA-A * 02: 09, HLA -A * 02: 10, HLA-A * 02: 11, HLA-A * 02: 12, HLA-A * 02: 13, HLA-A * 02: 14, HLA-A * 02: 15, HLA-A * 02: 16, HLA-A * 02: 17, HLA-A * 02: 18, HLA-A * 02: 19, HLA-A * 02: 20, HLA-A * 02: 21, HLA-A * 02 : 22 or HLA-A * 02: 24. In some embodiments, the MHC class I protein is HLA-A * 02: 01. HLA-A * 02: 01 is expressed in 39-46% of all Caucasians, and therefore represents a suitable choice for the MHC class I protein used in the present invention. HIV-1 RT peptides suitable for the production of anti-RTMC antibody portions can be based on, for example, HLA-A * 02: 01 binding motifs and cleavage sites of proteasomes and immunoproteasomes using computer prediction models known to those skilled in the art Exist. For predicting MHC binding sites, such models include (but are not limited to) IEDB (Vita et al., The immune epitope database (IEDB) 3.0.Nucleic Acids Res . October 9, 2014. pii: gku938), ProPred1 (described in more detail in Singh and Raghava,ProPred : prediction of HLA - DR binding sites . BIOINFORMATICS 17 (12): 1236-1237, 2001) and SYFPEITHI (see Schuler et al.SYFPEITHI , Database for Searching and T - Cell Epitope Prediction . Immunoinformatics Methods in Molecular Biology , Volume 409 (1): 75-93, 2007). Once the appropriate peptide is identified, peptide synthesis can be completed according to protocols well known to those skilled in the art. Due to its relatively small size, the peptides of the present invention can be synthesized directly in solution or on a solid support according to conventional peptide synthesis techniques. Various automatic synthesizers are commercially available and can be used according to known protocols. The synthesis of peptides in the solution phase has become an accepted procedure for the synthesis of peptides for large-scale production and is therefore a suitable alternative method for preparing the peptides of the present invention (see for example Solid Phase Peptide Synthesis, John Morrow Stewart and Martin et al.Application of Almez - mediated Amidation Reactions to Solution Phase Peptide Synthesis , Tetrahedron Letters Volume 39, pages 1517--1520, 1998). The binding activity of the candidate HIV-1 RT peptide can be tested using an antigen processing-deficient T2 cell line, which increases the performance of HLA-A when stabilized by the peptide in the antigen presentation groove. T2 cells are pulsed with candidate peptides for a time sufficient to stabilize HLA-A on the cell surface, which can be measured using any method known in the art, such as by using fluorescent labels specific for HLA-A Immunostaining of monoclonal antibodies (eg BB7.2) followed by fluorescence activated cell sorting (FACS) analysis.Preparation of anti RTMC Antibodies and anti RTMC Antibody section In some embodiments, the anti-RTMC antibody or anti-RTMC antibody portion is a monoclonal antibody. Monoclonal antibodies can, for example, use fusion tumor methods such as those described by Kohler and Milstein, Nature, 256: 495 (1975) and Sergeeva et al., Blood, 117 (16): 4262-4272, using the methods described herein and in the examples below Phage display method, or prepared using recombinant DNA method (see, eg, US Patent No. 4,816,567). In the fusion tumor method, hamsters, mice, or other suitable host animals are usually immunized with an immunological agent to produce lymphocytes, which produce or are capable of producing antibodies that will specifically bind to the immunological agent.Alternatively, lymphocytes can be immunized in vitro. Immunological agents may include fusion proteins of polypeptides or related proteins, or complexes containing at least two molecules, such as complexes containing HIV-1 RT peptides and MHC class I proteins. In general, if cells of human origin are required, peripheral blood lymphocytes ("PBL") are used; or if cells of non-human mammal origin are required, spleen cells or lymph node cells are used. Lymphocytes are then fused with immortalized cell lines using a suitable fusion agent (such as polyethylene glycol) to form fused tumor cells. See, for example, Goding, Monoclonal Antibodies: Principles and Practice (New York: Academic Press, 1986), pages 59-103. Immortalized cell lines are usually transformed mammalian cells, specifically myeloma cells of rodent, bovine, and human origin. Usually, rat or mouse myeloma cell lines are used. Fused tumor cells can be cultured in a suitable medium that preferably contains one or more substances that inhibit the growth or survival of unfused, immortalized cells. For example, if the parent cell lacks the enzyme hypoxanthine-guanine phosphoribosyl transferase (HGPRT or HPRT), the medium used for fusion tumors will usually include hypoxanthine, aminopterin, and thymidine HAT medium ”), which prevents the growth of cells lacking HGPRT. In some embodiments, the immortalized cell lines are efficiently fused to support stable high-level performance of antibodies by the selected antibody-producing cells and are sensitive to culture media such as HAT medium. In some embodiments, the immortalized cell line is a murine myeloma cell line, which can be obtained, for example, from Salk Institute Cell Distribution Center, San Diego, California and American Type Culture Collection, Manassas, Virginia. Human myeloma and mouse-human fusion myeloma cell lines have also been described for the preparation of human monoclonal antibodies. Kozbor,J . Immunol . , 133: 3001 (1984); and Brodeur et al., Monoclonal Antibody Production Techniques and Applications (Marcel Dekker, Inc., New York, 1987) pages 51-63. The media for culturing the fusion tumor cells can then be analyzed for the presence of monoclonal antibodies directed against the polypeptide. The binding specificity of monoclonal antibodies produced by fused tumor cells can be determined by immunoprecipitation or by in vitro binding analysis, such as radioimmunoassay (RIA) or enzyme-linked immunosorbent assay (ELISA). These techniques and analytical methods are known in the art. The binding affinity of monoclonal antibodies can be, for example, by Munson and Pollard,Anal . Biochem . , 107: 220 (1980) by Scatchard analysis. After identifying the desired fusion tumor cells, pure lines can be sub-colonized by limiting dilution procedures and grown by standard methods.Goding, Aforementioned. Suitable media for this purpose include, for example, Dulbecco's Modified Eagle's Medium and RPMI-1640 medium. Alternatively, the fusion tumor cells can be grown in vivo in mammals in the form of ascites fluid. Monoclonal antibodies secreted by sub-pure lines can be separated from the culture medium or ascites fluid by conventional immunoglobulin purification procedures (such as protein A-agarose, hydroxyapatite chromatography, gel electrophoresis, dialysis, or affinity chromatography) or purification. Anti-RTMC antibodies or antibody portions can also be identified by screening combinatorial libraries against antibodies with one or more desired activities. For example, various methods are known in the art for generating phage display libraries and screening such libraries for antibodies with desired binding characteristics. Such methods are reviewed in, for example, Hoogenboom et al., Methods in Molecular Biology 178: 1-37 (edited by O'Brien et al., Human Press, Totowa, N.J, 2001), and further described in, for example, McCafferty et al.,Nature 348: 552-554; Clackson et al.,Nature 352: 624-628 (1991); Marks et al.,J . Mol . Biol . 222: 581-597 (1992); Marks and Bradbury,Methods in Molecular Biology 248: 161-175 (Ed. Lo, Human Press, Totowa, N.J, 2003); Sidhu et al.,J . Mol . Biol . 338 (2): 299-310 (2004); Lee et al.,J . Mol . Biol . 340 (5): 1073-1093 (2004); Fellouse,Proc . Natl . Acad . Sci . USA 101 (34): 12467-12472 (2004); and Lee et al.,J . Immunol . Methods 284 (1-2): 119-132 (2004). In some phage presentation methods, V_H And V_L The pedigrees of the genes were selected by polymerase chain reaction (PCR) and randomly recombined in the phage library, which can be followed by Winter et al.,Ann . Rev . Immunol . 12: 433-455 (1994), screening for antigen-binding phages. Phages usually present antibody fragments in the form of single chain Fv (scFv) fragments or Fab fragments. Libraries from immunized sources provide high affinity antibodies to immunogens without the need to construct fusion tumors. Alternatively, primitive lineages (eg from humans) can be selected to provide a single source of antibodies against a wide range of non-self antigens and self antigens without any immunization, such as Griffiths et al.,EMBO J , 12: 725-734 (1993). Finally, the original library can also be prepared synthetically by colonizing unrearranged V gene segments from stem cells, and using PCR primers containing random sequences to encode highly variable CDR3 regions and achieving in vitro rearrangement, such as By Hoogenboom and Winter,J . Mol . Biol . , 227: 381-388 (1992). Patent publications describing human antibody phage libraries include, for example: US Patent No. 5,750,373 and US Patent Publication Nos. 2005/0079574, 2005/0119455, 2005/0266000, 2007/0117126, and 2007/0160598 No., No. 2007/0237764, No. 2007/0292936 and No. 2009/0002360. Antibodies or antigen-binding fragments thereof can be prepared using phage display to screen libraries of antibodies specific for complexes containing HIV-1 RT peptides and MHC class I proteins. The library may be at least 1 × 10⁹ (Such as at least about 1 × 10⁹ , 2.5 × 10⁹ , 5 × 10⁹ , 7.5 × 10⁹ , 1 × 10¹⁰ , 2.5 × 10¹⁰ , 5 × 10¹⁰ , 7.5 × 10¹⁰ Or 1 × 10¹¹ Any of) a diverse human scFv phage display library of unique human antibody fragments. In some embodiments, the library is an unprocessed human library constructed from DNA extracted from human PMBC and spleen from healthy donors and encompasses all human heavy and light chain subfamilies. In some embodiments, the library is an untreated human library constructed from DNA extracted from patients with various diseases, such as patients with autoimmune diseases, cancer patients, and infectious diseases (such as HIV) PBMC isolated from patients. In some embodiments, the library is a semi-synthetic human library in which the heavy chain CDR3 is completely randomized, and all amino acids (except cysteine) may also be present at any given position (see for example Hoet, RM Wait,Nat . Biotechnol . 23 (3): 344-348, 2005). In some embodiments, the length of the heavy chain CDR3 of a semi-synthetic human library is about 5 to about 24 (such as about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17 , 18, 19, 20, 21, 22, 23 or 24) amino acids. In some embodiments, the library is a non-human phage display library. Pure phage lines that bind to RTMC with high affinity can be selected as follows: by repeatedly binding the phage to RTMC, the RTMC is bound to a solid support (such as beads for solution panning or mammalian cells for cell panning) Then, remove the unbound phage and dissociate by specifically binding the phage. In the example of solution panning, RTMC may be labeled with biotin to be fixed to a solid support. The biotin-labeled RTMC is mixed with a phage library and a solid carrier, such as streptavidin-conjugated Dynabeads (Dynabeads) M-280, and then the RTMC-phage-bead complex is separated. The pure line of bound phage is then lysed and used to infect appropriate host cells, such as E. coli XL1-Blue, for expression and purification. In the cell panning example, TMC cells loaded with HIV-1 RT peptide of RTMC (TAP defect, HLA-A * 02: 01⁺ Lymphoblast cell line) was mixed with the phage library, after which the cells were collected and combined with pure lines were lysed and used to infect appropriate host cells for expression and purification. Panning can be performed by multiple rounds (such as about any of 2, 3, 4, 5, 6, or more) by solution panning, cell panning, or a combination of the two to enrich for specific binding to RTMC The pure line of bacteriophage. The enriched bacteriophage pure line can be tested for specific binding to RTMC by any method known in the art, including, for example, ELISA and FACS. Monoclonal antibodies can also be produced by recombinant DNA methods, such as those described in US Patent No. 4,816,567. The DNA encoding the monoclonal antibody of the present invention can be easily isolated and sequenced using conventional procedures (for example, by using oligonucleotide probes that can specifically bind to genes encoding the heavy and light chains of murine antibodies) . Fusion tumor cells as described above or the RTMC-specific phage pure line of the present invention can serve as a source of such DNA. After isolation, the DNA can be placed in expression vectors and then transfected into host cells (such as monkey COS cells, Chinese hamster ovary (CHO) cells or myeloma cells) (otherwise these host cells will not produce immunoglobulins) To obtain the synthesis of monoclonal antibodies in recombinant host cells. DNA can also be used, for example, by replacing homologous non-human sequences with coding sequences for the constant domains and / or framework regions of human heavy and light chains (US Patent No. 4,816,567; Morrison et al., Aforementioned) or by non-immunization All or part of the coding sequence of the globulin polypeptide is covalently joined to the immunoglobulin coding sequence for modification. Such non-immunoglobulin polypeptides can replace the constant domain of the antibody of the present invention, or can replace the variable domain of an antigen combination site of the antibody of the present invention to produce a chimeric bivalent antibody. The antibody may be a monovalent antibody. Methods for preparing monovalent antibodies are known in the art. For example, one method involves the recombinant expression of immunoglobulin light chains and modified heavy chains. The heavy chain is usually truncated at any point in the Fc region to prevent heavy chain crosslinking. Alternatively, the relevant cysteine residue is substituted with another amino acid residue or deleted to prevent crosslinking. The in vitro method is also suitable for preparing monovalent antibodies. Any method known in the art can be used to effect digestion of antibodies to produce fragments thereof, specifically Fab fragments. An antibody variable domain (antibody-antigen combination site) with the desired binding specificity can be fused to an immunoglobulin constant domain sequence. Preferably, it is fused to an immunoglobulin heavy chain constant domain comprising at least a part of the hinge, CH2 and CH3 regions. In some embodiments, the first heavy chain constant region (C_H 1) Exist in at least one of the fusions. The DNA encoding the immunoglobulin heavy chain fusion and, if necessary, the immunoglobulin light chain is inserted into a separate expression vector and co-transfected into a suitable host organism. For additional details on the production of bispecific antibodies, see for example Suresh et al.,Methods in Enzymology , 121: 210 (1986).Human and humanized antibodies The anti-RTMC antibody or antibody portion may be a humanized antibody or a human antibody. Humanized forms of non-human (e.g. murine) antibodies are chimeric immunoglobulins, immunoglobulin chains or fragments thereof (such as Fv, Fab, Fab ', F ( ab ')₂ , ScFv or other antigen-binding sequences of antibodies). Humanized antibodies include human immunoglobulins (recipient antibodies), where the residues of the recipient CDRs are composed of CDRs (donors) of non-human species (such as mice, rats, or rabbits) with the desired specificity, affinity, and ability Antibody). In some cases, Fv framework residues of the human immunoglobulin are replaced with corresponding non-human residues. Humanized antibodies can also include residues that are not present in the recipient antibody and in the introduced CDR or framework sequences. In general, a humanized antibody may comprise substantially all variable domains, at least one and usually two, where all or substantially all CDR regions correspond to their CDR regions and all or substantially all FRs of non-human immunoglobulins Regions are the FR regions of human immunoglobulin common sequence. In some embodiments, the humanized antibody will comprise at least a portion of an immunoglobulin constant region (Fc), usually at least a portion of human immunoglobulin. See for example Jones et al.,Nature , 321: 522-525 (1986); Riechmann et al.,Nature , 332: 323-329 (1988); Presta,Curr . Op . Struct . Biol . , 2: 593-596 (1992). In general, humanized antibodies have one or more amino acid residues introduced into them from non-human sources. These non-human amino acid residues are commonly referred to as "introduced" residues, which are typically taken from "introduced" variable domains. According to some embodiments, humanization can basically follow the method of Winter and colleagues (Jones et al.,Nature , 321: 522-525 (1986); Riechmann et al.,Nature , 332: 323-327 (1988); Verhoeyen et al.,Science , 239: 1534-1536 (1988)), by replacing the corresponding sequences of human antibodies with rodent CDRs or CDR sequences. Therefore, such "humanized" antibodies are antibodies in which substantially fewer intact human variable domains have been substituted by corresponding sequences from non-human species (US Patent No. 4,816,567). In fact, humanized antibodies are usually human antibodies in which some CDR residues and possibly some FR residues are substituted with residues from similar sites in rodent antibodies. As an alternative to humanization, human antibodies can be produced. For example, it is now possible to produce transgenic animals (such as mice) that are capable of producing a full lineage of human antibodies in the absence of endogenous immunoglobulin production after immunization. For example, it has been described that the homozygous deletion of the antibody rejoining region (JH) gene in chimeric and germline mutant mice results in complete inhibition of endogenous antibody production. Transfer of the human germline immunoglobulin gene array to such germline mutant mice will result in the production of human antibodies upon antigen challenge. See for example Jakobovits et al,PNAS USA , 90: 2551 (1993); Jakobovits et al.,Nature , 362: 255-258 (1993); Bruggemann et al.,Year in Immunol . , 7:33 (1993); US Patent Nos. 5,545,806, 5,569,825; 5,591,669; 5,545,807; and WO 97/17852. Alternatively, human antibodies can be prepared by introducing human immunoglobulin loci into transgenic animals (eg, mice whose endogenous immunoglobulin genes have been partially or completely inactivated). After the attack, observe human antibody production, which is very similar to that seen in humans in all aspects, including gene rearrangements, combinations, and antibody lineages. This method is described in, for example, U.S. Patent Nos. 5,545,807; 5,545,806; 5,569,825; 5,625,126; 5,633,425; and 5,661,016, and Marks et al.,Bio / Technology , 10: 779-783 (1992); Lonberg et al.,Nature , 368: 856-859 (1994); Morrison,Nature , 368: 812-813 (1994); Fishwild et al.,Nature Biotechnology , 14: 845-851 (1996); Neuberger,Nature Biotechnology , 14: 826 (1996); Lonberg and Huszar,Intern . Rev . Immunol . , 13: 65-93 (1995). Human antibodies can also be generated by activating B cells in vitro (see US Patent Nos. 5,567,610 and 5,229,275) or by using various techniques known in the art, including phage display libraries. Hoogenboom and Winter,J . Mol . Biol . , 227: 381 (1991); Marks et al.,J . Mol . Biol . , 222: 581 (1991). The techniques of Cole et al. And Boerner et al. Can also be used to prepare human monoclonal antibodies. Cole et al,Monoclonal Antibodies and Cancer Therapy , Alan R. Liss, page 77 (1985) and Boerner et al.,J. Immunol. , 147 (1): 86-95 (1991).Multispecific antibody In some embodiments, the anti-RTMC construct is a multispecific antibody. Suitable methods for preparing multispecific (eg bispecific) antibodies are well known in the art. For example, the production of bispecific antibodies can be based on the co-presentation of two immunoglobulin heavy / light chain pairs, each of which has a different specificity and produces a heterodimeric antibody after binding (see, eg, Milstein And Cuello,Nature , 305: 537-539 (1983); WO 93/08829, and Traunecker et al.,EMBO J . 10: 3655 (1991)). Due to the random classification of immunoglobulin heavy and light chains, these fusion tumors (four-source fusion tumors) produce a potential mixture of ten different antibody molecules, of which only one has an appropriate bispecific structure. Purification of appropriate molecules is usually achieved by affinity chromatography steps. Similar procedures are disclosed in WO 93/08829 and Traunecker et al.,EMBO , 10: 3655-3659 (1991). Alternatively, the combination of heavy and light chains can be oriented by using species-restricted pairing (see, for example, Lindhofer et al.,J . Immunol . , 155: 219-225 (1995)) and the heavy chain pairing can be oriented by using the "Pestle-Morch" engineering of the CH3 domain (see, eg, US Patent No. 5,731,168; Ridgway et al.,Protein Eng . , 9 (7): 617-621 (1996)). Multispecific antibodies can also be prepared by engineering the electrostatic turning effect to produce antibody Fc-heterodimer molecules (see, for example, WO 2009 / 089004A1). In another method, stable bispecific antibodies can be produced by controlled Fab arm exchange, where two parent antibodies with distinct antigen specificities and matching point mutations in the CH3 domain are mixed under reducing conditions to allow separation and recombination And reoxidation to form highly pure bispecific antibodies. Labrigin and others,Proc . Natl . Acad . Sci . , 110 (13): 5145-5150 (2013). Such antibodies comprising a mixture of heavy / light chain pairs are also referred to herein as "heteromultimeric antibodies". Antibodies or antigen-binding fragments with different specificities can also be chemically cross-linked to produce multispecific heteroconjugate antibodies. For example, two F (ab ') 2 molecules each specific for different antigens can be chemically linked. Pullarkat and others,Trends Biotechnol. , 48: 9-21 (1999). For example, such antibodies have been proposed to target immune system cells to unwanted cells (US Patent No. 4,676,980) and are used to treat HIV infection. WO 91/00360; WO 92/200373; EP 03089. It is expected that antibodies can be prepared in vitro using known methods in synthetic protein chemistry, including those involving cross-linking agents. For example, immunotoxins can be constructed using disulfide bond exchange reactions or by forming thioether bonds. Examples of reagents suitable for this purpose include iminothiol esters and methyl-4-mercaptobutyroimidate and reagents disclosed in, for example, US Patent No. 4,676,980. In some embodiments, multispecific antibodies can be prepared using recombinant DNA technology. For example, bispecific antibodies can be engineered by fusing two scFvs, such as by fusing them via peptide linkers to produce tandem scFvs. An example of a tandem scFv is a bispecific T cell junction molecule. Bispecific T cell junction molecules are prepared by attaching anti-CD3 scFv to a scFv specific for a surface antigen of a target cell, such as a tumor-associated antigen (TAA), resulting in the redirection of T cells to the target cell. Mack et al,Proc . Natl . Acad . Sci . , 92: 7021-7025 (1995); Brischwein et al.,Mol . Immunol . , 43 (8): 1129-1143 (2006). By shortening the length of the peptide linker between the two variable domains, it prevents self-assembly and forces pairing with the domain on the second polypeptide, resulting in a compact bispecific antibody called bifunctional antibody (Db) . Holliger et al.,Proc . Natl . Acad . Sci . , 90: 6444-6448 (1993). The two polypeptides of Db each contain a linker that is too short to allow pairing between the two domains on the same chain to V_L Of V_H . Therefore, the V of a polypeptide_H And V_L Domain is forced to be complementary to another polypeptide V_L And V_H The domains are paired to form two antigen binding sites. With this type of modification, two polypeptides are linked by another peptide linker, thereby generating a single chain bifunctional antibody (scDb). In another modification of the Db version, the dual affinity retargeting (DART) bispecific antibody can be introduced by introducing a disulfide bond between the cysteine residues at the C-terminus of each polypeptide, as appropriate The desired heterodimer structure is generated in the domain preceding the assembled C-terminal cysteine residue. Veri et al.,Arthritis Rheum. , 62 (7): 1933-1943 (2010). Dual variable domain immunoglobulins (DVD-Ig^TM ), Where the target binding variable domains of two monoclonal antibodies are combined via a naturally occurring linker to produce a tetravalent, bispecific antibody. Gu and Ghayur,Methods Enzymol. , 502: 25-41 (2012). In another version, by using a peptide (AD2) derived from the anchor domain of human A kinase anchor protein (AKAP) to a regulatory subunit peptide derived from human cAMP-dependent protein kinase (PKA) ( DDD2) Dimerization to prepare Dock and Lock (DNL) and bispecific antibodies. Rossi et al.,Proc . Natl . Acad . Sci . , 103: 6841-6846 (2006). Various techniques for preparing and isolating bispecific antibody fragments directly from recombinant cell culture have also been described. For example, leucine zippers have been used to generate bispecific antibodies. Kostelny and others,J. Immunol. , 148 (5): 1547-1553 (1992). This method can also be used to generate antibody homodimers.anti- RTMC Variants In some embodiments, amino acid sequence variants of the antibody portions provided herein are covered. For example, it may be necessary to improve the binding affinity and / or other biological properties of the antibody portion. Amino acid sequence variants of antibody portions can be prepared by introducing appropriate modifications into the nucleotide sequence encoding the antibody portion or by peptide synthesis. Such modifications include, for example, the deletion and / or insertion and / or substitution of residues within the amino acid sequence of the antibody portion. Any combination of deletion, insertion, and substitution can be made to obtain the final construct, with the restriction that the final construct has the desired characteristics, such as antigen binding. In some embodiments, antibody partial variants having one or more amino acid substitutions are provided. Related sites for substitution mutation induction include HVR and FR. Amino acid substitutions can be introduced into the product of the relevant antibody portion and screening for the desired activity (eg, maintaining / improving antigen binding, reducing immunogenicity, or improving ADCC or CDC). Conservative substitutions are shown in Table 6 below.table 6 : Conservative substitution Amino acids can be grouped into different categories based on common side chain properties: a. Hydrophobicity: n-leucine, Met, Ala, Val, Leu, Ile; b. Neutral hydrophilicity: Cys, Ser, Thr, Asn, Gln ; C. Acidic: Asp, Glu; d. Basic: His, Lys, Arg; e. Residues that affect chain orientation: Gly, Pro; f. Aromatic: Trp, Tyr, Phe. Non-conservative substitutions will inevitably be accompanied by replacing members of one of these categories with another category. Exemplary substitution variants are affinity matured antibody portions, which can be conveniently generated, for example, using affinity mature technology based on phage display. Briefly, one or more CDR residues are mutated and a variant antibody portion is displayed on the phage and screened for specific biological activity (eg, binding affinity). Modifications (eg, substitutions) can be made in HVR to, for example, improve the partial affinity of the antibody. Such changes can be in HVR "hot spots" (i.e. residues encoded by codons that undergo high frequency mutations during the somatic maturation process (see e.g. Chowdhury,Methods Mol . Biol . 207: 179-196 (2008)), and / or specificity-determining residues (SDR)), where the resulting variant V is tested_H Or V_L The binding affinity. Achieving affinity maturity by constructing secondary libraries and selecting from secondary libraries has been described in, for example, Hoogenboom et al.,Methods in Molecular Biology 178: 1-37 (edited by O'Brien et al., Human Press, Totowa, NJ, (2001)). In some embodiments of affinity maturation, diversity is introduced into variable genes selected for maturation by any of various methods (eg, error-prone PCR, strand shuffling, or oligonucleotide-induced mutation induction) in. Then a secondary library is generated. The library is then screened to identify any partial antibody variants with the desired affinity. Another method of introducing diversity includes the HVR targeting method, in which several HVR residues (eg, 4-6 residues at a time) are performed randomly. The HVR residues involved in antigen binding can be specifically identified, for example, using alanine to scan for mutation induction or model establishment. Especially CDR-H3 and CDR-L3 are usually targeted. In some embodiments, substitutions, insertions, or deletions can occur within one or more HVRs, as long as such modifications do not substantially reduce the ability of the antibody portion to bind antigen. For example, conservative changes (eg, conservative substitutions as provided herein) can occur in HVR that do not substantially reduce binding affinity. Such changes can be outside the HVR "hotspot" or SDR. Variation V provided above_H And V_L In certain embodiments of the sequence, each HVR is unchanged or contains no more than one, two, or three amino acid substitutions. A method suitable for identifying residues or regions of antibody parts that can be targeted by mutation induction is called "alanine scanning mutation induction", such as Cunningham and Wells (1989)Science , 244: 1081-1085. In this method, residues or target residue groups (eg charged residues such as arg, asp, his, lys and glu) are identified and consist of neutral or negatively charged amino acids (eg alanine or polyalanine) Replacement to determine if the interaction of the antibody part with the antigen is affected. Other substitutions can be introduced at amino acid positions that exhibit functional sensitivity to the initial substitution. Alternatively or additionally, the crystal structure of the antigen-antibody portion complex can be determined to identify the contact point between the antibody portion and the antigen. Such contact residues and neighboring residues can be targeted or excluded as candidates for substitution. Variants can be screened to determine if they contain the desired characteristics. Amino acid sequence insertions include amino-terminal and / or carboxy-terminal fusions ranging in length from one residue to a polypeptide containing one hundred or more residues, as well as sequences of single or multiple amino acid residues insert. Examples of terminal insertions include antibodies with N-terminal methionine residues. Other insertion variants of the antibody portion include fusions of the N-terminus or C-terminus of the antibody portion with an enzyme (for example for ADEPT) or a polypeptide that increases the serum half-life of the antibody portion.Fc Zone variant In some embodiments, one or more amino acid modifications can be introduced into the Fc region of full-length anti-RTMC antibodies provided herein, thereby generating Fc region variants. In some embodiments, Fc region variants have enhanced antibody-dependent cytotoxicity (ADCC) effector functions, which are generally associated with binding to Fc receptors (FcR). In some embodiments, Fc region variants have reduced ADCC effector function. There are multiple examples of changes or mutations in the Fc sequence that can alter the effector function. For example, WO 00/42072 and Shields et alJ Biol . Chem 9 (2): 6591-6604 (2001) describes antibody variants with increased or decreased binding to FcR. The contents of these publications are specifically incorporated by reference. Antibody-dependent cell-mediated cytotoxicity (ADCC) is the mechanism of action of therapeutic antibodies on tumor cells. ADCC is a cell-mediated immune defense, whereby effector cells of the immune system actively and efficiently lyse target cells (such as HIV-1 infected cells). The membrane surface antigens of the cells have been combined with specific antibodies (such as anti-RTMC antibodies) ) Combine. Typical ADCC involves the activation of NK cells by antibodies. NK cells appear as CD16 of Fc receptors. This receptor recognizes the Fc portion of the antibody that binds to the surface of the target cell and binds to the Fc portion. The most common Fc receptor on the surface of NK cells is called CD16 or FcγRIII. The binding of the Fc receptor to the Fc region of the antibody results in activation of NK cells, release of cytolytic particles and subsequent apoptosis of target cells. The contribution of ADCC to tumor cell killing can be measured by using a specific test of NK-92 cells that have been transfected with high affinity FcR. The results were compared with wild-type NK-92 cells that did not express FcR. In some embodiments, the present invention covers variants of anti-RTMC constructs that include FC regions with some but not all effector functions, which makes it important for the half-life of anti-RTMC constructs in vivo, while certain effector functions (such as CDC and ADCC) Required candidates for unnecessary or harmful applications. In vitro and / or in vivo cytotoxicity analysis can be performed to confirm the reduction / depletion of CDC and / or ADCC activity. For example, Fc receptor (FcR) binding analysis can be performed to ensure that the antibody lacks FcγR binding (hence likely lacking ADCC activity), but retains FcRn binding ability. Primary cells used to regulate ADCC (NK cells) only express FcγRIII, while monocytes express FcγRI, FcγRII and FcγRIII. The performance of FcR on hematopoietic cells is summarized in Ravetch and Kinet,Annu . Rev . Immunol . 9: 457-492 (1991), page 464, table 3. Non-limiting examples of in vitro analysis to assess the ADCC activity of the molecule of interest are described in U.S. Patent No. 5,500,362 (see for example Hellstrom, I. et al. Proc.Nat ' l Acad . Sci . USA 83: 7059-7063 (1986)) and Hellstrom, I and others,Proc . Nat ' l Acad . Sci . USA 82: 1499-1502 (1985); US Patent No. 5,821,337 (see Bruggemann, M. et al.,J . Exp . Med . 166: 1351-1361 (1987)). Alternatively, non-radioactive analysis methods (see, for example, ACTI ™ non-radioactive cytotoxicity analysis (CellTechnology, Inc. Mountain View, Calif.) For flow cytometry; and CytoTox 96 ™ non-radioactive cytotoxicity analysis ( Promega, Madison, Wis.)). Effector cells suitable for this type of analysis include peripheral blood mononuclear cells (PBMC) and natural killer (NK) cells. Alternatively or additionally, the ADCC activity of the molecule of interest can be assessed in vivo, for example, as disclosed in Clynes et al.Proc . Nat ' l Acad . Sci . In the animal model of USA 95: 652-656 (1998). Clq binding analysis can also be performed to confirm that the antibody cannot bind Clq and therefore lacks CDC activity. See, for example, C1q and C3c binding ELISA in WO 2006/029879 and WO 2005/100402. To assess complement activation, CDC analysis can be performed (see for example Gazzano-Santoro et al.,J . Immunol . Methods 202: 163 (1996); Cragg, M.S. and others,Blood 101: 1045-1052 (2003); and Cragg, M.S. and M.J. Glennie,Blood 103: 2738-2743 (2004)). Methods known in the art can also be used (see, for example, Petkova, S. B. et al.,Int ' l . Immunol . 18 (12): 1759-1769 (2006)) FcRn binding and clearance / half-life determination in vivo. Antibodies with reduced effect function include those antibodies having substitution of one or more of Fc region residues 238, 265, 269, 270, 297, 327 and 329 (US Patent No. 6,737,056). Such Fc mutants include Fc mutants that have substitutions at two or more of amino acid positions 265, 269, 270, 297, and 327, including the so-called "alanine residues 265 and 297 substitutions" "DANA" Fc mutant (US Patent No. 7,332,581). Describe certain antibody variants that have increased or decreased binding to FcR. (See, for example, US Patent No. 6,737,056; WO 2004/056312, and Shields et al.,J . Biol . Chem . 9 (2): 6591-6604 (2001)). In some embodiments, a variant of an anti-RTMC construct (eg, a full-length anti-RTMC antibody) is provided that includes a variant Fc region containing one or more amino acid substitutions of modified ADCC. In some embodiments, the variant Fc region includes one or more amino acid substitutions of modified ADCC, wherein the substitutions are at positions 298, 333, and / or 334 (residue EU numbering) of the variant Fc region. In some embodiments, anti-RTMC construct (eg, full-length anti-RTMC antibody) variants include the following amino acid substitutions in their variant Fc regions: S298A, E333A, and K334A. In some embodiments, changes are made in the Fc region that produces altered (ie, improved or decreased) Clq binding and / or complement dependent cytotoxicity (CDC), such as described in US Patent No. 6,194,551, WO 99/51642 Idusogie and others,J . Immunol . 164: 4178-4184 (2000). In some embodiments, a variant of an anti-RTMC construct (eg, a full-length anti-RTMC antibody) is provided that includes an amino acid substitution that includes one or more amino acids that increase half-life and / or improve binding to a nascent Fc receptor (FcRn) Of the variant Fc region. Antibodies with increased half-life and improved binding to FcRn are described in US2005 / 0014934A1 (Hinton et al.). These antibodies include an Fc region with one or more substitutions therein, which improves the binding of the Fc region to FcRn. Such Fc variants include those having substitutions at one or more of the following Fc region residues: 238, 256, 265, 272, 286, 303, 305, 307, 311, 312, 317, 340, 356 , 360, 362, 376, 378, 380, 382, 413, 424, or 434, for example, substitution of residue 434 in the Fc region (US Patent No. 7,371,826). For other examples of Fc region variants, see also Duncan and Winter,Nature 322: 738-40 (1988); US Patent No. 5,648,260; US Patent No. 5,624,821; and WO 94/29351. Anti-RTMC constructs (such as full-length anti-RTMC antibodies) comprising any of the Fc variants described herein, or a combination thereof are encompassed.Glycosylation variant In some embodiments, the anti-RTMC constructs provided herein are modified to increase or decrease the degree of glycosylation of the anti-RTMC constructs. The addition or deletion of the glycosylation site of the anti-RTMC construct can be facilitated by changing the amino acid sequence of the anti-RTMC construct or its polypeptide part, so that one or more glycosylation sites are generated or removed achieve. In the case where the anti-RTMC construct contains an Fc region, the carbohydrate attached to it can be changed. Natural antibodies produced by mammalian cells usually comprise branched-chain biantennary oligosaccharides, which are generally N-linked to Asn297 in the CH2 domain of the Fc region. See for example Wright et al.,TIBTECH 15: 26-32 (1997). Oligosaccharides can include various carbohydrates such as mannose, N-acetylglucosamine (GlcNAc), galactose, and sialic acid, and trehalose attached to GlcNAc in the "backbone" of the biantennary oligosaccharide structure. In some embodiments, modification of oligosaccharides in the anti-RTMC constructs of the present invention can be made to produce anti-RTMC construct variants with certain improved properties. In some embodiments, variants of an anti-RTMC construct (such as a full-length anti-RTMC antibody) comprising an Fc region are provided, wherein the carbohydrate structure attached to the Fc region has reduced or no trehalose, which can improve ADCC function . In particular, covered herein are anti-RTMC constructs with reduced trehalose relative to the amount of trehalose on the same anti-RTMC construct produced in wild-type CHO cells. That is, it is characterized by having a lower amount of trehalose than it would otherwise have if it were produced by natural CHO cells (for example, CHO cells that produce a natural glycosylation pattern, such as CHO cells containing a natural FUT8 gene) . In some embodiments, the anti-RTMC construct is a construct in which less than about 50%, 40%, 30%, 20%, 10%, or 5% of the N-linked glycans on it comprise trehalose. For example, the amount of trehalose in such anti-RTMC constructs may be 1% to 80%, 1% to 65%, 5% to 65%, or 20% to 40%. In some embodiments, the anti-RTMC construct is one in which none of the N-linked glycans on it contains trehalose, that is, wherein the anti-RTMC construct is completely free of trehalose, or does not have trehalose or is removed Trehalosylated. The amount of trehalose is calculated by summing the trehalose at Asn297 in the sugar chain relative to all sugar structures (e.g. complex, hybridization and high mannose structures) connected to Asn 297 as measured by MALDI-TOF mass spectrometry The average amount is determined as described in WO 2008/077546, for example. Asn297 refers to asparagine residues located at approximately position 297 in the Fc region (Eu numbering of residues in the Fc region); however, due to minor sequence variations in the antibody, Asn297 can also be located upstream or downstream of approximately position 297 ± 3 amino acids, that is, between position 294 and position 300. Such trehalosylated variants may have improved ADCC function. See, for example, US Patent Publication No. US 2003/0157108 (Presta, L.); US 2004/0093621 (Kyowa Hakko Kogyo Co., Ltd). Examples of publications related to "de-trehalosylated" or "trehalose-deficient" antibody variants include: US 2003/0157108; WO 2000/61739; WO 2001/29246; US 2003/0115614; US 2002/0164328; US 2004/0093621; US 2004/0132140; US 2004/0110704; US 2004/0110282; US 2004/0109865; WO 2003/085119; WO 2003/084570; WO 2005/035586; WO 2005/035778; WO2005 / 053742; WO2002 / 031140; Okazaki et al.J. Mol. Biol . 336: 1239-1249 (2004); Yamane-Ohnuki et al.. Biotech. Bioeng . 87: 614 (2004). Examples of cell lines capable of producing trehalosylated antibodies include Lec13 CHO cells lacking protein trehalosylation (Ripka et al., Arch. Biochem. Biophys. 249: 533-545 (1986); US Patent Application No. US 2003/0157108 A1, Presta, L; and WO 2004/056312 A1, Adams et al., Especially Example 11), and gene knockout cell lines, such as α-1,6-trehalosyltransferase gene, FUT8, gene knockout CHO cells (see, for example, Yamane-Ohnuki et al., Biotech. Bioeng. 87: 614 (2004); Kanda, Y. et al., Biotechnol. Bioeng., 94 (4): 680-688 (2006); and WO2003 / 085107 ). Variants of anti-RTMC constructs (such as full-length anti-RTMC antibodies) additionally have bisecting oligosaccharides, for example, diantennary oligosaccharides in which the Fc region linked to the anti-RTMC construct is bisected by GlcNAc. Such anti-RTMC construct variants (such as full-length anti-RTMC antibody) variants may have reduced trehalosylation and / or improved ADCC function. Examples of such antibody variants are described in, for example, WO 2003/011878 (Jean-Mairet et al.); US Patent No. 6,602,684 (Umana et al.); US 2005/0123546 (Umana et al.) And Ferrara et al.,Biotechnology and Bioengineering , 93 (5): 851-861 (2006). Variants of anti-RTMC constructs (such as full-length anti-RTMC antibodies) having at least one galactose residue in the oligosaccharide linked to the Fc region are also provided. Such anti-RTMC construct variants may have improved CDC function. Such antibody variants are described in, for example, WO 1997/30087 (Patel et al.); WO 1998/58964 (Raju, S.); and WO 1999/22764 (Raju, S.). In some embodiments, Fc region-containing anti-RTMC constructs (such as full-length anti-RTMC antibody variants are capable of binding to FcyRIII. In some embodiments, Fc region-containing anti-RTMC constructs (such as full-length anti-RTMC antibody) variants ADCC activity in the presence of human effector cells or increased ADCC activity in the presence of human effector cells compared to another identical anti-RTMC construct (such as a full-length anti-RTMC antibody) comprising human wild-type IgG1 Fc region.Cysteine engineered variants In some embodiments, it may be necessary to generate cysteine engineered anti-RTMC constructs (such as full-length anti-RTMC antibodies) in which one or more amino acid residues are substituted with cysteine residues. In some embodiments, the substituted residue is present at an accessible site of the anti-RTMC construct. By replacing their residues with cysteine, the reactive thiol group is thus located at an accessible site of the anti-RTMC construct and can be used to bind the anti-RTMC construct to other parts, such as drug moieties or linkers -A drug moiety to produce an anti-RTMC immunoconjugate, as described further herein. Cysteine engineered anti-RTMC constructs (such as full-length anti-RTMC antibodies) can be generated as described in, for example, US Patent No. 7,521,541.derivative In some embodiments, the anti-RTMC constructs provided herein can be further modified to contain additional non-protein portions known in the art and readily available. Parts suitable for anti-RTMC construct derivatization include (but are not limited to) water soluble polymers. Non-limiting examples of water-soluble polymers include, but are not limited to, polyethylene glycol (PEG), ethylene glycol / propylene glycol copolymer, carboxymethyl cellulose, polydextrose, polyvinyl alcohol, polyvinylpyrrolidone, Poly-1,3-dioxolane, poly-1,3,6-trioxane, ethylene / maleic anhydride copolymer, polyamino acid (homopolymer or random copolymer) and Polydextrose or poly (n-vinylpyrrolidone) polyethylene glycol, propylene glycol homopolymer, polyoxypropylene / ethylene oxide copolymer, polyoxyethylene polyol (such as glycerin), polyvinyl alcohol, and mixtures thereof. Polyethylene glycol propionaldehyde can have advantages in production due to its stability in water. The polymer can have any molecular weight and can be branched or unbranched. The number of polymers attached to the RTMC-resistant construct can vary, and if more than one polymer is attached, they can be the same or different molecules. In general, the number and / or type of polymers used for derivatization can be based on including (but not limited to) the specific characteristics or functions of the anti-RTMC construct to be improved, and whether the anti-RTMC construct derivative will be used under limited conditions Considerations such as treatment. In some embodiments, a combination of an anti-RTMC construct and a non-proteinaceous moiety that can be selectively heated by exposure to radiation is provided. In some embodiments, the non-protein portion is a carbon nanotube (Kam et al.,Proc. Natl.Acad. Sci. USA 102: 11600-11605 (2005)). The radiation may have any wavelength, and includes, but is not limited to, wavelengths that do not damage normal cells but heat the non-protein portion to a temperature that kills cells proximal to the anti-RTMC construct-non-protein portion.Preparation of chimeric receptor effector cells In one aspect, the invention provides effector cells (such as lymphocytes, such as T cells) that exhibit anti-RTMC chimeric receptors (such as anti-RTMC CAR or anti-RTMC abTCR). Provided herein are exemplary methods for preparing effector cells (such as T cells) expressing anti-RTMC chimeric receptors (anti-RTMC chimeric receptor effector cells, such as anti-RTMC CAR T cells or anti-RTMC abTCR T cells). In some embodiments, anti-RTMC chimeric receptor (such as anti-RTMC CAR or anti-RTMC abTCR) effector cells (such as T cells) can be introduced into the effector by introducing a vector (including, for example, a lentiviral vector) that encodes the following sequence Produced in cells (such as T cells): anti-RTMC CAR (for example, CAR containing anti-RTMC antibody portion and CD28 or 4-1BB and CD3ζ intracellular signaling sequences) or anti-RTMC abTCR. In some embodiments, the anti-RTMC chimeric receptor effector cells (such as T cells) of the present invention are capable of replicating in vivo, causing long-term persistence that can lead to continued control of HIV-1 infection. In some embodiments, the present invention relates to the administration of genetically modified T cells expressing anti-RTMC CAR or anti-RTMC abTCR for the use of lymphocyte infusion to treat patients at or at risk of HIV-1 infection patient. In some embodiments, autologous lymphocyte infusion is used in the treatment. Autologous PBMCs are collected from patients in need of treatment and T cells are activated and expanded using methods described herein and known in the art, and then infused back into the patients. In some embodiments, the anti-RTMC CAR T cells exhibit anti-RTMC CAR that includes an anti-RTMC antibody portion (also referred to herein as "anti-RTMC CAR T cells"). In some embodiments, the anti-RTMC CAR T cells express an anti-RTMC CAR that includes an extracellular domain that contains an anti-RTMC antibody portion and an intracellular domain that includes the intracellular signaling sequences of CD3ζ and CD28 and / or 4-1BB. In some embodiments, the anti-RTMC abTCR T cells express an anti-RTMC abTCR that includes an anti-RTMC antibody portion (also referred to herein as "anti-RTMC abTCR T cells"). In some embodiments, the anti-RTMC abTCR T cell expression comprises the following anti-RTMC abTCR: a) the extracellular domain, which comprises an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein; And b) T cell receptor module (TCRM), which can recruit at least one TCR related signaling module. The anti-RTMC chimeric receptor T cells (such as anti-RTMC CAR T cells or anti-RTMC abTCR T cells) of the present invention can withstand stable in vivo T cell expansion, and can be established at a higher level to remain in the blood and bone marrow. Long-term RTMC-specific memory cells. In some embodiments, the anti-RTMC chimeric receptor T cells of the present invention infused into patients can eliminate RTMC presenting cells, such as RTMC presenting HIV-1 infected cells, in patients with HIV-1 infection in vivo. In some embodiments, the anti-RTMC chimeric receptor T cells of the present invention infused into patients can eliminate RTMC presenting cells in vivo in patients with HIV-1 infection that are difficult to treat with at least one conventional treatment, such as RTMC presents HIV-1 infected cells. Prior to T cell expansion and genetic modification, T cell sources were obtained from individuals. T cells can be obtained from many sources, including peripheral blood mononuclear cells, bone marrow, lymph node tissue, umbilical cord blood, thymus tissue, tissue from the site of infection, ascites, pleural effusion, spleen tissue, and tumors. In some embodiments of the invention, any number of T cell lines available in the technology can be used. In some embodiments of the invention, T cells can be obtained from any number of blood units collected from the individual using techniques known to those skilled in the art, such as Ficoll ™ isolation. In some embodiments, cells from the circulating blood of the individual are obtained by haemocytosis. Hemocytosis products usually contain lymphocytes, including T cells, monocytes, granulocytes, B cells, other nucleated white blood cells, red blood cells, and platelets. In some embodiments, the cells collected by hemocytolysis can be washed to remove the plasma fraction and placed in an appropriate buffer or medium for subsequent processing steps. In some embodiments, the cells are washed with phosphate buffered saline (PBS). In some embodiments, the wash solution lacks calcium and may lack magnesium or may lack many, if not all, divalent cations. As one of ordinary skill will readily understand, the washing step can be achieved by methods known to those skilled in the art, such as by using a semi-automatic "flow-through" centrifuge according to the manufacturer's instructions (eg, Cobe 2991 cell processor, Baxter CytoMate or Haemonetics Cell holder 5). After washing, cells can be resuspended in a variety of biocompatible buffers, such as Ca-free²⁺ , Without Mg²⁺ PBS, PlasmaLyte A or other physiological saline solution with or without buffer. Alternatively, undesired components of the hemocytometer sample can be removed and the cells resuspended directly in the medium. In some embodiments, T cells are isolated from peripheral blood lymphocytes by lysing red blood cells and depleting monocytes, for example, by PERCOLL ™ gradient centrifugation or by countercurrent centrifugation. Specific subsets of T cells (such as CD3⁺ , CD28⁺ , CD4⁺ , CD8⁺ , CD45RA⁺ And CD45RO⁺ T cells) can be further separated by positive selection or negative selection techniques. For example, in some embodiments, by incubating with anti-CD3 / anti-CD28 (ie, 3 × 28) binding beads (such as DYNABEADS® M-450 CD3 / CD28 T), sufficient T cells are selected for positive selection Time to isolate T cells. In some embodiments, the time period is about 30 minutes. In some embodiments, the time period is in the range of 30 minutes to 36 hours or longer and all integer values in between. In some embodiments, the time period is at least 2, 3, 4, 5, or 6 hours. In some embodiments, the time period is 10 to 24 hours. In some embodiments, the incubation period is 24 hours. To isolate T cells from patients with leukemia, the use of longer incubation times (such as 24 hours) can increase cell yield. In any case where there are very few T cells compared to other cell types, a longer incubation time may be used to isolate T cells, such as the isolation of tumor infiltrating lymphocytes (TIL) from tumor tissue or immunocompromised individuals. In addition, using a longer incubation time can improve the capture of CD8⁺ T cell efficiency. Therefore, by only shortening or prolonging the time allowing T cells to bind to CD3 / CD28 beads and / or by increasing or decreasing the ratio of beads to T cells, other times during the initiation of culture or method Click to select T cell subsets first. In addition, by increasing or decreasing the ratio of anti-CD3 and / or anti-CD28 antibodies on beads or other surfaces, T cell subpopulations can be preferentially selected for or for initiation of culture or other time points. Those skilled in the art will recognize that multiple selection rounds can also be used in the context of the present invention. In some embodiments, it may be necessary to perform a selection procedure and use "unselected" cells during activation and expansion. "Unselected" cells can also withstand other selection rounds. Enriched T cell populations by negative selection can achieve negative selection using a combination of antibodies against surface markers that are different from negative selection cells. One method is to sort and / or select cells by negative magnetic immunoadhesion or flow cytometry, which uses a single strain against cell surface markers present on negative selection cells Antibody mixture. For example, to enrich CD4 by negative selection⁺ Cells, monoclonal antibody mixtures usually include antibodies to CD14, CD20, CD11b, CD16, HLA-DR and CD8. In some embodiments, it may be necessary to enrich or positively select regulatory T cells, which typically exhibit CD4⁺ , CD25⁺ , CD62Lhi, GITR⁺ And FoxP3⁺ . Alternatively, in some embodiments, T regulatory cells are depleted by anti-CD25 binding beads or other similar selection methods. In order to separate the desired cell population by positive selection or negative selection, the cell concentration and surface (eg particles, such as beads) can be varied. In some embodiments, it may be necessary to significantly reduce the volume of beads and cells mixed together (ie, increase the cell concentration) to ensure maximum contact between cells and beads. For example, in some embodiments, a concentration of about 2 billion cells / ml is used. In some embodiments, a concentration of about 1 billion cells / ml is used. In some embodiments, greater than about 100 million cells / ml are used. In some embodiments, about 10 million, 15 million, 20 million, 25 million, 30 million, 35 million, 40 million, 45 million, or 5,000 are used The cell concentration of any one of 10,000 cells / ml. In some embodiments, a concentration of any of about 75 million, 80 million, 85 million, 90 million, 95 million, or 100 million cells / ml is used. In some embodiments, a concentration of about 125 million cells or about 150 million cells / ml is used. The use of high concentrations can lead to increased cell yield, cell activation and cell expansion. In addition, the use of a high cell concentration allows more effective capture of target antigens that may be of weak performance (such as CD28 negative T cells) or cells from samples where there are many tumor cells (ie, leukemia blood, tumor tissue, etc.). Such cell populations may have therapeutic value and will need to be obtained. For example, the use of high cell concentrations allows more efficient selection of CD8, which usually has weaker CD28 performance⁺ T cells. In some embodiments of the invention, T cells are obtained directly from the patient after treatment. In this regard, it has been observed that after certain cancer treatments, specifically after treatment with drugs that damage the immune system, shortly after treatment, during which patients usually recover from the treatment period, the quality of T cells obtained may be optimal Its ability to expand in vitro has been improved. Likewise, after ex vivo manipulation using the methods described herein, enhanced transplantation and in vivo expansion of these cells may be in a better state. Therefore, the collection of blood cells (including T cells), dendritic cells, or other cells of the hematopoietic lineage during this recovery phase is covered within the context of the present invention. In addition, in some embodiments, movement (eg, movement with GM-CSF) and adjustment schemes can be used to establish conditions within the individual, where it is advisable to reproliferate, recycle, regenerate, and / or expand, especially during the established time window after treatment Increase specific cell types. Illustrative cell types include T cells, B cells, dendritic cells, and other cells of the immune system. Whether before or after genetically modifying T cells to express the desired anti-RTMC chimeric receptor (such as anti-RTMC CAR or anti-RTMC abTCR), T cells can generally be activated and expanded using methods such as those described in the following : U.S. Patent No. 6,352,694; U.S. Patent No. 6,534,055; U.S. Patent No. 6,905,680; U.S. Patent No. 6,692,964; U.S. Patent No. 5,858,358; U.S. Patent No. 6,887,466; U.S. Patent No. 6,905,681; U.S. Patent No. 7,144,575; U.S. Patent No. 7,067,318; U.S. Patent No. 7,172,869; U.S. Patent No. 7,232,566; U.S. Patent No. 7,175,843; U.S. Patent No. 5,883,223; U.S. Patent No. 6,905,874; U.S. Patent No. 6,797,514; U.S. Patent No. 6,867,041; and U.S. Patent Application Open Case No. 20060121005. In general, the T cells of the present invention are expanded by contacting the surface to which they are connected with an agent that stimulates signals related to the CD3 / TCR complex and ligands that stimulate costimulatory molecules on the surface of the T cells. In particular, the T cell population may be such as by contact with an anti-CD3 antibody or antigen-binding fragment thereof, or an anti-CD2 antibody immobilized on the surface, or by a protein kinase C activator (such as moss) bound to a calcium ionophore Insecticidal) stimulated by contact. To co-stimulate accessory molecules on the surface of T cells, ligands that bind accessory molecules are used. For example, the T cell population can be contacted with anti-CD3 antibodies and anti-CD28 antibodies under conditions suitable to stimulate T cell proliferation. To stimulate CD4⁺ T cells or CD8⁺ For the proliferation of T cells, anti-CD3 antibodies and anti-CD28 antibodies can be used. Examples of anti-CD28 antibodies include 9.3, B-T3, XR-CD28 (Diaclone, Besançon, France), which can be generally used by other methods generally known in this technology (Berg et al.Transplant Proc .30 (8): 3975-3977, 1998; Haanen et al.,J . Exp . Med . 190 (9): 13191328, 1999; Garland et al,J . Immunol Meth . 227 (1-2): 53-63, 1999).Immune conjugate preparation Anti-RTMC immunoconjugates can be prepared using any method known in the art. See, for example, WO 2009/067800, WO 2011/133886, and US Patent Application Publication No. 2014322129, which are incorporated herein by reference in their entirety. The anti-RTMC antibody portion of the anti-RTMC immunoconjugate can be "linked" to the effector molecule by any method, and the anti-RTMC antibody portion can be bound to the effector molecule or linked to the effector molecule by this method. For example, the anti-RTMC antibody portion of the anti-RTMC immunoconjugate can be linked to the effector molecule by chemical or recombinant methods. Chemical methods for preparing fusions or conjugates are known in the art and can be used to prepare anti-RTMC immunoconjugates. The method used to bind the anti-RTMC antibody moiety to the effector molecule must be able to conjugate the binding protein to the effector molecule without interfering with the binding protein's ability to bind to the antigen on the target cell. The anti-RTMC antibody portion of the anti-RTMC immunoconjugate can be indirectly linked to the effector molecule. For example, the anti-RTMC antibody portion of the anti-RTMC immunoconjugate can be directly linked to liposomes containing effector molecules of one of several types. Effector molecules and / or anti-RTMC antibody moieties can also bind to solid surfaces. In some embodiments, the anti-RTMC antibody portion of the anti-RTMC immunoconjugate and the effector molecule are both proteins and can be bound using techniques well known in the art. There are hundreds of available cross-linking agents that can bind two proteins. (See, for example, "Chemistry of Protein Conjugation and Crosslinking". 1991, Shans Wong, CRC Press, Ann Arbor). The cross-linking agent is generally selected based on the reactive functional groups available or inserted into the anti-RTMC antibody moiety and / or effector molecule. In addition, if no reactive groups are present, a photoactivatable crosslinking agent can be used. In some cases, it may be necessary to include a spacer between the anti-RTMC antibody portion and the effector molecule. The crosslinking agents known in the art include homobifunctional agents: glutaraldehyde, dimethyl diiminoadipate, and bis (diazobenzidine); and heterobifunctional agents: m-cis-butadiene diacetyl Aminobenzyl-N-hydroxysuccinimide and sulfonate-m-maleimide dibenzimidylbenzyl-N-hydroxysuccinimide. In some embodiments, the anti-RTMC antibody portion of the anti-RTMC immunoconjugate can be engineered with specific residues to chemically link effector molecules. Specific residues known in the art for chemically linking molecules include lysine and cysteine. The cross-linking agent is selected based on the reactive functional groups inserted on the anti-RTMC antibody moiety and on the effector molecule. Anti-RTMC immunoconjugates can also be prepared using recombinant DNA technology. In this case, the DNA sequence encoding the anti-RTMC antibody portion is fused to the DNA sequence encoding the effector molecule, resulting in a chimeric DNA molecule. The chimeric DNA sequence is transfected into host cells expressing the fusion protein. The fusion protein can be recovered from the cell culture and purified using techniques known in the art. Examples of linking effector molecules (which are labels) to binding proteins include the methods described in the following: Hunter et al.,Nature 144: 945 (1962); David et al.,Biochemistry 13: 1014 (1974); Pain et al.,J . Immunol . Meth . 40: 219 (1981); Nygren,J . Histochem . and Cytochem . 30: 407 (1982); Wensel and Meares,Radioimmunoimaging And Radioimmunotherapy , Elsevier, N.Y. (1983); and Colcher et al., "Use Of Monoclonal Antibodies As Radiopharmaceuticals For The Localization Of Human Carcinoma Xenografts In Athymic Mice",Meth . Enzymol . , 121: 802-16 (1986). Radioactive or other labels can be incorporated into the immunoconjugate in a known manner. For example, peptides can be biosynthesized or can be synthesized by chemical amino acid synthesis using suitable amino acid precursors (including, for example, fluorine-19 instead of hydrogen). Such as⁹⁹ Tc or¹²³ I,¹⁸⁶ Re,¹⁸⁸ Re and¹¹¹ The label of In can be connected via a cysteine residue in the peptide. Yttrium-90 can be attached via lysine residues. The IODOGEN method (Fraker et al., Biochem. Biophys. Res. Commun. 80: 49-57 (1978)) can be used to incorporate iodine-123. "Monoclonal Antibodies in Immunoscintigraphy" (Chatal, CRC Press 1989) describes other methods in detail. Immunoconjugates of antibody moieties and cytotoxic agents can be prepared using a variety of such as the following: bifunctional protein coupling agent, N-butanediimido-3- (2-pyridyldithio) propionate (SPDP) , Butadiene imino-4- (N-maleimide diiminomethyl) cyclohexane-1-carboxylate (SMCC), iminothiolane (IT); amide Bifunctional derivatives of imine esters (such as dimethyl diimino adipate HCl); active esters (such as dibutylenediimidate suberate); aldehydes (such as glutaraldehyde); double stacks Nitrogen-based compounds (such as bis (p-azidobenzyl) hexamethylenediamine); double nitrogen derivatives (such as bis (p-diazobenzyl) -ethylenediamine); diisocyanates (such as toluene 2, 6-diisocyanate); and double-active fluorine compounds (such as 1,5-difluoro-2,4-dinitrobenzene). For example, the ricin toxin immunotoxin may be such as Vitetta et al.,Science 238: 1098 (1987). Carbon 14-labeled 1-isothiocyanatobenzyl-3-methyldiethylenetriaminepentaacetic acid (MX-DTPA) is an exemplary chelating agent for binding radionucleotide to antibodies. See for example WO94 / 11026. The linker may be a "cleavable linker" that promotes the release of cytotoxic drugs in cells. For example, acid labile linkers, peptidase sensitive linkers, photolabile linkers, dimethyl linkers or disulfide bond-containing linkers (Chari et al.,Cancer Research 52: 127-131 (1992); US Patent No. 5,208,020). The anti-RTMC immunoconjugates of the present invention specifically cover but are not limited to ADCs prepared with crosslinker reagents: BMPS, EMCS, GMBS, HBVS, LC-SMCC, MBS, MPBH, SBAP, SIA, SIAB, SMCC, SMPB, SMPH , Sulfo-EMCS, sulfo-GMBS, sulfo-KMUS, sulfo-MBS, sulfo-SIAB, sulfo-SMCC and sulfo-SMPB, and SVSB (succinimide- (4-ethylene Base)), which is commercially available (for example from Pierce Biotechnology, Inc., Rockford, IL., USA). See pages 467-498, 2003-2004 Applications Handbook and Catalog.Pharmaceutical composition Also provided herein are compositions comprising anti-RTMC constructs (such as pharmaceutical compositions, also referred to herein as formulations). In some embodiments, the composition further comprises cells (such as effector cells, such as T cells) that bind to the anti-RTMC construct. In some embodiments, a pharmaceutical composition comprising an anti-RTMC construct and a pharmaceutically acceptable carrier is provided. In some embodiments, the pharmaceutical composition further comprises cells (such as effector cells, such as T cells) that bind to the anti-RTMC construct. Suitable formulations of anti-RTMC constructs are obtained by combining anti-RTMC constructs with the required purity with pharmaceutically acceptable carriers, excipients or stabilizers as appropriateRemington ' s Pharmaceutical Sciences 16th edition, Osol, A. (1980)) is obtained by mixing lyophilized formulations or aqueous solutions. Acceptable carriers, excipients or stabilizers are non-toxic to the recipient at the dosage and concentration used and include: buffers such as phosphates, citrates and other organic acids; antioxidants including ascorbic acid And methionine; preservatives (such as octadecyl dimethyl benzyl ammonium chloride; hexahydroxy ammonium chloride; benzalkonium chloride, benzethonium chloride; phenol, butanol or benzene Methanol; alkyl parabens, such as methyl paraben or propyl paraben; catechol; resorcinol; cyclohexanol; 3-pentanol; and m-cresol); low Polypeptides of molecular weight (less than about 10 residues); proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers, such as polyvinylpyrrolidone; amino acids, such as glycine, glutamic acid, Aspartic acid, histidine, arginine, or lysine; monosaccharides, disaccharides, and other carbohydrates, including glucose, mannose, or dextrin; chelating agents, such as EDTA; sugars, such as sucrose, mannitol, Trehalose or sorbitol; salt-forming counter ions, such as sodium; metal complexes (eg (Eg Zn-protein complex); and / or non-ionic surfactants such as TWEEN ™, PLURONICS ™ or polyethylene glycol (PEG). Exemplary formulations are described in WO98 / 56418, which is expressly incorporated herein by reference. Lyophilized formulations suitable for subcutaneous administration are described in WO97 / 04801. Such a lyophilized formulation can be reconstituted to a high protein concentration by a suitable diluent and the reconstituted formulation can be administered subcutaneously to the subject to be treated herein. Lipofectin / liposome can be used to deliver the anti-RTMC construct of the present invention into cells. The formulations herein may also contain one or more active compounds other than anti-RTMC constructs (depending on the needs of the particular indication being treated), preferably those with complementary activities that do not adversely affect each other. For example, it may be necessary to further provide anti-neoplastic agents, growth inhibitors, cytotoxic agents, or chemotherapeutic agents in addition to anti-RTMC constructs. Such molecules are preferably present in the combination in an amount effective for the intended purpose. The effective amount of such other agents depends on the amount of anti-RTMC constructs present in the formulation, the stage of HIV-1 infection, and other factors discussed above. These agents are generally used at about 1% to 99% of the same dose and route of administration as described herein or the doses used to date. It is also possible to embed the anti-RTMC construct in the prepared microcapsules by, for example, coagulation technology or interfacial polymerization, such as hydroxymethyl cellulose or gelatin microcapsules and poly- (methyl methacrylate) microcapsules Embedding in colloidal drug delivery systems (such as liposomes, albumin microspheres, microemulsions, nanoparticles and nanocapsules) or in giant emulsions. Such techniques are revealed inRemington ' s Pharmaceutical Sciences 16th edition, edited by Osol, A. (1980). Sustained-release preparations can be prepared. Sustained-release formulations against RTMC constructs can be prepared. Suitable examples of sustained-release preparations include semipermeable matrices of solid hydrophobic polymers containing antibodies (or fragments thereof), which matrices are in the form of shaped articles, such as films or microcapsules. Examples of sustained-release matrices include polyester, hydrogel (eg, poly (2-hydroxyethyl methacrylate) or poly (vinyl alcohol)), polylactide (US Patent No. 3,773,919), L-glutamine Copolymers of acid and ethyl-L-glutamine ester, non-degradable ethylene-vinyl acetate, such as Lupron DEPOTTM (injectable microspheres composed of lactic acid-glycolic acid copolymer and leuprolide acetate ) Of degradable lactic acid-glycolic acid copolymer and poly-D-(-)-3-hydroxybutyric acid. Although polymers such as ethylene-vinyl acetate and lactic acid-glycolic acid allow sustained release of molecules for more than 100 days, some hydrogels release proteins for a shorter period of time. If the encapsulated antibody remains in the body for a long time, it may be denatured or aggregated by exposure to water at 37 ° C, causing loss of biological activity and possible changes in immunogenicity. Depending on the relevant mechanism, a reasonable strategy for stabilizing the RTMC structure can be designed. For example, if the aggregation mechanism is found to form intermolecular SS bonds through sulfide-disulfide exchange, stabilization can be achieved by modifying sulfhydryl residues, freeze drying from acidic solutions, controlling moisture content, using appropriate additives and The specific polymer matrix composition is achieved. In some embodiments, the anti-RTMC construct is formulated in a buffer containing citrate, NaCl, acetate, succinate, glycine, polysorbate 80 (Tween 80), or any combination of the foregoing. In some embodiments, the anti-RTMC construct is formulated in a buffer containing about 100 mM to about 150 mM glycine. In some embodiments, the anti-RTMC construct is formulated in a buffer containing about 50 mM to about 100 mM NaCl. In some embodiments, the anti-RTMC construct is formulated in a buffer containing about 10 mM to about 50 mM acetate. In some embodiments, the anti-RTMC construct is formulated in a buffer containing about 10 mM to about 50 mM succinate. In some embodiments, the anti-RTMC construct is formulated in a buffer containing about 0.005% to about 0.02% polysorbate 80. In some embodiments, the anti-RTMC construct is formulated in a buffer with a pH between about 5.1 and 5.6. In some embodiments, the anti-RTMC construct is formulated in a buffer containing 10 mM citrate, 100 mM NaCl, 100 mM glycine, and 0.01% polysorbate 80, where the pH of the formulation is 5.5. The formulation administered in vivo must be sterile. This is easily achieved by, for example, filtration through a sterile filtration membrane.Use anti RTMC Constructive treatment The anti-RTMC construct and / or composition of the present invention can be administered to an individual (eg, a mammal, such as a human) to treat HIV-1 infection. Therefore, in some embodiments, the present application provides a method of treating HIV-1 infection in an individual, which comprises administering to the individual an effective amount of a composition (such as a pharmaceutical composition), the composition comprising an anti-RTMC antibody-containing portion Anti-RTMC constructs, such as any of the anti-RTMC constructs described herein. In some embodiments, the composition further comprises cells (such as effector cells) that bind to the anti-RTMC construct. For example, in some embodiments, there is provided a method of treating HIV-1 infection in an individual, which comprises administering to the individual an effective amount of a composition comprising a specific binding to a complex (including HIV-1 RT peptide and MHC class I protein) anti-RTMC constructs of anti-RTMC antibody part. In some embodiments, the HIV-1 RT peptide comprises (such as consisting of) the amino acid sequence of any one of SEQ ID NOs: 5-18. In some embodiments, the HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8) or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9). In some embodiments, the MHC class I protein is HLA-A02. In some embodiments, the MHC class I protein is HLA-A * 02: 01. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the composition further comprises cells (such as effector cells) that bind to the anti-RTMC construct. In some embodiments, the individual is a human. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex The complex contains HIV-1 RT 181 (SEQ ID NO: 5), HIV-1 RT 181 M184V (SEQ ID NO: 6), HIV-1 RT 181 M184I (SEQ ID NO: 7), HIV-1 RT 181 Y181C (SEQ ID NO: 8), or HIV-1 RT 181 Y181C, M184V (SEQ ID NO: 9) peptide and HLA-A * 02: 01. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the composition further comprises cells (such as effector cells) that bind to the anti-RTMC construct. In some embodiments, the individual is a human. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex The complex comprises HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody portion comprises: i) a heavy chain variable domain sequence, which comprises HC-CDR1, which comprises the amino acid of SEQ ID NO: 240 Sequence or variants comprising up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions; HC-CDR2, which comprises the amine of any of SEQ ID NOs: 241-244 Base acid sequence or variants comprising up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions; and HC-CDR3, which includes any of SEQ ID NO: 245-246 The amino acid sequence of it may comprise up to about 3 (eg about any of 1, 2, or 3) amino acid substituted variants thereof; and ii) the light chain variable domain comprising LC-CDR1, It comprises an amino acid sequence of any one of SEQ ID NO: 247-249 or a variant thereof comprising at most about 3 (eg, about any of 1, 2, or 3) amino acid substitutions; and LC -CDR3, its package SEQ ID NO: 250-253 in the amino acid sequence of any one of or contains up to about 3 (e.g. about 1, 2 or 3 according to any one of) amino acid substituted variants thereof. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex The complex contains HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody part contains: i) heavy chain variable domain sequence, which contains HC-CDR1, which contains the amino acid of SEQ ID NO: 240 Sequence; HC-CDR2, which contains the amino acid sequence of any one of SEQ ID NO: 241-244; and HC-CDR3, which contains the amino acid sequence of any one of SEQ ID NO: 245-246 ; And ii) a light chain variable domain comprising LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 247-249; and LC-CDR3 comprising SEQ ID NO: 250-253 Any one of the amino acid sequences. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the composition further comprises cells (such as effector cells) that bind to the anti-RTMC construct. In some embodiments, the individual is a human. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex This complex contains HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody part contains: i) heavy chain variable domain sequence, which contains HC-CDR1, which contains SEQ ID NO: 75-96 The amino acid sequence of any one or variants containing up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions; HC-CDR2, which includes SEQ ID NO : An amino acid sequence of any one of 97-124 or a variant thereof comprising at most about 5 (eg, any of about 1, 2, 3, 4, or 5) amino acid substitutions; and HC- CDR3, which contains the amino acid sequence of any one of SEQ ID NOs: 125-163 or contains up to about 5 (eg, about any of 1, 2, 3, 4, or 5) amino acid substitutions Variants thereof; and ii) a light chain variable domain sequence comprising LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189 or comprising up to about 5 (eg about 1, 2, 3, 4 or 5 One) amino acid substituted variants thereof; LC-CDR2, which contains the amino acid sequence of any one of SEQ ID NOs: 190-207 or contains up to about 3 (eg, about 1, 2 or 3) Any one of them) amino acid substituted variants thereof; and LC-CDR3, which comprises the amino acid sequence of any one of SEQ ID NO: 208-239 or contains up to about 5 (eg, about 1, 2 , Any of 3, 4 or 5) amino acid substituted variants thereof. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex This complex contains HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody part contains: i) heavy chain variable domain sequence, which contains HC-CDR1, which contains SEQ ID NO: 75-96 The amino acid sequence of any one; HC-CDR2, which includes the amino acid sequence of any one of SEQ ID NO: 97-124; and HC-CDR3, which includes any one of SEQ ID NO: 125-163 An amino acid sequence of one; or a variant comprising at most about 5 (eg, any of about 1, 2, 3, 4, or 5) amino acid substitutions included in the HC-CDR sequence; and ii ) Light chain variable domain sequence, which contains LC-CDR1, which contains the amino acid sequence of any one of SEQ ID NO: 164-189; LC-CDR2, which contains any of SEQ ID NO: 190-207 Amino acid sequence of one; and LC-CDR3, which contains the amino acid sequence of any one of SEQ ID NO: 208-239; or up to about 5 (eg, about 1, in the LC-CDR sequence) 2, 3, Either 4 or 5) amino acid substituted variants thereof. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex This complex contains HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody part contains: i) heavy chain variable domain sequence, which contains HC-CDR1, which contains SEQ ID NO: 75-96 The amino acid sequence of any one; HC-CDR2, which includes the amino acid sequence of any one of SEQ ID NO: 97-124; and HC-CDR3, which includes any one of SEQ ID NO: 125-163 The amino acid sequence of one; and ii) the light chain variable domain sequence, which comprises LC-CDR1, which comprises the amino acid sequence of any one of SEQ ID NO: 164-189; LC-CDR2, which comprises The amino acid sequence of any one of SEQ ID NO: 190-207; and LC-CDR3, which contains the amino acid sequence of any one of SEQ ID NO: 208-239. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the composition further comprises cells (such as effector cells) that bind to the anti-RTMC construct. In some embodiments, the individual is a human. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex The complex comprises HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody part comprises: a heavy chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 19-46 or Variants thereof having at least about 95% (e.g., at least about any of 96%, 97%, 98%, or 99%) sequence identity; and a light chain variable domain comprising SEQ ID NO: 47-74 The amino acid sequence of any of them or a variant thereof having at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity. In some embodiments, there is provided a method of treating HIV-1 infection in an individual comprising administering to the individual an effective amount of a composition comprising an anti-RTMC construct comprising an anti-RTMC antibody portion that specifically binds to the complex The complex comprises HIV-1 RT peptide and MHC class I protein, wherein the anti-RTMC antibody part comprises: a heavy chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 19-46; And a light chain variable domain comprising the amino acid sequence of any one of SEQ ID NO: 47-74. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the composition further comprises cells (such as effector cells) that bind to the anti-RTMC construct. In some embodiments, the individual is a human. For example, in some embodiments, the anti-RTMC construct included in a composition administered to an individual in a method of treating HIV-1 infection includes an anti-RTMC antibody portion containing heavy chain and light chain variable domains, heavy The chain and light chain variable domains include HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3 containing the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, 190 and 208, respectively SEQ ID NO: 76, 98, 126, 165, 191 and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, respectively SEQ ID NO: 85, 108, 137, 169 , 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198 and 220, respectively SEQ ID NO: 80, 102, 139, 174, 199 and 221, respectively SEQ ID NO: 79, 110 , 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO : 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 And 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, respectively SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151 , 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93 , 121, 154, 183, 204 and 233, SEQ ID NO: 92, 120, 155, 184, 191 and 2 respectively 14, respectively SEQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, respectively SEQ ID NO: 79, 110, 159, 187, 205 and 236, respectively SEQ ID NO: 92, 108, 160, 177, 191 and 218, respectively SEQ ID NO: 94, 122, 161, 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238, respectively SEQ ID NO: 96, 124, 163, 189, 207 and 239; or individually at HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1 and / or LC-CDR3 contain up to about 5 (e.g. about any of 1, 2, 3, 4 or 5) amino acid substitutions and And / or include variants of up to about 3 (eg, about any of 1, 2, or 3) amino acid substitutions in LC-CDR2. In some embodiments, the anti-RTMC construct included in a composition administered to an individual in a method of treating HIV-1 infection comprises an anti-RTMC antibody portion containing heavy and light chain variable domains, heavy and light chains The variable domain includes HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3 containing the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, respectively, 190 and 208, respectively SEQ ID NO: 76, 98, 126, 165, 191 and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198, and 220, respectively, SEQ ID NO: 80, 102, 139, 174, 199, and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively S EQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, SEQ ID NO: 79, 110, 159, 187, 205, and 236, respectively, SEQ ID NO: 92, 108, 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, respectively 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238, or SEQ ID NO: 96, 124, 163, 189, 207 and 239, respectively; or in the HC-CDR sequence Contains up to about 5 (such as about any of 1, 2, 3, 4, or 5) amino acid substitutions and / or up to about 5 (such as about 1, 2, 3, Either 4 or 5) amino acid substituted variants thereof. In some embodiments, the anti-RTMC construct included in a composition administered to an individual in a method of treating HIV-1 infection comprises an anti-RTMC antibody portion containing heavy and light chain variable domains, heavy and light chains The variable domain includes HC-CDR1, HC-CDR2, HC-CDR3, LC-CDR1, LC-CDR2 and LC-CDR3 containing the following amino acid sequences: SEQ ID NO: 75, 97, 125, 164, respectively, 190 and 208, respectively SEQ ID NO: 76, 98, 126, 165, 191 and 209, respectively SEQ ID NO: 77, 99, 127, 164, 192 and 210, respectively SEQ ID NO: 78, 100, 128, 166, 193 and 211, respectively SEQ ID NO: 79, 101, 129, 167, 194 and 212, respectively SEQ ID NO: 80, 102, 130, 168, 192 and 213, respectively SEQ ID NO: 81, 103, 131, 169, 191 and 214, respectively SEQ ID NO: 80, 104, 132, 170, 195 and 215, respectively SEQ ID NO: 76, 98, 133, 171, 196 and 216, respectively SEQ ID NO: 82, 105, 134, 164, 192 and 217, respectively SEQ ID NO: 83, 106, 135, 169, 191 and 218, respectively SEQ ID NO: 84, 107, 136, 172, 197 and 219, SEQ ID NO: 85, 108, 137, 169, 191 and 218, respectively SEQ ID NO: 86, 109, 138, 173, 198, and 220, respectively, SEQ ID NO: 80, 102, 139, 174, 199, and 221, respectively SEQ ID NO: 79, 110, 140, 164, 192 and 208, respectively SEQ ID NO: 87, 111, 141, 175, 200 and 222, respectively SEQ ID NO: 85, 108, 142, 176, 192 and 208, respectively SEQ ID NO: 80, 112, 143, 177, 191 and 223, respectively SEQ ID NO: 88, 113, 144, 178, 201 and 224, respectively SEQ ID NO: 82, 114, 145, 179, 202 and 225, respectively SEQ ID NO: 89, 115, 146, 175, 200 and 226, respectively SEQ ID NO: 90, 116, 147, 169, 191 and 227, respectively SEQ ID NO: 81, 117, 148, 169, 191 and 218, respectively SEQ ID NO: 82, 118, 149, 180, 199 and 228, SEQ ID NO: 82, 114, 150, 176, 200 and 229, respectively SEQ ID NO: 91, 119, 151, 181, 191 and 230, respectively SEQ ID NO: 92, 120, 152, 182, 203 and 231, respectively SEQ ID NO: 80, 102, 153, 164, 192 and 232, respectively SEQ ID NO: 93, 121, 154, 183, 204 and 233, respectively SEQ ID NO: 92, 120, 155, 184, 191 and 214, respectively S EQ ID NO: 80, 102, 156, 164, 192 and 234, respectively SEQ ID NO: 85, 108, 157, 185, 200 and 235, respectively SEQ ID NO: 85, 108, 158, 186, 191 and 218, SEQ ID NO: 79, 110, 159, 187, 205, and 236, respectively, SEQ ID NO: 92, 108, 160, 177, 191, and 218, SEQ ID NO: 94, 122, 161, respectively 173, 206 and 237, respectively SEQ ID NO: 95, 123, 162, 188, 200 and 238, or SEQ ID NO: 96, 124, 163, 189, 207 and 239, respectively. In some embodiments, the anti-RTMC construct included in a composition administered to an individual in a method of treating HIV-1 infection comprises an anti-RTMC antibody portion containing heavy and light chain variable domains, heavy and light chains The variable domain contains the following amino acid sequences: SEQ ID NO: 19 and 47, SEQ ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, respectively , SEQ ID NO: 23 and 51, SEQ ID NO: 24 and 52, SEQ ID NO: 25 and 53, SEQ ID NO: 26 and 54, SEQ ID NO: 27 and 55, respectively , SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, SEQ ID NO: 30 and 58 respectively, SEQ ID NO: 31 and 59 respectively, SEQ ID NO: 32 and 60 respectively , SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, SEQ ID NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, respectively , SEQ ID NO: 38 and 66, SEQ ID NO: 39 and 67, SEQ ID NO: 40 and 68, SEQ ID NO: 41 and 69, SEQ ID NO: 42 and 70, respectively , SEQ ID NO: 43 and 71, respectively, SEQ ID NO: 44 72, SEQ ID NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively; or individually having at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99% The variant of sequence identity. In some embodiments, the anti-RTMC antibody portion comprises heavy and light chain variable domains, the heavy chain and light chain variable domains comprise the following amino acid sequences: SEQ ID NOs: 19 and 47, respectively, SEQ ID NO: 20 and 48, SEQ ID NO: 21 and 49, SEQ ID NO: 22 and 50, SEQ ID NO: 23 and 51, SEQ ID NO: 24 and 52, SEQ ID, respectively NO: 25 and 53, respectively SEQ ID NO: 26 and 54, respectively SEQ ID NO: 27 and 55, respectively SEQ ID NO: 28 and 56, respectively SEQ ID NO: 29 and 57, respectively SEQ ID NO: 30 and 58, SEQ ID NO: 31 and 59, SEQ ID NO: 32 and 60, SEQ ID NO: 33 and 61, SEQ ID NO: 34 and 62, SEQ ID, respectively NO: 35 and 63, SEQ ID NO: 36 and 64, SEQ ID NO: 37 and 65, SEQ ID NO: 38 and 66, SEQ ID NO: 39 and 67, SEQ ID, respectively NO: 40 and 68, SEQ ID NO: 41 and 69, SEQ ID NO: 42 and 70, SEQ ID NO: 43 and 71, SEQ ID NO: 44 and 72, SEQ ID, respectively NO: 45 and 73, or SEQ ID NO: 46 and 74, respectively. In some embodiments, the anti-RTMC construct included in a composition administered to an individual in a method of treating HIV-1 infection includes an anti-RTMC antibody portion that includes the following heavy and light chain variable domains : Amino acid sequences of SEQ ID NOs: 27 and 55, or variants thereof that individually have at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity . In some embodiments, the anti-RTMC construct included in the composition administered to an individual in a method of treating HIV-1 infection comprises an anti-RTMC antibody portion containing a heavy chain variable domain and a light chain variable domain, the heavy chain And the light chain variable domain comprise the amino acid sequences of SEQ ID NO: 27 and 55, respectively. In some embodiments, the anti-RTMC construct included in a composition administered to an individual in a method of treating HIV-1 infection includes an anti-RTMC antibody portion that includes the following heavy and light chain variable domains : Amino acid sequences of SEQ ID NOs: 30 and 58, or variants thereof that individually have at least about 95% (eg, at least about any of 96%, 97%, 98%, or 99%) sequence identity . In some embodiments, the anti-RTMC construct included in a composition administered to an individual in a method of treating HIV-1 infection includes an anti-RTMC antibody portion that includes the following heavy and light chain variable domains : SEQ ID NO: amino acid sequence of 30 and 58. In some embodiments of any of the methods for treating HIV-1 infection described above, the anti-RTMC construct is combined with cells (such as immune cells, such as T cells) before administration to the individual . Thus, by way of example, a method of treating HIV-1 infection in an individual is provided, which comprises: a) combining any of the anti-RTMC constructs described herein with cells (such as immune cells, such as T cells) , Forming an anti-RTMC construct / cell conjugate, and b) administering an effective amount of a composition comprising an anti-RTMC construct / cell conjugate to an individual. In some embodiments, the cells are derived from individuals. In some embodiments, the cells are not derived from the individual. In some embodiments, the anti-RTMC construct is bound to the cell by a molecule covalently attached to the cell surface. In some embodiments, the anti-RTMC construct is bound to the cell by a molecule that is non-covalently attached to the cell surface. In some embodiments, the anti-RTMC construct is bound to the cell by inserting a portion of the anti-RTMC construct into the outer cell membrane. In some embodiments, the anti-RTMC construct is non-naturally occurring. In some embodiments, the anti-RTMC construct is a full-length antibody. In some embodiments, the anti-RTMC construct is a multispecific (such as bispecific) molecule. In some embodiments, the anti-RTMC construct is a chimeric antigen receptor. In some embodiments, the anti-RTMC construct is an immunoconjugate. In some embodiments, the individual is a human. In some embodiments, the individual is a mammal (eg, human, non-human primate, rat, mouse, cow, horse, pig, sheep, goat, dog, cat, etc.). In some embodiments, the individual is a human. In some embodiments, the individual is a clinical patient, clinical trial volunteer, laboratory animal, or the like. In some embodiments, the individual is less than about 60 years old (including, for example, any age less than about 50, 40, 30, 25, 20, 15, or 10 years old). In some embodiments, the individual is older than about 60 years of age (including, for example, any age greater than about 70, 80, 90, or 100 years old). In some embodiments, the individual is diagnosed with HIV-1 infection. In some embodiments, the present application provides for delivery of an anti-RTMC construct (such as any of the anti-RTMC constructs described herein) in an individual to present on its surface an HIV-1 RT peptide and A method of cells of a complex of MHC class I proteins, the method comprising administering to a subject a composition comprising an anti-RTMC construct. In some embodiments, the anti-RTMC construct to be delivered binds to cells (such as effector cells, such as T cells). Many diagnostic methods for HIV-1 infection are known in the art. Such methods include, but are not limited to, for example, immunohistochemistry, PCR, and fluorescent in situ hybridization (FISH). In some embodiments, the anti-RTMC constructs and / or compositions of the present invention are administered in combination with a second, third, or fourth agent (including, for example, antiviral drugs) to treat HIV-1 infection. In some embodiments, the anti-RTMC construct is administered in combination with an agent that increases MHC class I protein performance and / or enhances surface presentation of HIV-1 RT peptides by MHC class I protein. In some embodiments, agents include, for example, IFN receptor agonists, Hsp90 inhibitors, p53 performance enhancers, and chemotherapeutic agents. In some embodiments, the agent is an IFN receptor agonist, including, for example, IFNγ, IFNβ, and IFNα. In some embodiments, the agent is an Hsp90 inhibitor, including, for example, tanspiramycin (tanespimycin) (17-AAG), alvespimycin (17-DMAG), retaspimycin (IPI- 504), IPI-493, CNF2024 / BIIB021, MPC-3100, Debio 0932 (CUDC-305), PU-H71, Ganetespib (STA-9090), NVP-AUY922 (VER-52269), HSP990 , KW-2478, AT13387, SNX-5422, DS-2248 and XL888. In some embodiments, the agent is a p53 performance enhancer, including, for example, 5-fluorouracil and nutlin-3. In some embodiments, the agent is a chemotherapeutic agent, including, for example, topotecan, etoposide, cisplatin, paclitaxel, and vinblastine. In some embodiments, a method of treating HIV-1 infection in an individual is provided, wherein cells expressing HIV-1 RT are generally not presented on their surface, or are presented at a relatively low level containing HIV-1 RT protein and MHC class I Protein complex, the method comprising administering to a subject a composition comprising an anti-RTMC construct comprising a combination of agents that increase the performance of MHC class I proteins and / or enhance the surface presentation of HIV-1 RT peptides by MHC class I proteins . In some embodiments, agents include, for example, IFN receptor agonists, Hsp90 inhibitors, p53 performance enhancers, and chemotherapeutic agents. In some embodiments, the agent is an IFN receptor agonist, including, for example, IFNγ, IFNβ, and IFNα. In some embodiments, the agent is an Hsp90 inhibitor, including, for example, tamiromycin (17-AAG), aspiramycin (17-DMAG), retamycin (IPI-504), IPI-493, CNF2024 / BIIB021, MPC-3100, Debio 0932 (CUDC-305), PU-H71, Galitepi (STA-9090), NVP-AUY922 (VER-52269), HSP990, KW-2478, AT13387, SNX-5422, DS -2248 and XL888. In some embodiments, the agent is a p53 performance enhancer, including, for example, 5-fluorouracil and nutlin-3. In some embodiments, the agent is a chemotherapeutic agent, including, for example, topotecan, etoposide, cisplatin, paclitaxel, and vinblastine. Cancer treatment can be assessed, for example, by tumor regression, tumor weight or size contraction, time to progression, duration of survival, progression-free survival, total response rate, duration of response, quality of life, protein performance, and / or activity. Methods for determining the efficacy of therapy can be used, including, for example, measuring response via radiography. In some embodiments, the therapeutic efficacy is measured in terms of percent tumor growth inhibition (TGI%), which is calculated using the equation 100- (T / C × 100), where T is the average relative tumor volume of the treated tumor, and C is The average relative tumor volume of untreated tumors. In some embodiments, the TGI% is about 10%, about 20%, about 30%, about 40%, about 50%, about 60%, about 70%, about 80%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95% or greater than 95%.Cast against RTMC Dosage and method of structure composition The dose of the anti-RTMC construct composition administered to an individual (such as a human) can vary depending on the specific composition, the mode of administration, and the stage of HIV-1 infection. In some embodiments, the amount of the composition is effective to generate an undetectable viral load. In some embodiments, the amount of anti-RTMC construct composition is sufficient to produce a complete elimination of latent HIV reserves. In some embodiments, the amount of the composition is sufficient to extend the overall survival of the individual. In some embodiments, the amount of the composition (eg, when administered alone) is sufficient to produce greater than any of about 50%, 60%, 70%, or 77% in the population of individuals treated with the anti-RTMC construct composition The clinical benefit of the person. In some embodiments, the amount of the composition alone or in combination with the second, third, and / or fourth agent is the number of corresponding viral loads or HIV-1 infected cells in the same individual before treatment Compared, or compared with the corresponding value in other individuals who have not received treatment, is sufficient to reduce the viral load or reduce the number of HIV-1 infected cells by at least about 10%, 20%, 30%, 40%, 50%, 60% , 70%, 80%, 90%, 95%, or 100%. Standard methods can be used to measure the magnitude of this effect, such as by in vitro analysis of purified enzymes, cell-based analysis, animal models, or human testing. In some embodiments, the amount of anti-RTMC construct (eg, full-length anti-RTMC antibody, multispecific anti-RTMC molecule, anti-RTMC CAR, anti-RTMC abTCR, or anti-RTMC immunoconjugate) in the composition is lower than induced toxicology The level of effect (ie, an effect that is higher than the clinically acceptable toxicity level) may be at a level that can control or allow potential side effects when the composition is administered to an individual. In some embodiments, the amount of the composition is close to the maximum tolerated dose (MTD) of the composition following the same dosing regimen. In some embodiments, the amount of the composition is greater than any of about 80%, 90%, 95%, or 98% of the MTD. In some embodiments, the amount of anti-RTMC construct in the composition (eg, full-length anti-RTMC antibody, multispecific anti-RTMC molecule, anti-RTMC CAR, anti-RTMC abTCR, or anti-RTMC immunoconjugate) is included from about 0.001 μg to Within the range of about 1000 µg. In some embodiments of any of the above aspects, the anti-RTMC construct in the composition (eg full-length anti-RTMC antibody, multispecific anti-RTMC molecule, anti-RTMC CAR, anti-RTMC abTCR or anti-RTMC immunoconjugate) The amount is in the range of about 0.1 μg / kg total weight to about 100 μg / kg total weight. The anti-RTMC construct composition can be administered to an individual (such as a human) via various routes including, for example, intravenous, intraarterial, intraperitoneal, intrapulmonary, oral, inhalation, intravesicular, intramuscular, intratracheal, subcutaneous, Intraocular, intrathecal, transmucosal and percutaneous. In some embodiments, a continuous continuous release formulation of the composition may be used. In some embodiments, the composition is administered intravenously. In some embodiments, the composition is administered intraportally. In some embodiments, the composition is administered intra-arterially. In some embodiments, the composition is administered intraperitoneally. In other embodiments, the composition is administered intrahepatic. In some embodiments, the composition is administered by hepatic artery infusion.anti- RTMC Chimeric receptor effector cell therapy The present application also provides methods for using anti-RTMC chimeric receptors (such as anti-RTMC CAR or anti-RTMC abTCR) to redirect effector cells (such as primary T cells) to specificity including HIV-1 RT peptides and MHC class I proteins . Therefore, the present invention also provides a method for stimulating an effector cell-mediated response (such as a T cell-mediated immune response) against a target cell population or tissue (including RTMC presenting cells) in a mammal, which comprises administering to the mammal Steps with effector cells (such as T cells) that exhibit anti-RTMC CAR or anti-RTMC abTCR. Anti-RTMC chimeric receptor effector cells that exhibit anti-RTMC chimeric receptors (such as anti-RTMC CAR T cells or anti-RTMC abTCR T cells) can be infused to recipients in need. The infused cells can kill RTMC presenting cells in the recipient. In some embodiments, unlike antibody therapy, anti-RTMC chimeric receptor effector cells (such as T cells) are able to replicate in vivo, causing long-term persistence that can lead to continued tumor control. In some embodiments, the anti-RTMC chimeric receptor effector cells are anti-RTMC CAR T cells or anti-RTMC abTCR T cells that can withstand the expansion of solid T cells in vivo and can persist for an extended amount of time. In some embodiments, the anti-RTMC CAR T cells or anti-RTMC abTCR T cells of the invention develop into specific memory T cells that can be reactivated to inhibit the formation or growth of any additional tumors. The anti-RTMC chimeric receptor T cells (such as anti-RTMC CAR T cells or anti-RTMC abTCR T cells) of the present invention can also be used as a vaccine type for mammalian ex vivo immunization and / or in vivo therapy. In some embodiments, the mammal is a human. For in vitro immunization, at least one of the following occurs in vitro before the cells are administered to the mammal: i) expansion of the cells, ii) introduction of nucleic acids encoding anti-RTMC CAR or anti-RTMC abTCR into the cells , And / or iii) cryopreservation of cells. In vitro procedures are well known in the art and are discussed more fully below. Briefly, cells are isolated from mammals (preferably humans) and genetically modified (ie, transduced or transfected in vitro) with a vector expressing the anti-RTMC CAR or anti-RTMC abTCR disclosed herein. Anti-RTMC CAR cells or anti-RTMC abTCR cells can be administered to mammalian recipients to obtain therapeutic benefits. The mammalian recipient can be a human, and the anti-RTMC CAR or anti-RTMC abTCR cells can be autologous to the recipient. Alternatively, the cells may be allogeneic, homologous, or heterologous to the recipient. The procedure for ex vivo expansion of hematopoietic stem cells and progenitor cells is described in US Patent No. 5,199,942 (which is incorporated herein by reference) and can be applied to the cells of the present invention. Other suitable methods are known in the art, so the invention is not limited to any particular method of expanding cells ex vivo. Briefly, the in vitro culture and expansion of T cells includes: (1) CD34 collection from mammals through peripheral blood collection or bone marrow explants⁺ Hematopoietic stem cells and progenitor cells; and (2) Expansion of such cells in vitro. In addition to the cell growth factors described in US Patent No. 5,199,942, other factors such as flt3-L, IL-1, IL-3, and c-kit ligands can be used to culture and expand these cells. In addition to using cell-based vaccines for ex vivo immunization, the present invention also provides compositions and methods for in vivo immunization to elicit an immune response against an antigen in a patient. The anti-RTMC chimeric receptor effector cells (such as anti-RTMC CAR T cells or anti-RTMC abTCR T cells) of the present invention can be administered alone or as a diluent and / or other components (such as IL-2 or other interleukins (Or cell population) combination of pharmaceutical compositions. Briefly, the pharmaceutical composition of the present invention may comprise anti-RTMC chimeric receptor effector cells (such as T cells) in combination with one or more pharmaceutically or physiologically acceptable carriers, diluents or excipients . Such compositions may include: buffers such as neutral buffered saline, phosphate buffered saline and the like; carbohydrates such as glucose, mannose, sucrose or polydextrose, mannitol; proteins; polypeptides or such as glycine Amino acids; antioxidants; chelating agents, such as EDTA or glutathione; adjuvants (such as aluminum hydroxide); and preservatives. In some embodiments, the anti-RTMC chimeric receptor effector cell (such as T cell) composition is formulated for intravenous administration. The precise amount of the anti-RTMC chimeric receptor effector cell (such as anti-RTMC CAR T cell or anti-RTMC abTCR T cell) composition of the invention to be administered can be determined by the physician taking into account the age, weight, tumor size, infection or cancer metastasis of the individual The degree of difference and the patient (individual) symptoms are determined. In some embodiments, the pharmaceutical composition comprising anti-RTMC chimeric receptor effector cells (such as T cells)⁴ Up to about 10⁹ Dose per cell / kg body weight, such as any of the following: about 10⁴ Up to about 10⁵ , About 10⁵ Up to about 10⁶ , About 10⁶ Up to about 10⁷ , About 10⁷ Up to about 10⁸ Or about 10⁸ Up to about 10⁹ Cells / kg body weight, including all integer values in their range. The composition of anti-RTMC chimeric receptor effect cells (such as T cells) can also be administered multiple times at this same dose. Cells can be administered by using infusion techniques commonly known in immunotherapy (see, for example, Rosenberg et al., New Eng.  J.  of Med.  319: 1676, 1988). The optimal dose and treatment plan for a particular patient can be easily determined by those skilled in medicine by monitoring the patient's disease signs and adjusting the treatment accordingly. In some embodiments, it may be necessary to administer activated anti-RTMC chimeric receptor T cells (such as anti-RTMC CAR T cells or anti-RTMC abTCR T cells) to the individual, and then subsequently draw blood (or perform hemocytosis), According to the present invention, patients are re-infused from their activated T cells and with these activated and expanded T cells. This process can be performed multiple times every few weeks. In some embodiments, T cells can be activated from a blood draw of 10 cc to 400 cc. In some embodiments, T cells are activated from blood draws of 20 cc, 30 cc, 40 cc, 50 cc, 60 cc, 70 cc, 80 cc, 90 cc, or 100 cc. Administration of anti-RTMC chimeric receptor effector cells (such as anti-RTMC CAR T cells or anti-RTMC abTCR T cells) can be performed in any convenient manner, including by aerosol inhalation, injection, ingestion, infusion, implantation ). May be subcutaneous, intradermal, intratumoral, intranodular, intramedullary, intramuscular, or intravenous (i. v. ) Injection or intraperitoneal administration of the composition described herein to the patient. In some embodiments, The anti-RTMC chimeric receptor effector cell (such as T cell) composition of the present invention is administered to the patient by intradermal or subcutaneous injection. In some embodiments, The anti-RTMC chimeric receptor effector cell (such as T cell) composition of the present invention is administered by intravenous injection. Compositions of anti-RTMC chimeric receptor effector cells (such as T cells) can be injected directly into tumors, Lymph nodes or sites of infection.  therefore, For example, In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8) or HIV-1 RT 181 Y181C,  M184V (SEQ ID NO:  9). In some embodiments, The MHC class I protein is HLA-A02. In some embodiments, The MHC class I protein is HLA-A * 02: 01. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains specific binding to HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8) or HIV-1 RT 181 Y181C,  M184V (SEQ ID NO:  9) Peptide and HLA-A * 02: 01 anti-RTMC antibody part of the complex; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to a complex comprising HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of 240 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 241-244 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 245-246 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; And ii) light chain variable domain, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 247-249 may contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 250-253 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of 240; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 241-244; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 245-246; And ii) light chain variable domain, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 247-249; And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 250-253; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any of 75-96 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any of 97-124 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 125-163 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any of 164-189 may contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, LC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 190-207 may contain up to about 3 (such as about 1, Any one of 2 or 3) amino acid substituted variants thereof, And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 208-239 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 75-96; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 97-124; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 125-163; Or contain up to about 5 (such as about 1, in the HC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain sequence, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 164-189; LC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 190-207; And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 208-239; Or include up to about 5 (such as about 1, in the LC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 75-96; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 97-124; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 125-163; And ii) light chain variable domain sequence, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 164-189; LC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 190-207; And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 208-239; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46; Or have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) variants of sequence identity; And ii) light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74; Or have at least about 95% (including for example at least about 96%, 97%, 98% or 99%) variants of sequence identity; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC CAR (such as T cells), This anti-RTMC CAR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, This MHC class I protein contains the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46; And the light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  For example, In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239; Or in HC-CDR1 HC-CDR2, HC-CDR3, LC-CDR1 and / or LC-CDR3 individually include up to about 5 (e.g. about 1, 2, 3. Any of 4 or 5) amino acid substitutions and / or up to about 3 (e.g. Either 2 or 3) amino acid substituted variants thereof.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238 or SEQ ID NO:  96, 124, 163, 189, 207 and 239, Or contain up to about 5 (such as about 1, in the HC-CDR sequence 2, 3. Any one of 4 or 5) amino acid substitutions and / or include up to about 5 (such as about 1, 2, 3. Either 4 or 5) amino acid substituted variants thereof.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains contain the following amino acid sequences: SEQ ID NO:  19 and 47, SEQ ID NO:  20 and 48, SEQ ID NO:  21 and 49, SEQ ID NO:  22 and 50, SEQ ID NO:  23 and 51, SEQ ID NO:  24 and 52, SEQ ID NO:  25 and 53, SEQ ID NO:  26 and 54, SEQ ID NO:  27 and 55, SEQ ID NO:  28 and 56, SEQ ID NO:  29 and 57, SEQ ID NO:  30 and 58, SEQ ID NO:  31 and 59, SEQ ID NO:  32 and 60, SEQ ID NO:  33 and 61, SEQ ID NO:  34 and 62, SEQ ID NO:  35 and 63, SEQ ID NO:  36 and 64, SEQ ID NO:  37 and 65, SEQ ID NO:  38 and 66, SEQ ID NO:  39 and 67, SEQ ID NO:  40 and 68, SEQ ID NO:  41 and 69, SEQ ID NO:  42 and 70, SEQ ID NO:  43 and 71, SEQ ID NO:  44 and 72, SEQ ID NO:  45 and 73, Or SEQ ID NO:  46 and 74; Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, The anti-RTMC antibody part contains heavy and light chain variable domains, The heavy and light chain variable domains contain the following amino acid sequences: SEQ ID NO:  19 and 47, SEQ ID NO:  20 and 48, SEQ ID NO:  21 and 49, SEQ ID NO:  22 and 50, SEQ ID NO:  23 and 51, SEQ ID NO:  24 and 52, SEQ ID NO:  25 and 53, SEQ ID NO:  26 and 54, SEQ ID NO:  27 and 55, SEQ ID NO:  28 and 56, SEQ ID NO:  29 and 57, SEQ ID NO:  30 and 58, SEQ ID NO:  31 and 59, SEQ ID NO:  32 and 60, SEQ ID NO:  33 and 61, SEQ ID NO:  34 and 62, SEQ ID NO:  35 and 63, SEQ ID NO:  36 and 64, SEQ ID NO:  37 and 65, SEQ ID NO:  38 and 66, SEQ ID NO:  39 and 67, SEQ ID NO:  40 and 68, SEQ ID NO:  41 and 69, SEQ ID NO:  42 and 70, SEQ ID NO:  43 and 71, SEQ ID NO:  44 and 72, SEQ ID NO:  45 and 73, Or SEQ ID NO:  46 and 74.  In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion includes the following heavy and light chain variable domains: SEQ ID NO:  Amino acid sequence of 27 and 55, Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion contains SEQ ID NO:  The heavy and light chain variable domains of the amino acid sequences of 27 and 55. In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion includes the following heavy and light chain variable domains: SEQ ID NO:  The amino acid sequence of 30 and 58, Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, Anti-RTMC CAR contains anti-RTMC antibody part, The antibody portion contains SEQ ID NO:  The heavy and light chain variable domains of the amino acid sequences of 30 and 58.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein; And b) T cell receptor module (TCRM) capable of recruiting at least one TCR related signaling module. In some embodiments, The HIV-1 RT peptide is HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8) or HIV-1 RT 181 Y181C,  M184V (SEQ ID NO:  9). In some embodiments, The MHC class I protein is HLA-A02. In some embodiments, The MHC class I protein is HLA-A * 02: 01. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT 181 (SEQ ID NO:  5), HIV-1 RT 181 M184V (SEQ ID NO:  6), HIV-1 RT 181 M184I (SEQ ID NO:  7), HIV-1 RT 181 Y181C (SEQ ID NO:  8), Or HIV-1 RT 181 Y181C,  M184V (SEQ ID NO:  9) Peptide and HLA-A * 02: 01; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of 240 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 241-244 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 245-246 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; And ii) light chain variable domain, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 247-249 may contain up to about 3 (e.g. about 1, Any one of 2 or 3) amino acid substituted variants thereof, And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 250-253 may contain up to about 3 (e.g. about 1, Either 2 or 3) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of 240; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 241-244; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 245-246; And ii) light chain variable domain, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 247-249; And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 250-253; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any of 75-96 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any of 97-124 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 125-163 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any of 164-189 may contain up to about 5 (such as about 1, 2, 3. Any one of 4 or 5) amino acid substituted variants thereof, LC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 190-207 may contain up to about 3 (such as about 1, Any one of 2 or 3) amino acid substituted variants thereof, And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 208-239 may contain up to about 5 (such as about 1, 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 75-96; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 97-124; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 125-163; Or contain up to about 5 (such as about 1, in the HC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; And ii) light chain variable domain sequence, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 164-189; LC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 190-207; And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 208-239; Or include up to about 5 (such as about 1, in the LC-CDR sequence 2, 3. Either 4 or 5) Amino acid substituted variants; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain sequence, It contains HC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 75-96; HC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 97-124; And HC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 125-163; And ii) light chain variable domain sequence, It contains LC-CDR1, It contains SEQ ID NO:  The amino acid sequence of any one of 164-189; LC-CDR2, It contains SEQ ID NO:  The amino acid sequence of any one of 190-207; And LC-CDR3, It contains SEQ ID NO:  The amino acid sequence of any one of 208-239; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, The MHC class I protein contains i) the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46 may have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) variants of sequence identity, And ii) light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74 may have at least about 95% (including, for example, at least about 96%, 97%, 98% or 99%) variants of sequence identity; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  In some embodiments, Provide a method of treating individuals' HIV-1 infection, It comprises administering to the individual an effective amount of a composition comprising effector cells that exhibit anti-RTMC abTCR (such as T cells), The anti-RTMC abTCR contains: a) extracellular domain, It contains an anti-RTMC antibody portion that specifically binds to the complex, The complex contains HIV-1 RT peptide and MHC class I protein, This MHC class I protein contains the heavy chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 19-46; And the light chain variable domain, It contains SEQ ID NO:  The amino acid sequence of any one of 47-74; b) Transmembrane domain; And c) intracellular signaling domain, It includes CD3ζ intracellular signaling sequence and CD28 and / or 4-1BB intracellular signaling sequence. In some embodiments, The individual is human.  For example, In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2, And LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239, Or in HC-CDR1 HC-CDR2, HC-CDR3, LC-CDR1 and / or LC-CDR3 individually include up to about 5 (e.g. about 1, 2, 3. Any of 4 or 5) amino acid substitutions and / or up to about 3 (e.g. Either 2 or 3) amino acid substituted variants thereof.  In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239, Or contain up to about 5 (such as about 1, in the HC-CDR sequence 2, 3. Any one of 4 or 5) amino acid substitutions and / or include up to about 5 (such as about 1, 2, 3. Either 4 or 5) amino acid substituted variants thereof.  In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains include HC-CDR1 containing the following amino acid sequence HC-CDR2, HC-CDR3, LC-CDR1 LC-CDR2 and LC-CDR3: SEQ ID NO:  75. 97, 125, 164, 190 and 208, SEQ ID NO:  76, 98, 126, 165, 191 and 209, SEQ ID NO:  77, 99, 127, 164, 192 and 210, SEQ ID NO:  78. 100, 128, 166, 193 and 211, SEQ ID NO:  79, 101, 129, 167, 194 and 212, SEQ ID NO:  80, 102, 130, 168, 192 and 213, SEQ ID NO:  81. 103, 131, 169, 191 and 214, SEQ ID NO:  80, 104, 132, 170, 195 and 215, SEQ ID NO:  76, 98, 133, 171, 196 and 216, SEQ ID NO:  82. 105, 134, 164, 192 and 217, SEQ ID NO:  83. 106, 135, 169, 191 and 218, SEQ ID NO:  84, 107, 136, 172, 197 and 219, SEQ ID NO:  85. 108, 137, 169, 191 and 218, SEQ ID NO:  86, 109, 138, 173, 198 and 220, SEQ ID NO:  80, 102, 139, 174, 199 and 221, SEQ ID NO:  79, 110, 140, 164, 192 and 208, SEQ ID NO:  87, 111, 141, 175, 200 and 222, SEQ ID NO:  85. 108, 142, 176, 192 and 208, SEQ ID NO:  80, 112, 143, 177, 191 and 223, SEQ ID NO:  88, 113, 144, 178, 201 and 224, SEQ ID NO:  82. 114, 145, 179, 202 and 225, SEQ ID NO:  89. 115, 146, 175, 200 and 226, SEQ ID NO:  90, 116, 147, 169, 191 and 227, SEQ ID NO:  81. 117, 148, 169, 191 and 218, SEQ ID NO:  82. 118, 149, 180, 199 and 228, SEQ ID NO:  82. 114, 150, 176, 200 and 229, SEQ ID NO:  91, 119. 151, 181, 191 and 230, SEQ ID NO:  92, 120, 152, 182, 203 and 231, SEQ ID NO:  80, 102, 153, 164, 192 and 232, SEQ ID NO:  93, 121, 154, 183, 204 and 233, SEQ ID NO:  92, 120, 155, 184, 191 and 214, SEQ ID NO:  80, 102, 156, 164, 192 and 234, SEQ ID NO:  85. 108, 157, 185, 200 and 235, SEQ ID NO:  85. 108, 158, 186, 191 and 218, SEQ ID NO:  79, 110, 159, 187, 205 and 236, SEQ ID NO:  92, 108, 160, 177, 191 and 218, SEQ ID NO:  94, 122, 161 173, 206 and 237, SEQ ID NO:  95, 123, 162, 188, 200 and 238, Or SEQ ID NO:  96, 124, 163, 189, 207 and 239.  In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy and light chain variable domains contain the following amino acid sequences: SEQ ID NO:  19 and 47, SEQ ID NO:  20 and 48, SEQ ID NO:  21 and 49, SEQ ID NO:  22 and 50, SEQ ID NO:  23 and 51, SEQ ID NO:  24 and 52, SEQ ID NO:  25 and 53, SEQ ID NO:  26 and 54, SEQ ID NO:  27 and 55, SEQ ID NO:  28 and 56, SEQ ID NO:  29 and 57, SEQ ID NO:  30 and 58, SEQ ID NO:  31 and 59, SEQ ID NO:  32 and 60, SEQ ID NO:  33 and 61, SEQ ID NO:  34 and 62, SEQ ID NO:  35 and 63, SEQ ID NO:  36 and 64, SEQ ID NO:  37 and 65, SEQ ID NO:  38 and 66, SEQ ID NO:  39 and 67, SEQ ID NO:  40 and 68, SEQ ID NO:  41 and 69, SEQ ID NO:  42 and 70, SEQ ID NO:  43 and 71, SEQ ID NO:  44 and 72, SEQ ID NO:  45 and 73, Or SEQ ID NO:  46 and 74, Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, The anti-RTMC antibody part contains heavy and light chain variable domains, The heavy and light chain variable domains contain the following amino acid sequences: SEQ ID NO:  19 and 47, SEQ ID NO:  20 and 48, SEQ ID NO:  21 and 49, SEQ ID NO:  22 and 50, SEQ ID NO:  23 and 51, SEQ ID NO:  24 and 52, SEQ ID NO:  25 and 53, SEQ ID NO:  26 and 54, SEQ ID NO:  27 and 55, SEQ ID NO:  28 and 56, SEQ ID NO:  29 and 57, SEQ ID NO:  30 and 58, SEQ ID NO:  31 and 59, SEQ ID NO:  32 and 60, SEQ ID NO:  33 and 61, SEQ ID NO:  34 and 62, SEQ ID NO:  35 and 63, SEQ ID NO:  36 and 64, SEQ ID NO:  37 and 65, SEQ ID NO:  38 and 66, SEQ ID NO:  39 and 67, SEQ ID NO:  40 and 68, SEQ ID NO:  41 and 69, SEQ ID NO:  42 and 70, SEQ ID NO:  43 and 71, SEQ ID NO:  44 and 72, SEQ ID NO:  45 and 73, Or SEQ ID NO:  46 and 74.  In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody part, The antibody portion includes the following heavy and light chain variable domains: SEQ ID NO:  The amino acid sequences of 27 and 55 or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody part, The antibody portion contains SEQ ID NO:  The heavy and light chain variable domains of the amino acid sequences of 27 and 55. In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody parts containing heavy and light chain variable domains, The heavy chain and light chain variable domains comprise SEQ ID NO:  The amino acid sequence of 30 and 58, Or individually have at least about 95% (e.g. at least about 96%, 97%, 98% or 99%) sequence variants. In some embodiments, Anti-RTMC abTCR contains anti-RTMC antibody part, The antibody portion contains SEQ ID NO:  The heavy and light chain variable domains of the amino acid sequences of 30 and 58.Use anti RTMC Diagnosis and imaging method of structure The labeled anti-RTMC antibody portion and its derivatives and analogs that specifically bind to RTMC on the cell surface can be used for diagnostic purposes to detect, diagnose, or monitor HIV-1 infection. For example, the anti-RTMC antibody portion of the invention can be used for in situ, in vivo, ex vivo, and in vitro diagnostic analysis or imaging analysis. Other embodiments of the present invention include methods of diagnosing HIV-1 infection in an individual (eg, a mammal, such as a human). The method includes detecting RTMC presenting cells in the individual. In some embodiments, a method of diagnosing an HIV-1 infection in an individual (eg, a mammal, such as a human) is provided, which comprises: (a) administering an effective amount to the individual according to any of the embodiments described above The labeled anti-RTMC antibody portion of one; and (b) determining the level of the label in the individual, such that the label level is higher than the threshold level indicates that the individual has HIV-1 infection. The threshold level can be determined by various methods, including, for example, by the diagnostic methods described above in the first group of individuals with HIV-1 infection and the second group of individuals without HIV-1 infection. Measure the mark and set the threshold to a level that allows to distinguish between the first group and the second group. In some embodiments, the threshold level is zero, and the method includes determining the presence or absence of the marker in the individual. In some embodiments, the method further includes waiting for a certain time interval after the administration step (a) to allow the labeled anti-RTMC antibody portion to be preferentially concentrated at a site in the individual expressing RTMC (and for removing unbound labeled anti RTMC antibody section). In some embodiments, the method further includes subtracting the background level of the marker. The background level can be determined by various methods, including, for example, by detecting the label in the individual before administering the labeled anti-RTMC antibody portion, or by detecting the absence of the patient according to the diagnostic methods described above Markers in HIV-1 infected individuals. The anti-RTMC antibody portion of the present invention can be used to analyze the level of RTMC presenting cells in biological samples using methods known to those skilled in the art. Suitable antibody labels are known in the art and include enzyme labels, such as glucose oxidase; radioisotopes, such as iodine (¹³¹ I,¹²⁵ I,¹²³ I,¹²¹ I), carbon (¹⁴ C), sulfur (³⁵ S), tritium (³ H), indium (^115m In,^113m In,¹¹² In,¹¹¹ In), cu⁹⁹ Tc,^99m Tc), thallium (²⁰¹ Ti), gallium (⁶⁸ Ga,⁶⁷ Ga), palladium (¹⁰³ Pd), molybdenum (⁹⁹ Mo), Xenon (¹³³ Xe), fluorine (¹⁸ F), samarium (¹⁵³ Sm), 镏 (¹⁷⁷ Lu), Yao (¹⁵⁹ Gd), 鉕 (¹⁴⁹ Pm), lanthanum (¹⁴⁰ La), Ytterbium (¹⁷⁵ Yb), 鈥 (¹⁶⁶ Ho), yttrium (⁹⁰ Y), scandium (⁴⁷ Sc), rhenium (¹⁸⁶ Re,¹⁸⁸ Re) 、 鐠 (¹⁴² Pr), rhodium (¹⁰⁵ Rh) and Ruthenium (⁹⁷ Ru); luminol; fluorescent labels, such as fluorescein and rhodamine; and biotin. Techniques known in the art can be applied to the labeled anti-RTMC antibody portion of the invention. Such techniques include (but are not limited to) the use of bifunctional binders (see, eg, US Patent Nos. 5,756,065; 5,714,631; 5,696,239; 5,652,361; 5,505,931; 5,489,425; 5,435,990; 5,428,139 ; No. 5,342,604; No. 5,274,119; No. 4,994,560; and No. 5,808,003). In addition to the above analysis, those familiar with this technique can use various in vivo and in vitro analyses. For example, cells in the body of an individual can be exposed to portions of anti-RTMC antibodies optionally labeled with a detectable label (eg, radioisotope), and can be derived from previous exposure to anti-cancer, such as by external radioactive scanning or by analysis Samples of individuals with RTMC antibody portions (such as biopsies or other biological samples) evaluate the binding of anti-RTMC antibody portions to cells.Products and sets In some embodiments of the present invention, there is provided a material containing materials suitable for treating HIV-1 infection, for delivering anti-RTMC constructs to cells presenting RTMC on its surface, or for isolating or detecting individuals RTMC presents cell preparations. The product may include a container and a label or a package insert on or accompanying the container. Suitable containers include, for example, bottles, vials, syringes, and the like. The container may be formed of various materials, such as glass or plastic. In general, the container holds a composition effective for treating HIV-1 infection and may have a sterile access port (for example, the container may be an intravenous solution bag or vial with a stopper pierceable by a hypodermic injection needle). At least one active agent in the composition is the anti-RTMC construct of the present invention. The label or package insert indicates that the composition is used to treat a specific condition. The label or package insert will further include instructions for administering the anti-RTMC construct composition to the patient. Articles and kits containing the combination therapy described herein are also covered. A drug package insert refers to a package containing information about the indications, use, dosage, administration, contraindications and / or warnings related to the use of such therapeutic products, which are usually included in the package of commercially available therapeutic products. In some embodiments, the package insert indicates that the composition is used to treat HIV-1 infection. In addition, the product may further include a second container containing a pharmaceutically acceptable buffer, such as Bacteriostatic Water for Injection (BWFI), phosphate buffered saline, Ringer's solution, and dextrose solution. It may further include other substances required from a commercial and user point of view, including other buffers, diluents, filters, needles and syringes. Also provides kits suitable for various purposes, such as for the treatment of HIV-1 infection, for delivery of anti-RTMC constructs to cells presenting RTMC on their surface, or for the isolation or detection of RTMC presenting cells in individuals, Group, which is combined with the product as appropriate. The kit of the present invention includes one or more containers that contain an anti-RTMC construct composition (or unit dosage form and / or article), and in some embodiments, further includes any of the methods described herein Another medicament (as described herein) and / or instructions for use. The kit may further include instructions for selecting individuals suitable for treatment. The instructions supplied in the kit of the present invention are written instructions usually on the label or the instructions of the medicine (for example, including the paper in the kit), but the machine-readable instructions (for example, the instructions on the magnetic or optical storage disk) are also As acceptable. For example, in some embodiments, the kit includes a composition containing an anti-RTMC construct (eg, full-length anti-RTMC antibody, multispecific anti-RTMC molecule (such as bispecific anti-RTMC antibody), or anti-RTMC immunoconjugate) . In some embodiments, the kit comprises a) a composition comprising an anti-RTMC construct, and b) an effective amount of at least one other agent, wherein the other agent increases the performance of MHC class I protein and / or enhances HIV-1 RT peptide By surface presentation of MHC class I proteins (eg IFNγ, IFNβ, IFNα or Hsp90 inhibitors). In some embodiments, the kit includes a) a composition comprising an anti-RTMC construct, and b) instructions for administering an anti-RTMC construct composition to an individual for use in treating HIV-1 infection. In some embodiments, the kit comprises a) a composition comprising an anti-RTMC construct, b) an effective amount of at least one other agent, wherein the other agent increases the performance of MHC class I protein and / or enhances HIV-1 RT peptide Presented by the surface of MHC class I proteins (eg, IFNγ, IFNβ, IFNα, or Hsp90 inhibitors), and c) instructions for administering anti-RTMC construct compositions and other agents to individuals for the treatment of HIV-1 infection. Anti-RTMC constructs and other agents can be present in separate containers or single containers. For example, the kit may include a different composition or two or more than two compositions, where one composition includes an anti-RTMC construct and the other composition includes another agent. In some embodiments, the kit comprises a) a composition comprising an anti-RTMC construct (eg, a full-length anti-RTMC antibody, a multispecific anti-RTMC molecule (such as a bispecific anti-RTMC antibody), or an anti-RTMC immunoconjugate), and b) About combining anti-RTMC constructs with cells (such as cells derived from an individual, such as immune cells) to form a composition comprising an anti-RTMC construct / cell combination and administering the anti-RTMC construct / cell combination to an individual Instructions for the composition for the treatment of HIV-1 infection. In some embodiments, the kit comprises a) a composition comprising an anti-RTMC construct, and b) cells (such as cytotoxic cells). In some embodiments, the kit comprises a) a composition comprising anti-RTMC constructs, b) cells (such as cytotoxic cells), and c) regarding combining anti-RTMC constructs with cells to form an anti-RTMC construct / The composition of the cell conjugate and instructions for administering the anti-RTMC construct / cell conjugate composition to an individual for the treatment of HIV-1 infection. In some embodiments, the kit includes a composition containing an anti-RTMC construct that binds to cells, such as cytotoxic cells. In some embodiments, the kit includes a) a composition comprising an anti-RTMC construct that binds to cells (such as cytotoxic cells), and b) instructions for administering the composition to an individual for treatment of HIV-1 infection . In some embodiments, the binding is a molecule that binds to the cell surface by an anti-RTMC construct. In some embodiments, binding is by inserting a portion of the anti-RTMC construct into the outer cell membrane. In some embodiments, the kit comprises an anti-RTMC construct (eg, full-length anti-RTMC antibody, multispecific anti-RTMC molecule (such as bispecific anti-RTMC antibody), anti-RTMC CAR, anti-RTMC abTCR, or anti-RTMC immunoconjugate ) Or the nucleic acid (or nucleic acid collection) of its polypeptide part. In some embodiments, the kit contains a) a nucleic acid (or nucleic acid collection) encoding an anti-RTMC construct or a polypeptide portion thereof, and b) a host cell (such as an effector cell) that expresses the nucleic acid (or nucleic acid collection). In some embodiments, the kit comprises a) a nucleic acid (or nucleic acid collection) encoding an anti-RTMC construct or a polypeptide portion thereof, and b) with respect to i) exhibiting anti-RTMC in a host cell (such as an effector cell, such as a T cell) Constructs, ii) preparing a composition comprising an anti-RTMC construct or a host cell expressing an anti-RTMC construct, and iii) administering to a subject a composition comprising an anti-RTMC construct or a host cell expressing an anti-RTMC construct for use Instructions for the treatment of HIV-1 infection. In some embodiments, the host cell is derived from an individual. In some embodiments, the kit contains a) a nucleic acid (or nucleic acid collection) encoding an anti-RTMC construct or a polypeptide portion thereof, b) a host cell (such as an effector cell) used to express the nucleic acid (or nucleic acid collection), and c ) Regarding i) Expression of anti-RTMC constructs in host cells, ii) Preparation of a composition comprising anti-RTMC constructs or host cells expressing anti-RTMC constructs, and iii) Administration of anti-RTMC constructs or expression of anti-RTMC constructs to individuals The composition of the host cells of the RTMC construct is used in the instructions for the treatment of HIV-1 infection. In some embodiments, the kit comprises a nucleic acid encoding anti-RTMC CAR or anti-RTMC abTCR. In some embodiments, the kit comprises a vector containing a nucleic acid encoding anti-RTMC CAR or anti-RTMC abTCR. In some embodiments, the kit comprises a) a vector comprising a nucleic acid encoding anti-RTMC CAR or anti-RTMC abTCR, and b) with respect to i) introducing the vector into effector cells (such as T cells from an individual), ii) A composition comprising anti-RTMC CAR or anti-RTMC abTCR effector cells is prepared, and iii) instructions for administering an anti-RTMC CAR or anti-RTMC abTCR effector cell composition to an individual for the treatment of HIV-1 infection. The kit of the present invention is in a suitable package. Suitable packages include, but are not limited to, vials, bottles, cans, flexible packages (such as sealed Mylar or plastic bags), and the like. The kit can provide additional components such as buffer and descriptive information as appropriate. Therefore, the present application also provides articles including vials (such as sealed vials), bottles, cans, flexible packages, and the like. The instructions related to the use of anti-RTMC construct compositions generally include information about the dose of treatment desired, the timing of administration, and the route of administration. The container may be in unit dose, bulk (eg, multi-dose packaging), or sub-unit dose. For example, kits can be provided that contain sufficient doses of anti-RTMC constructs as disclosed herein (eg, full-length anti-RTMC antibodies, multispecific anti-RTMC molecules (such as bispecific anti-RTMC antibodies), anti-RTMC CAR Or anti-RTMC abTCR or anti-RTMC immunoconjugate) for an extended period of time, such as one week, 8 days, 9 days, 10 days, 11 days, 12 days, 13 days, 2 weeks, 3 weeks, 4 weeks, 6 weeks, 8 Any one of weeks, 3 months, 4 months, 5 months, 7 months, 8 months, 9 months or longer provides effective treatment for the individual. The kit may also include multiple unit doses of anti-RTMC constructs and pharmaceutical compositions and instructions for use and are packaged in an amount sufficient for storage and use in pharmacies (eg, hospital pharmacies and dispensing pharmacies).Illustrative embodiment Example 1. An isolated anti-RTMC construct comprising an antibody portion that specifically binds to a complex comprising human immunodeficiency virus 1 (HIV-1) reverse transcriptase (RT) peptide compatible with major tissues (MHC) Class I protein ("RTMC"). Example 2. An isolated anti-RTMC construct as in Example 1, wherein the HIV-1 RT / MHC class I complex is present on the cell surface. Example 3. The isolated anti-RTMC construct as in Example 1, wherein the HIV-1 RT / MHC class I complex is present on the surface of T cells. Embodiment 4. The isolated anti-RTMC construct of any one of embodiments 1 to 3, wherein the MHC class I protein is human leukocyte antigen (HLA) -A. Example 5. The isolated anti-RTMC construct as in Example 4, wherein the MHC class I protein is HLA-A02. Example 6. The isolated anti-RTMC construct as in Example 5, wherein the MHC class I protein is selected from the group consisting of: HLA-A * 02: 01, HLA-A * 02: 02, HLA-A * 02 : 06, HLA-A * 02: 07 and HLA-A * 02: 11. Example 7. The isolated anti-RTMC construct as in Example 6, wherein the MHC class I protein is HLA-A * 02: 01. Embodiment 8. The isolated anti-RTMC construct of any one of embodiments 1 to 7, wherein the antibody portion cross-reacts with a complex comprising the HIV-1 RT peptide and a second MHC class I protein, the second The MHC class I protein has an HLA dual gene that is different from the MHC class I protein. Embodiment 9. The isolated anti-RTMC construct of any one of embodiments 1 to 8, wherein the HIV-1 RT peptide is 8 to 12 amino acids in length. Embodiment 10. The isolated anti-RTMC construct of any one of embodiments 1 to 9, wherein the HIV-1 RT peptide is derived from the region corresponding to amino acids 181 to 189 of SEQ ID NO: 1. Embodiment 11. The isolated anti-RTMC construct according to any one of embodiments 1 to 10, wherein the HIV-1 RT peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 5-18. Example 12. The isolated anti-RTMC construct as in Example 10, wherein the HIV-1 RT peptide has the amino acid sequence of YQYVDDLYV (SEQ ID NO: 6). Example 13. The isolated anti-RTMC construct as in Example 12, wherein the isolated anti-RTMC construct cross-reacts with a complex comprising a variant of HIV-1 RT peptide and a complex of the MHC class I protein, the HIV-1 The RT peptide has the amino acid sequence of any one of YQYMDDLYV (SEQ ID NO: 5), YQYIDDLYV (SEQ ID NO: 7), CQYMDDLYV (SEQ ID NO: 8), or CQYVDDLYV (SEQ ID NO: 9). Example 14. An isolated anti-RTMC construct as in Example 10, wherein the HIV-1 RT peptide has the amino acid sequence of YQYMDDLYV (SEQ ID NO: 5). Example 15. The isolated anti-RTMC construct as in Example 14, wherein the isolated anti-RTMC construct cross-reacts with a complex comprising a variant of HIV-1 RT peptide and a complex of the MHC class I protein, the HIV-1 The RT peptide has an amino acid sequence of any of YQYVDDLYV (SEQ ID NO: 6), YQYIDDLYV (SEQ ID NO: 7), CQYMDDLYV (SEQ ID NO: 8), or CQYVDDLYV (SEQ ID NO: 9). Embodiment 16. The isolated anti-RTMC construct of any one of embodiments 1 to 15, wherein the antibody portion is human, humanized, synthetic, or semi-synthetic. Embodiment 17. The isolated anti-RTMC construct of any one of embodiments 1 to 16, wherein the antibody portion is a full-length antibody, Fab, Fab ', (Fab') 2, Fv, or single chain Fv (scFv). Embodiment 18. The isolated anti-RTMC construct of any one of embodiments 1 to 17, wherein the antibody portion binds to the HIV-1 RT / MHC with an equilibrium dissociation constant (Kd) of about 0.1 pM to about 500 nM Class I complex. Embodiment 19. The isolated anti-RTMC construct of any one of embodiments 1 to 18, wherein the isolated anti-RTMC construct binds to the HIV-1 RT / MHC I with a Kd of about 0.1 pM to about 500 nM Similar compounds. Embodiment 20. The isolated anti-RTMC construct of any one of embodiments 1 to 19, wherein the antibody portion comprises: i) a heavy chain variable domain comprising a heavy chain complementarity determining region (HC-CDR) 1, It contains the amino acid sequence of SEQ ID NO: 240 or its variant containing up to about 3 amino acid substitutions; HC-CDR2, which contains the amino acid sequence of any of SEQ ID NO: 241-244 Or a variant thereof comprising up to about 3 amino acid substitutions; and HC-CDR3, which comprises the amino acid sequence of any one of SEQ ID NOs: 245-246 or which comprises up to about 3 amino acid substitutions Variants; and ii) a light chain variable domain comprising: a light chain complementarity determining region (LC-CDR) 1, which comprises the amino acid sequence of any one of SEQ ID NOs: 247-249, or at most Variants with about 3 amino acid substitutions; and LC-CDR3, which contains the amino acid sequence of any one of SEQ ID NOs: 250-253, or variants containing up to about 3 amino acid substitutions body. Embodiment 21. The isolated anti-RTMC construct of any one of embodiments 1 to 19, wherein the antibody portion comprises: i) a heavy chain variable domain comprising HC-CDR1, which comprises SEQ ID NO: 75 to The amino acid sequence of any one of SEQ ID NO: 96, or a variant thereof containing up to about 5 amino acid substitutions; HC-CDR2, which comprises any one of SEQ ID NO: 97-124 An amino acid sequence, or a variant thereof containing up to about 5 amino acid substitutions; and HC-CDR3, which comprises the amino acid sequence of any one of SEQ ID NOs: 125-163, or up to about 5 Amino acid substituted variants thereof; and ii) a light chain variable domain comprising LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189 or comprising up to about 5 Amino acid substituted variants thereof; LC-CDR2, which comprises the amino acid sequence of any one of SEQ ID NOs: 190-207 or variants comprising up to about 3 amino acid substitutions; and LC- CDR3, which contains the amino acid sequence of any one of SEQ ID NO: 208-239 or a variant thereof that contains up to about 5 amino acid substitutions. Embodiment 22. The isolated anti-RTMC construct of any one of embodiments 1 to 19, wherein the antibody portion comprises: i) a heavy chain (HC) variable domain, which comprises HC-CDR1, which comprises SEQ ID NO : The amino acid sequence of any one of 75-96; HC-CDR2, which comprises the amino acid sequence of any one of SEQ ID NO: 97-124; and HC-CDR3, which comprises SEQ ID NO: The amino acid sequence of any one of 125-163; or variants containing up to about 5 amino acid substitutions in the HC-CDR regions; and ii) the light chain (LC) variable domain, which Comprising LC-CDR1, which comprises the amino acid sequence of any one of SEQ ID NO: 164-189; LC-CDR2, which comprises the amino acid sequence of any one of SEQ ID NO: 190-207; and LC-CDR3, which comprises the amino acid sequence of any one of SEQ ID NO: 208-239; or variants comprising up to about 5 amino acid substitutions in these LC-CDR regions. Embodiment 23. The isolated anti-RTMC construct of embodiment 21 or 22, wherein the antibody portion comprises: a) a heavy chain variable domain comprising the amino acid of any one of SEQ ID NOs: 19-46 Sequence or a variant thereof having at least about 95% sequence identity with any one of SEQ ID NO: 19-46; and b) a light chain variable domain comprising any one of SEQ ID NO: 47-74 The amino acid sequence of the variant or its variant having at least about 95% sequence identity with any of SEQ ID NOs: 47-74. Embodiment 24. The isolated anti-RTMC construct of Embodiment 23, wherein the antibody portion comprises: a heavy chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 19-46; and light A chain variable domain comprising the amino acid sequence of any one of SEQ ID NO: 47-74. Embodiment 25. The isolated anti-RTMC construct of any one of embodiments 1 to 24, wherein the isolated anti-RTMC construct is a full-length antibody. Embodiment 26. The isolated anti-RTMC construct of any one of embodiments 1 to 25, wherein the isolated anti-RTMC construct is monospecific. Embodiment 27. The isolated anti-RTMC construct of any one of embodiments 1 to 25, wherein the isolated anti-RTMC construct is multispecific. Example 28. The isolated anti-RTMC construct of Example 27, wherein the isolated anti-RTMC construct is bispecific. Embodiment 29. The isolated anti-RTMC construct of embodiment 27 or 28, wherein the isolated anti-RTMC construct is a tandem scFv, a bifunctional antibody (Db), a single chain bifunctional antibody (scDb), a double affinity Targeting (DART) antibodies, dual variable domain (DVD) antibodies, knob-into-hole (KiH) antibodies, dock and lock (DNL) antibodies, chemical cross-linking antibodies, heteromultimers Antibodies or heteroconjugate antibodies. Embodiment 30. The isolated anti-RTMC construct of embodiment 29, wherein the isolated anti-RTMC construct is a tandem scFv comprising two scFvs connected by a peptide linker. Example 31. The isolated anti-RTMC construct of Example 30, wherein the peptide linker comprises the amino acid sequence of SEQ ID NO: 276. Embodiment 32. The isolated anti-RTMC construct of any one of embodiments 27 to 31, wherein the isolated anti-RTMC construct further comprises a second antibody portion that specifically binds to a second antigen. Embodiment 33. The isolated anti-RTMC construct of embodiment 32, wherein the second antigen is an antigen on the surface of T cells. Example 34. The isolated anti-RTMC construct of Example 33, wherein the second antigen is selected from the group consisting of CD3γ, CD3δ, CD3ε, CD3ζ, CD28, OX40, GITR, CD137, CD27, CD40L, and HVEM. Embodiment 35. The isolated anti-RTMC construct of embodiment 33, wherein the second antigen is CD3ε, and wherein the isolated anti-RTMC construct is comprised of HIV-1 RT / MHC class I complex specific Tandem scFv of N-terminal scFv and C-terminal scFv specific for CD3ε. Embodiment 36. The isolated anti-RTMC construct of embodiment 33, wherein the T cells are selected from the group consisting of: cytotoxic T cells, helper T cells, and natural killer T cells. Embodiment 37. The isolated anti-RTMC construct of embodiment 32, wherein the second antigen is an antigen on the surface of natural killer cells, neutrophils, monocytes, macrophages, or dendritic cells. Embodiment 38. The isolated anti-RTMC construct of any one of embodiments 1 to 24, wherein the isolated anti-RTMC construct is a chimeric antigen receptor (CAR). Embodiment 39. The isolated anti-RTMC construct of embodiment 38, wherein the chimeric antigen receptor comprises an extracellular domain containing an antibody portion, a transmembrane domain, and an intracellular signaling sequence including CD3ζ and CD28 and / or 4-1BB The intracellular signaling domain of the intracellular signaling sequence. Embodiment 40. The isolated anti-RTMC construct of any one of embodiments 1 to 24, wherein the isolated anti-RTMC construct is a chimeric antibody / T cell receptor (abTCR), which includes a portion containing the antibody portion Extracellular domain and T cell receptor (TCR) module (TCRM) containing TCR transmembrane domain. Embodiment 41. The isolated anti-RTMC construct of Embodiment 40, wherein the TCRM is capable of recruiting at least one TCR-related signaling module. Embodiment 42. The isolated anti-RTMC construct of Embodiment 41, wherein the TCR-related signaling module is selected from the group consisting of CD3δε, CD3γε, and ζζ. Embodiment 43. The isolated anti-RTMC construct of any one of embodiments 40 to 42, wherein the antibody portion comprises: a) a first polypeptide chain comprising V-containing_H Antibody domain and C_H 1 the first antigen binding domain of the antibody domain; and b) the second polypeptide chain, which contains V_L Antibody domain and C_L The second antigen binding domain of the antibody domain, wherein the V of the first antigen binding domain_H Domain and the C_H 1 domain and the V of the second antigen binding domain_L Domain and C_L The domain forms a Fab-like antigen binding module that specifically binds to the RTMC. Embodiment 44. The isolated anti-RTMC construct of any one of embodiments 1 to 24, wherein the isolated anti-RTMC construct is an immunoconjugate comprising the antibody portion and an effector molecule. Embodiment 45. The isolated anti-RTMC construct of Embodiment 44, wherein the effector molecule is a therapeutic agent selected from the group consisting of drugs, toxins, radioisotopes, proteins, peptides, and nucleic acids. Embodiment 46. The isolated anti-RTMC construct of Embodiment 45, wherein the therapeutic agent is a drug or toxin. Example 47. The isolated anti-RTMC construct as in Example 44, wherein the effector molecule is a label. Embodiment 48. A host cell expressing the isolated anti-RTMC construct of any one of embodiments 1 to 47. Embodiment 49. A nucleic acid encoding one or more polypeptides contained in the isolated anti-RTMC construct of any one of embodiments 1 to 47. Embodiment 50. A vector comprising the nucleic acid as in Embodiment 49. Embodiment 51. An effector cell expressing the isolated anti-RTMC construct of any one of Embodiments 38 to 43. Embodiment 52. The effector cell of embodiment 51, wherein the effector cell is a T cell. Embodiment 53. A pharmaceutical composition comprising the isolated anti-RTMC construct of any one of Embodiments 1 to 46, the nucleic acid of Embodiment 49, the vector of Embodiment 50, or the effector cells of Embodiment 51 or 52. Embodiment 54. A method for detecting a cell presenting a complex comprising HIV-1 RT peptide and MHC class I protein on its surface, comprising contacting the cell with the isolated anti-RTMC construct of Example 47 , And detect the presence of markers on the cell. Embodiment 55. A method for treating an individual with HIV-1 infection, which comprises administering to the individual an effective amount of the pharmaceutical composition of Embodiment 53. Embodiment 56. A method for treating an individual suffering from HIV-1 infection, which comprises administering to the individual an effective amount of the effector cells of embodiment 51 or 52. Embodiment 57. A method of diagnosing an individual with HIV-1 infection, comprising: a) administering an effective amount of the isolated anti-RTMC construct of Example 47 to the individual; and b) measuring the marker in the individual Level, where the level of the mark is higher than the threshold level indicates that the individual has the HIV-1 infection. Embodiment 58. A method of diagnosing an individual with HIV-1 infection, comprising: a) contacting a sample derived from the individual with the isolated anti-RTMC construct of Example 47; and b) determining the presence of The number of cells bound to the isolated anti-RTMC construct, wherein the value of the number of cells bound to the isolated anti-RTMC construct is higher than the threshold indicates that the individual has the HIV-1 infection. Embodiment 59. The method of any one of embodiments 55 to 58, wherein the individual is human. Embodiment 60. The isolated anti-RTMC construct of any one of embodiments 1 to 19, wherein the HIV-1 RT peptide is HIV-1 RT 181, wherein the antibody portion comprises HC-CDR and LC-CDR sequences, And wherein the bispecific antibody as in Example 35 and comprising the HC-CDR and LC-CDR sequences of the isolated anti-RTMC construct is stable in aqueous solution formulations for at least about 2 years. Example 61. The isolated anti-RTMC construct as in Example 60, wherein the aqueous formulation is stored at about 4 ° C. Embodiment 62. The isolated anti-RTMC construct of embodiment 60 or 61, wherein the bispecific antibody in the aqueous solution formulation retains at least about 40% of its target cell killing activity for at least about 2 years. Embodiment 63. The isolated anti-RTMC construct of any one of embodiments 60 to 62, wherein the anti-RTMC construct is a bispecific antibody as in embodiment 35.Examples Those skilled in the art will recognize that several embodiments are possible within the scope and spirit of the present invention. The invention will now be described in more detail with reference to the following non-limiting examples. The following examples further illustrate the invention, but of course should not be interpreted as limiting its scope in any way.material Cell samples, cell lines and antibodies Cell lines include: liver adenocarcinoma cell line SK-HEP-1 (ATCC HTB-52, HLA-A2⁺ , HIV-1^- ) And lymphoblast cell line T2 (ATCC CRL-1992, HLA-A2⁺ , HIV-1^- ). T2 is a TAP-deficient cell line. The cell line was supplemented with 5% FCS, penicillin, streptomycin, 2 mmol / L glutamic acid and 2-mercaptoethanol at 37 ° C / 5% CO₂ Under cultivation. All peptides were purchased from and synthesized by Genemed Synthesis, Inc. (San Antonio, Tex.) Or Elim Biopharm (Hayward, CA). The purity of the peptide is> 90%. The peptide was dissolved in DMSO at 10 mg / mL and frozen at -80 ° C. By labeling peptides with recombinant HLA-A02 (BirA at the C-terminus, biotin-protein ligase from Avidity (Aurora, Colorado) for biotin labeling) and β-2 microglobulin (β2M) (~ 2M) Refold to prepare recombinant HIV-1 RT peptide / HLA-A * 02: 01 and control peptide / HLA-A * 02: 01 complex. 20 control peptides (P20, SEQ ID NO: 255-274) that bind HLA-A * 02: 01 are produced by the following 15 genes: BCR, BTG2, CALR, CD247, CSF2RA, CTSG, DDX5, DMTN, HLA-E , IFI30, IL7, PIM1, PPP2R1B, RPS6KB1, SSR1 and β-hemoglobin genes.Examples 1 . produce Biotinylated HIV - 1 RT / HLA - A * 02 : 01 Compound monomer The biotinylated HIV-1 RT / HLA-A * 02: 01 complex single system was prepared according to standard protocols (John D. Altman and Mark M. Davis,Current Protocols in Immunology 17.3.1-17.3.33, 2003). Briefly, DNA encoding full-length human β-2 microglobulin (β2m) was synthesized by Genewiz and cloned into the vector pET-27b. DNA encoding HLA-A * 02: 01 ECD-BSP (BirA substrate peptide (BSP) fused to the C-terminus of HLA-A * 02: 01 extracellular domain (ECD)) was also synthesized by Genewiz and cloned into the vector pET -27b. The vectors expressing human β2m and HLA-A * 02: 01 ECD-BSP were transformed into E. coli BL21 cells, respectively, and the expressed proteins were isolated from the bacterial culture in the form of inclusion bodies. Refolding the peptide ligand HIV-1 RT peptide 181 M184V (YQYVDDLYV, SEQ ID NO: 6) with human β2m and HLA-A * 02: 01 ECD-BSP to form HIV-1 RT peptide / HLA-A * 02:01 Complex monomer. The folded peptide / HLA-A * 02: 01 monomer was concentrated by ultrafiltration and further purified by size exclusion chromatography. HiPrep 26/60 Sephacryl S-300 HR was equilibrated with 1.5 column volume of Hyclone Dulbecco's phosphate buffered saline solution (Thermo Scientific, catalog number SH3002802). The unpurified sample was loaded on the column and dissolved with 1 column volume. The first peak corresponding to the misfolded aggregate dissolves at approximately 111 mL, the peak corresponding to the properly folded MHC complex is observed at 212 mL, and the peak corresponding to the free β2M is observed at 267 mL (data not shown) ). The peptide / HLA-A * 02: 01 monomer was labeled with biotin via BirA-mediated enzyme reaction. Biotin-labeled peptide / HLA-A * 02: 01 monomer was stored in PBS at -80 ° C. SDS-PAGE of purified HIV-1 RT peptide / MHC complex can be performed to determine protein purity. For example, mix 1 µg of protein complex with 2.5 µL NuPAGE LDS sample buffer (Life Technologies, NP0008) and bring it to a total of 10 µL with deionized water. The sample was heated at 70 ° C for 10 minutes, and then loaded onto the gel. Gel electrophoresis was performed at 180V for 1 hour.Examples 2 . Selection and characterization HIV - 1 RT / HLA - A * 02 : 01 Complex-specific scFv . Human scFv antibody phage display library constructed by Eureka therapy (diversity = 10 × 10¹⁰ ) Is used to select human mAb specific for HIV-1 RT 181 M184V / HLA-A * 02: 01 / β2M complex. Twenty-four human phage scFv libraries were used for panning HIV-1 RT / HLA-A * 02: 01 complex. In order to reduce the configuration change of the MHCI complex introduced by fixing the protein complex on the plastic surface, solution panning and cell panning are used instead of conventional plate panning. In the solution panning, the recombinant biotin-labeled antigen was first mixed with the human scFv phage library after prolonged washing with PBS buffer, and then, the antigen-scFv antibody phage complex was combined with streptavidin-dino beads (Dynabead) M-280 is pulled down through the track. Next, the combined pure line was lysed and used to infect E. coli XL1-Blue cells. In cell panning, T2 cells loaded with HIV-1 RT peptide were first mixed with human scFv phage libraries. T2 cell is TAP defective, HLA-A * 02: 01⁺ Lymphocyte cell line. To load peptides, T2 cells were pulsed with serum-free RPMI1640 medium containing peptides (50 µg / ml). After prolonged washing with PBS, T2 cells with peptide load bound to scFv antibody phage were subjected to rapid centrifugation. Next, the combined pure line was lysed and used to infect E. coli XL1-Blue cells. Next, the pure bacteriophage expressed in bacteria was purified. Perform 3 rounds of panning with any of solution panning, cell panning, or a combination of solution and cell panning to enrich scFv phage pure lines that specifically bind HIV-1 RT / HLA-A * 02: 01, and 1350 pure lines were selected for screening. The streptavidin ELISA plate is coated with monomer biotin-labeled HIV-1 RT 181 peptide / HLA-A * 02: 01 complex monomer or monomer biotin-labeled C3 control peptide / HLA-A * 02: 01 monomer. The C3 peptide is the peptide YLLPAIVHI (SEQ ID NO: 255) derived from the human nuclear protein p68. The individual phage pure lines from the enriched phage display panning pool relative to the HIV-1 RT 181 peptide / HLA-A * 02: 01 complex were cultivated in a coating dish. The binding of phage pure lines was detected by HRP-conjugated anti-M13 antibody and developed using HRP substrate. The absorbance is read at 450 nm. The 1,350 bacteriophage pure lines enriched from phage panning were screened by ELISA to identify 214 positive pure lines. By DNA sequencing 214 ELISA-positive bacteriophage pure lines, 39 unique pure lines were identified. By flow cytometry (FACS analysis), HIV-1 RT loaded live T2 cells were used to further test the binding of specific and unique pure lines to the HLA-A * 02: 01 / peptide complex on the cell surface. T2 cells were loaded with a control mixture of HIV-1 RT 181 WT peptide, HIV-1 RT 181 M184V peptide or 19 peptides (P19, SEQ ID NO: 255-273). Controls included T2 cells without peptide loading (T2), R-PE-conjugated horse anti-mouse IgG control (secondary antibody only), and cells stained with negative control phage (NC phage). Briefly, peptide-loaded T2 cells were first stained with purified scFv bacteriophage pure line, followed by a second staining with mouse anti-M13 mAb, and a third time with R-PE conjugated horse anti-mouse IgG from Vector Labs dyeing. Each staining step was performed on ice for between 30 and 60 minutes and the cells were washed twice between staining. As reported in Table 7, of the 39 tested pure lines, all 39 specifically recognized HIV-1 RT 181 M184V loaded T2 cells, and 37 also specifically recognized HIV-1 RT 181 WT loaded T2 cells. These bacteriophage pure lines specifically bind to HIV-1 RT-loaded T2 cells and do not recognize T2 cells loaded with the control peptide mixture P19 in the case of HLA-A * 02: 01, or T2 cells without peptide loading. To confirm peptide loading, T2-P19 cells and T2-RT 181 cells were stained with BB7.2 (an anti-HLA-A * 02 specific antibody). The peptide bound to the MHC complex stabilizes the MHC complex on the cell surface, and this stability change can be detected with BB7.2. Therefore, the fluorescent signal of T2 cells loaded with MHC binding peptide and stained with BB7.2 will be enhanced compared to T2 cells without peptide loading. BB7.2 binding data shows that the mixture of HIV-1 RT peptide and control peptide P19 can bind HLA-A * 02: 01 molecules and form a surface peptide / MHC complex, as seen in the change in MFI compared to T2 cells.table 7 On average, each nucleated cell in the human body exhibits approximately 500,000 different peptide / MHC class I complexes. In order to develop anti-peptide / MHCI complex antibodies as anti-cancer drugs with high specificity and therapeutic index, it is important for antibodies to specifically recognize the target peptide / MHCI complex, not the MHCI molecule itself, or bind to cells MHCI molecules of other peptides presented on the surface. Screen pure phage lines against a mixture of 19 endogenous HLA-A * 02: 01 peptides derived from proteins that are commonly expressed in many types of nucleated human cells, such as hemoglobin alpha chain, beta chain, nuclear Protein p68 and its analogs. As reported in Table 7, HIV-1 RT peptide / HLA-A * 02: 01 specific antibody bacteriophage pure line binds HIV-1 RT peptide / HLA-A * 02: 01 complex instead of folding with endogenous peptides The HLA-A * 02: 01 complex. We infer that the identified antibodies are specific to the HIV-1 RT peptide / HLA-A * 02: 01 complex and will not recognize HLA-A * 02 bound to other HLA-A * 02: 01 restricted peptides: 01 molecule.Examples 3 . FACS Positive HIV - 1 RT Characterization of specific bacteriophage pure lines HIV - 1 RT Peptide181 Cross reaction of variants The HIV-1 RT 181 peptide selected in the present invention is highly conserved among various HIV-1 strains. Selected from pure T2 cells for WT and M184V HIV-1 RT peptide 181-loaded FACS binding analysis using variant HIV-1 RT peptide-loaded live T2 cells by FACS analysis on HIV-1 RT on the surface of live cells The cross-reactivity of the peptide 181 variant / HLA-A * 02: 01 complex was further characterized. The variant peptide differs from the WT HIV-1 RT 181 peptide by one or two amino acids at positions 181 and / or 184. The tested peptide sequences include HIV-1 RT 181 M184V (YQYVDDLYV, SEQ ID NO: 6), HIV-1 RT 181 M184I (YQYIDDLYV, SEQ ID NO: 7), HIV-1 RT 181 Y181C (CQYMDDLYV, SEQ ID NO: 8) and HIV-1 RT 181 Y181C / M184V (CQYVDDLYV, SEQ ID NO: 9). Briefly, T2 cells are loaded with HIV-1 RT 181 peptide. Controls included T2 cells without peptide loading (T2). Peptide-loaded T2 cells were stained with purified scFv phage pure line, followed by a second stain with mouse anti-M13 mAb, and a third stain with R-PE-conjugated horse anti-mouse IgG from Vector Labs. Each staining step was performed on ice for 30 to 60 minutes and the cells were washed twice between each staining step. As reported in Table 8, of the 8 tested pure lines, 6 specifically recognized all HIV-1 RT 181 peptide-loaded T2 cells, and 2 of them could not bind to HIV-1 RT WT-loaded T2 cells, of which 1 Neither species can bind to T2 cells loaded with HIV-1 RT 181 Y181C or HIV-1 RT 181 Y181C / M184V. BB7.2 binding data shows that all HIV-1 RT peptides can bind HLA-A * 02: 01 molecules to form a surface peptide / MHC complex, but loaded with HIV-1 RT 181 Y181C or HIV-1 RT 181 Y181C / T2 cells of M184V displayed much higher surface performance than T2 cells loaded with other HIV-1 RT peptides (Figure 1).table 8 Epitope localization through alanine walking To accurately study the epitope for mAb recognition, HIV-1 RT peptides with alanine substitution at positions 1, 2, 3, 4, 5, 6, 7, 8, or 9 (Table 9) were pulsed to T2 On the cell surface. Then, FACS analysis was used to test the binding of antibody phage pure lines to the T2 cells loaded with these peptides. The average fluorescence intensity (MFI) value of each stain is shown in Table 9. All test antibody bacteriophage bacteriophages recognize the smaller configuration epitopes formed by the HIV-1 RT peptide and the surrounding MHC alpha chain residues, and the main peptide residues that interact with various antibodies seem to reside in the C-terminal half of the peptide Because most of the pure lines are sensitive to substitutions at positions 6 and 7 (Table 10). Based on BB7.2 binding, positions 5, 8, and 9 appear to affect peptide loading (Figure 1). Controls included T2 cells without peptide loading ("T2" in Table 10 and "T2 cells + secondary antibody" in Figure 1).table 9 table 10 Antibody binding specificity assessment for endogenous peptides Phage pure lines can also be screened against individual endogenous HLA-A * 02: 01 peptides, which are derived from proteins that are commonly expressed in many types of nucleated human cells, such as peptides contained in P20 (SEQ ID NO : 255-274). For example, a recombinant peptide / HLA-A * 02: 01 complex folded with 20 endogenous peptides (SEQ ID NO: 255-274) is coated on a streptavidin disc separately, and via ELISA analysis determines antibody binding. Briefly, individual phage pure lines were cultivated on a peptide / HLA-A * 02: 01 complex coated plate. The binding of phage pure lines was detected by HRP-conjugated anti-M13 antibody and developed using HRP substrate. The absorbance is read at 450 nm.Examples 4. Engineered bispecific antibody Bispecific antibodies (BsAb) were generated using scFv sequences of HIV-1 RT / HLA-A * 02: 01 specific phage pure lines. BsAbs is a single-chain bispecific antibody, which comprises a monoclonal scFv (SEQ ID NO: 277) fused to an anti-human CD3ε mouse at the C-terminal end by a BsAb linker (SEQ ID NO: 278) (Brischwein, K. et al.Molecular Immunology 43: 1129-1143, 2006) HIV-1 RT / HLA-A * 02: 01 pure bacteriophage specific line (from N-terminus to C-terminus: light chain variable region (LCVR), scFv linker (SEQ ID NO: 276), scFv sequence of heavy chain variable region (HCVR). The phage pure heavy and light chain variable regions used to produce BsAb are listed in Table 11. DNA fragments encoding HIV-1 RT scFv and anti-human CD3ε scFv were synthesized by Genewiz and sub-selected into Eureka mammalian expression vector pGSN-Hyg using standard DNA techniques. Six histamine tags are inserted into the C-terminal end for antibody purification and detection. Chinese hamster ovary (CHO) cells were transfected with BsAb expression vector, and then cultured for 7 days to produce BsAb antibodies. The CHO cell supernatant containing the secreted HIV-1 RT BsAb molecule was collected. BsAb was purified by affinity chromatography using HisTrap HP columns (GE healthcare) and AKTA FPLC system. Briefly, CHO cell culture was clarified and loaded onto the column at low imidazole concentration (20 mM), and then isocratic high imidazole concentration dissolution buffer (500 mM) was used to dissociate the bound BsAb protein. The purity and molecular weight of the purified HIV-1 RT BsAb can be determined by gel electrophoresis under reducing conditions. For example, 4 µg of protein is mixed with 2.5 µL NuPAGE LDS sample buffer (Life Technologies, NP0008) and brought to a total of 10 µL with deionized water. The sample was heated at 70 ° C for 10 minutes, and then loaded onto the gel. Gel electrophoresis was performed at 180V for 1 hour.table 11 Antibody aggregation can be assessed by size exclusion chromatography (SEC). For example, a 50 µL sample is injected into an SEC tube while flowing a buffer solution (adjusted to pH 7.0) consisting of Dulbecco's phosphate buffered saline (Fisher Scientific, SH30028.FS) and 0.2 M arginine. In a column (eg, Agilent, BioSEC-3, 300A, 4.6 × 300 mm). BsAbs with high molecular weight aggregation of less than 10% were selected for further characterization.Examples 5 . HIV - 1 RT BsAb Characterization of antibodies HIV - 1 RT BsAb Antibody binding affinity For example, by surface plasmon resonance (BiaCore), the binding affinity of HIV-1 RT BsAb and recombinant HIV-1 RT / HLA-A * 02: 01 complex is measured. For example, using the His Capture kit (GE Healthcare, catalog number 28995056) to measure HIV-1 RT BsAb and HIV-1 RT / HLA on Biacore X100 (GE Healthcare) according to the manufacturer ’s protocol for multi-cycle kinetic measurement A * 02: 01 The binding parameters between the complexes. All proteins used for analysis were diluted with HBS-E buffer. For example, 1 µg / mL of HIV-1 RT BsAb is fixed to a sensor chip pre-functionalized with antihistamine antibody by flowing the solution at 2 µL / min for 2 minutes through the flow cell 2 . Binding to HIV-1 RT / A * 02: 01 complex is analyzed at, for example, 0.19, 0.38, 7.5, 15 and 30 µg / mL. Each run consists of 3 minutes of binding and 3 minutes of dissociation at 30 µL / min. At the end of the cycle, the surface was regenerated using regeneration buffer from His Capture kit. The data was analyzed using BiaCore X-100 evaluation software using a 1: 1 binding site pattern. Next, calculate the binding parameter (binding rate constant k_a , Dissociation constant k_d And equilibrium dissociation constant K_d ).Peptide pulse T2 Of the cell T Cell killing analysis Tumor cytotoxicity was analyzed by LDH cytotoxicity analysis (Promega). Human T cells purchased from AllCells were activated and expanded by CD3 / CD28 Dynano beads (Invitrogen) according to the manufacturer's protocol. Activated T cells (ATC) were cultured and maintained in RPMI1640 medium with 10% FBS plus 30 U / ml IL-2 and used on days 7 to 14. According to FACS analysis, T cells are> 99% CD3⁺ . Activated αβ T cells (effector cells) and target peptide-loaded T2 cells were co-cultured with 1 µg / ml or 0.2 µg / ml BsAb at a ratio of 5: 1 for 16 hours. The peptide-loaded T2 was prepared by incubating T2 cells with 50 μg / ml of target HIV-1 RT 181 M184V (YQYVDDLYV, SEQ ID NO: 6) or control peptide mixture P20 (SEQ ID NO: 255-274) cell. Next, cytotoxicity was determined by measuring LDH activity in the culture supernatant. As shown in Figure 2, BsAbs 1, 4, 9, 10, 13, 14, 17, 27, 30, and 34 kill HIV-1 RT peptide-loaded T2 cells in a selective manner.With the cell line T cell Lethal analysis Target cell cytotoxicity was analyzed by LDH cytotoxicity analysis (Promega). Human T cells were purchased from AllCells and activated and expanded by CD3 / CD28 Dynabeads (Invitrogen) according to the manufacturer's protocol. Activated T cells (ATC) were cultured and maintained in RPMI1640 medium with 10% FBS plus 30 U / mL IL-2, and used on days 7 to 14. Activated T cells (effector cells) and target cancer cells were co-cultured at a 5: 1 ratio with different concentrations of BsAb (including for example 0.2, 0.04, 0.008, and 0.0016 μg / ml BsAb) for 16 hours. Next, cytotoxicity was determined by measuring LDH activity in the culture supernatant. The tested target cells include parental SK-Hep1 cells and stably express HIV-1 RT WT (SEQ ID NO: 1) (SK-Hep1 HIV-1 RT WT), HIV-1 RT M184V (SEQ ID NO: 3) (SK-Hep1 HIV-1 RT M184V) or SK-Hep1 cells of HIV-1 RT M184I (SEQ ID NO: 4) (SK-Hep1 HIV-1 RT M184I). As shown in FIG. 3, BsAb 1, 9, 10, 13, 14, 27, and 34 can specifically directly kill SK-Hep1 WT, M184V, and M184I cells, but not the parental SK-Hep1 cells. BsAb pure line 4 can specifically kill SK-Hep1 M184V and M184I cells directly, but not SK-Hep1 WT cells. BsAb 17 and 30 show evidence of non-specific killing. Other target cells that can be tested include T cells (such as CD4⁺ T cells), which are transduced to express HIV-1 RT WT (SEQ ID NO: 1), HIV-1 RT M184V (SEQ ID NO: 3) or HIV-1 RT M184I (SEQ ID NO: 4 ).HIV - 1 RT BsAb Antibodies against multiple HLA - A02 Cross-reactivity of dual genes Human MHCI molecules are composed of 6 classes of isoforms HLA-A, -B, -C, -E, -F and G. The HLA-A, -B and -C heavy chain genes are highly polymorphic. For each isoform, the HLA genes are additionally grouped according to the similarity of the heavy chain sequences. For example, HLA-A is divided into different dual genes, such as HLA-A01, -A02, -A03, and so on. For the HLA-A02 dual gene, there are multiple subtypes, such as HLA-A * 02: 01, A * 02: 02 and so on. Among the different subtypes of the HLA-A02 group, the sequence difference is limited to several amino acids. Therefore, in many cases, peptides bound to HLA-A * 02: 01 molecules can also form complexes with multiple subtypes of HLA-A02 dual genes. As shown in Table 12 (http://www.allelefrequencies.net/), although HLA-A * 02: 01 is the dominant HLA-A02 subtype in the Caucasian population, in Asia, A * 02: 05, A * 02: 06, A * 02: 07 and A * 02: 11 are also common HLA-A02 subtypes. The ability of HIV-1 RT antibodies to recognize HIV-1 RT peptides not only in HLA-A * 02: 01, but also in other subtypes of HLA-A02 will make it possible to benefit from HIV-1 RT antibody drug therapy The patient population has greatly widened. To measure cross-reactivity, HIV-1 RT / MHC class I complexes with other subtypes of HLA-A02 dual genes were generated and tested for antibodies specific to HIV-1 RT / HLA-A * 02: 01 for these other complexes Binding affinity of things. For example, ForteBio Octet QK is used to determine binding affinity. In short, the HIV-1 RT peptide / HLA-A02 MHC complex with 5 μg / mL biotin labeling of varying subtypes was loaded onto the streptavidin biosensor. After washing away excess antigen, BsAb is tested for binding and dissociation kinetics at, for example, 10 µg / mL. The binding parameters were calculated using a 1: 1 binding site and a partially fitted model.table 12 HIV - 1 RT BsAb Antibody stability Anti-RTMC BsAb pure lines No. 10, No. 14 and No. 27 were stored in formulation buffer (30 mM citric acid, 200 mM lysine, 0.05% polysorbate 80, pH 7) at 4 ° C for two years Target cell killing analysis as described above (using SK-Hep1 target cells expressing HIV-1 RT 181 WT small gene). The percentage specific lysis rate of pure line No. 10 was found to be ~ 48% (64% of the 75% level determined two years ago, as shown in Figure 3), and the percentage specific lysis rate of pure line No. 14 was found to be ~ 52% (69% of the 75% level determined two years ago, as shown in Figure 3), and found that the percentage of pure line No. 27 was ~ 4% than the lysis rate (5% of the 83% level determined two years ago ).Examples 6A . HIV - 1 RT / HLA - A * 02 : 01 Specific chimeric antigen receptor ( CAR ) Construction of the structure Chimeric antigen receptor therapy (CAR-T therapy) is a relatively novel form of targeted immunotherapy. It combines the acute targeting specificity of monoclonal antibodies with the strong cytotoxicity and long-term durability provided by cytotoxic T cells. This technology enables T cells to obtain long-term novel antigen specificity independent of endogenous TCR. Clinical trials have been conducted in neuroblastoma (Louis C.U. et al.,Blood 118 (23): 6050-6056), B-ALL (Maude S.L., etc.,N . Engl . J . Med . 371 (16): 1507-1517, 2014), CLL (Brentjens R.J. et al.,Blood 118 (18): 4817-4828, 2011) and B-cell lymphoma (Kochenderfer J.N. et al.,Blood . 116 (20): 4099-4102, 2010) shows the clinically significant antitumor activity of CAR-T therapy. In one study, 90% of the 30 patients with B-ALL treated with CD19-CAR T therapy reported a complete remission rate (Maude S.L. et al., Supra). To further explore the efficacy of HIV-1 RT / HLA-A * 02: 01 specific antibodies, a CAR containing anti-RTMC scFv was constructed and transduced into T cells. For example, a lentiviral CAR expression vector is used to construct HIV-1 RT / HLA-A * 02: 01 specific CARs. Transplant anti-HIV-1 RT / HLA-A * 02: 01 scFv to a signaling domain with a costimulatory signaling domain (such as from CD28 or 4-1BB) and a signaling domain from TCRζ (whichcis On the second generation of CAR (Mackall C.L. et al.,Nat . Rev . Clin . Oncol . 11 (12): 693-703, 2014) to provide intracellular T cell stimulation signals and activate T cells. For example, the anti-HIV-1 RT / HLA-A * 02: 01 scFv is grafted onto a CAR polypeptide having the amino acid sequence of SEQ ID NO: 279 or SEQ ID NO: 280.Examples 6B . HIV - 1 RT / HLA - A * 02 : 01 Specific chimeric antigen receptor ( CAR ) Construction of the structure HIV-1 RT / HLA-A * 02: 01 specific CAR uses HIV-1 RT / HLA-A * that produces anti-HIV CAR 10 (SEQ ID NO: 254) and anti-HIV CAR 14 (SEQ ID NO: 275) 02:01 The scFv sequences of phage-specific pure lines 10 and 14 were generated. Anti-HIV-1 RT / HLA-A * 02: 01 CAR contains HIV fused at its C-terminal end to a CAR polypeptide comprising CD3ζ intracellular signaling sequence and CD28 intracellular signaling sequence (SEQ ID NO: 279) -1 RT / HLA-A * 02: 01 phage-specific pure line (from N-term to C-term: light chain variable region (LCVR), scFv linker (SEQ ID NO: 276), heavy chain variable region (HCVR )) ScFv sequence. The heavy and light chain variable regions of phage pure lines used for CAR production are listed in Table 13.table 13 Examples 7 . HIV - 1 RT / HLA - A * 02 : 01 Specific chimeric antibody / TCR Receptor presentation T cell ( abTCR T cell ) Production Chimeric antibody / T cell receptor (abTCR) is regulated by a naturally occurring mechanism that controls TCR activation, and thus constitutive activation and the negative consequences associated with such activation can be avoided. The abTCRT cell signaling is expected to regulate and respond to endogenous T cell regulation and prove to increase persistence in vivo. To further explore the efficacy of HIV-1 RT / HLA-A * 02: 01 specific antibodies, anti-RTMC abTCR was constructed and transduced into T cells. For example, one or more lentiviral abTCR expression vectors are used to construct HIV-1 RT / HLA-A * 02: 01 specific abTCR. Transplant anti-HIV-1 RT / HLA-A * 02: 01 Fab-like antigen-binding module to the T cell receptor transmembrane module containing the T cell receptor subunit transmembrane domain to provide passage and endogenous TCR-associated signaling molecules (such as CD3δε, CD3γε, and ζζ) are associated with intracellular T cell stimulation signals and activated T cells. For example, an anti-HIV-1 RT / HLA-A * 02: 01 Fab-like antigen-binding module is grafted onto an abTCR polypeptide comprising the amino acid sequences of SEQ ID NO: 301 and 302.Examples 8A . anti- RTMC Chimeric receptor T cell Characterization anti- RTMC Chimeric receptor T cell In vitro cytotoxicity study For example, by transfecting 293T cells with anti-RTMC CAR vector or anti-RTMC abTCR vector, to generate HIV-1 RT / HLA-A * 02: 01 specific chimeric antigen receptor (CAR) or chimeric antibody TCR (abTCR) lentivirus. Human T cells were used for transduction in the presence of interleukin-2 at 30 U / ml after stimulation with CD3 / CD28 beads (Dynabeads®, Invitrogen) for 2 days. The concentrated lentivirus was coated on a 6-well plate coated with Retronectin (Takara) containing T cells for 72 hours. The transduction efficiency was assessed by FACS using biotin-labeled HIV-1 RT tetramer and PE-conjugated streptavidin. The FACS analysis was repeated at 72 hours and every 3 to 4 days thereafter. The functional evaluation of transduced T cells (anti-RTMC CAR T cells or anti-RTMC abTCR T cells) was performed using LDH cytotoxicity analysis. The ratio of effector cells to target cells used includes, for example, 5: 1 and 10: 1. Target cell lines may include, for example, SK-HEP-1 (ATCC HTB-52, HLA to A2⁺ , HIV-1^- ), T cell leukemia cell line Jurkat (ATCC TIB-152, HLA-A2^- , HIV-1^- ), Leukemia cell line K562 (ATCC CCL-243, HLA-A2^- , HIV-1^- ) And primary T cells, such as CD4⁺ T cells. SK-HEP-1, Jukat, K562 and primary T cells encode WT HIV-1 RT (SEQ ID NO: 1), M184V HIV-1 RT (SEQ ID NO: 3) or M184I HIV-1 RT (SEQ ID NO : 4) HIV-1 RT expresses small gene cassette transduction, which produces a higher level of cell surface performance of HIV-1 RT peptide / HLA-A * 02: 01 complex. The specificity and efficiency of T cells expressing anti-RTMC CAR or T cells expressing anti-RTMC abTCR to kill target positive cells were determined using LDH analysis as described above.anti- RTMC Chimeric receptor T cell Virus suppression research Anti-RTMC chimeric receptor T cells (anti-RTMC CAR T cells or anti-RTMC abTCR T cells) were generated as described above. PBMC were treated with RPMI-1640 containing 1 mg / ml PHA and 10 ng / ml IL-2 + 10% FBS for 2 days. CD4⁺ T cells are isolated by negative selection using magnetic beads and infected with various HIV strains (eg NL4-3, Bal and SF162). After 48 hours, the cells were washed with fresh medium. Infect HIV with CD4⁺ T cells and CD8 transduced with anti-RTMC CAR or anti-RTMC abTCR⁺ T cells are mixed at an exemplary effect target ratio of 5: 1 or 1: 1. Every 2 days (for 8 days) the intracellular p24 (Gag) level is measured by flow cytometry. In short, HIV infected CD4⁺ T cells are stained with antibodies to CD4, CD8 and p24 using, for example, FIX & PERM® Cell Fixation & Cell Permeabilization kit. For examples of virus suppression studies, see Varela-Rohena, A. et al. (2008)Nature medicine 14 (12): 1390-1395.anti- RTMC Chimeric receptor transduced CD8 ⁺ T cell Respond to HIV infected CD4 ⁺ T cell Proliferation The purpose of this experiment is to measure CD8 transduced with anti-RTMC CAR or anti-RTMC abTCR⁺ T cells respond to CD4 exposure to HIV infection⁺ T cell proliferation ability. HIV-infected CD4⁺ T cells are produced as described above. The target cells are irradiated with, for example, high dose gamma radiation (eg, 10,000 rads). Anti-RTMC chimeric receptor T cells (anti-RTMC CAR T cells or anti-RTMC abTCR T cells) were labeled with Cell Trace Violet (ThermoFisher) according to the manufacturer's instructions. The target cells and anti-RTMC chimeric receptor T cells are mixed in a ratio of, for example, 1: 1. After 3 days, the medium was changed, and after 7 days, the cells were measured to track purple fluorescence. For examples of proliferation studies, see Ali, A. et al. (2016)Journal of virology JVI-00805. CD8 transduced by activated anti-RTMC chimeric receptor⁺ T cell cytokine release The purpose of this analysis is to measure the activation of CD8⁺ Anti-RTMC chimeric receptor T cells (anti-RTMC CAR T cells or anti-RTMC abTCR T cells) in response to HIV-infected CD4⁺ T cell cytokines are released. For CD8 by transduction⁺ For examples of analysis of T cell production of cytokines, see Varela-Rohena, A. et al. (2008)Nature medicine 14 (12): 1390-1395. HIV-infected CD4⁺ T cells are produced as described above. For example, target cells and anti-RTMC chimeric receptor T cells are mixed at an exemplary E: T ratio of 1: 1 or 1: 8. For example, ELISA kit analysis using Granzyme B (Neobioscience), IL-2 (MultiSciences, Lianke Biotech) and IFN-γ from CD8⁺ Interleukin release of chimeric receptor T cells. See for example Liu, B. et al. (2016)Journal of Virology JVI-00852.Examples 8B . anti- RTMC CAR T cell Characterization anti- RTMC Chimeric receptor T cell In vitro cytotoxicity study Lentivirus encoding HIV-1 RT / HLA-A * 02: 01 specific CAR by using anti-RTMC CAR encoding anti-HIV CAR 10 (SEQ ID NO: 254) and anti-HIV CAR 14 (SEQ ID NO: 275) Produced by vector-transfected 293T cells. Human T cells were used for transduction in the presence of interleukin-2 at 30 U / ml after stimulation with CD3 / CD28 beads (Dynabeads®, Invitrogen) for 1 day. The concentrated lentivirus (MOI 3: 1) was applied to a 6-well plate coated with Retronectin (Takara) containing T cells for 72 hours. Mock-transfected T cells were also prepared for use as controls. The transduction efficiency was assessed by FACS using biotin-labeled HIV-1 RT tetramer and PE-bound streptavidin (Figure 4). The functional evaluation of transduced T cells (anti-HIV CAR 10 T cells or anti-HIV CAR 14 T cells) and simulated T cells on day 9 of IL-2 growth was performed using LDH cytotoxicity analysis. To roughly 1 × 10⁵ Each target cell / well uses an effective target ratio of 5: 1. Target cell lines include SK-HEP-1 control cells (ATCC HTB-52, HLA-A2⁺ , HIV-1^- ) And SK-HEP-1-MG, the SK-HEP-1-MG is transduced by a small gene cassette encoding HIV-1 RT peptide encoding WT HIV-1 RT 181-189 (SEQ ID NO: 5) Prepared from parental SK-HEP-1 cells, producing a higher level of cell surface performance of HIV-1 RT 181-189 / HLA-A * 02: 01 complex. The specificity and efficiency of T cells expressing anti-RTMC CAR to kill target positive cells was determined using LDH analysis as described above (Figure 5). Both T cells expressing anti-RTMC CAR kill target-positive SK-HEP-1-MG cells in a specific and efficient manner. However, the same T cells poorly recognize target-negative wild-type SK-HEP1 cells. These results indicate that the antibody pure line is highly specific for cells expressing HIV RT and does not mediate non-specific killing of cell lines that do not express HIV RT.Examples 9 . full length IgG1 HIV - 1 RT Antibody production and characterization For example, full-length human IgG1 of the selected bacteriophage pure line is produced in HEK293 and Chinese hamster ovary (CHO) cell lines as described (Tomimatsu K. et al.,Biosci . Biotechnol . Biochem . 73 (7): 1465-1469, 2009). Briefly, antibody variable regions are sub-cloned into mammalian expression vectors with matching human lambda or kappa light chain constant region and human IgG1 constant region sequences. Using the same colonization strategy, chimeric anti-HIV-1 RT peptide / MHC full-length antibodies with mouse IgG1 heavy and light chain constant regions were generated. Under both reducing and non-reducing conditions, the molecular weight of the purified full-length IgG antibody was measured by electrophoresis. SDS-PAGE of purified HIV-1 RT mouse chimeric IgG1 antibody was performed to determine protein purity. Briefly, 2 µg of protein was mixed with 2.5 µL NuPAGE LDS sample buffer (Life Technologies, NP0008) and brought to a total of 10 µL with deionized water. The sample was heated at 70 ° C for 10 minutes, and then loaded onto the gel. Gel electrophoresis was performed at 180V for 1 hour. By flow cytometry, test anti-HIV-1 RT peptide / MHC chimeric IgG1 antibody and HIV-1 RT presenting cells (such as SK-Hep1, Jurkat, K562 and transduced with a small gene cassette as described above Beginner CD4⁺ Cells). The HIV-1 RT small gene cassette (expressing WT, M184V or M184I HIV-1 RT) is transfected into cells to produce HIV-1 RT presenting target cells. Add 10 µg / mL antibody to the cells on ice for 1 hour. After washing, R-PE-conjugated anti-mouse IgG (H + L) (Vector Labs # EI-2007) was added to detect antibody binding. The binding affinity of mouse chimeric IgG1 anti-HIV-1 RT peptide / MHC antibody was determined by ForteBio Octet QK. Load the 5 µg / mL biotin-labeled HIV-1 RT peptide / HLA-A * 02: 01 complex onto the streptavidin biosensor. After washing away excess antigen, the binding and dissociation kinetics of the mouse chimeric full-length antibody were tested at 10 µg / mL. The binding parameters were calculated using a 1: 1 binding site and a partially fitted model. The binding of HIV-1 RT specific and negative control mouse chimeric IgG1 to HIV-1 RT / HLA-A * 02: 01, HIV-1 RT recombinant protein and free HIV-1 RT 181 peptide was tested in ELISA analysis. Antibodies are tested, for example, at 3 × serial dilutions, starting at 100 ng / mL for a total of 8 concentrations. Biotinylated HIV-1 RT / A * 02: 01 MHC was applied to streptavidin discs at 2 µg / mL, HIV-1 RT protein was applied at 2 µg / mL and HIV-1 RT peptide was applied at 40 ng / mL coating. The ability of the full-length anti-HIV-1 RT / HLA-A * 02: 01 antibody in the case of HLA-A02 to recognize only the HIV-1 RT peptide and does not bind recombinant HIV-1 RT protein or free HIV-1 RT peptide.Examples 10 . In vivo effect research Antibodies in mice RTMC Chimeric receptor T cell treatment Anti-RTMC chimeric receptor T cells (such as anti-RTMC CAR T cells or anti-RTMC abTCR cells) are evaluated in a mouse model of HIV infection. For examples of such mouse models, see Akkina, R. (2013)Virology 435 (1): 14-28. For example, human peripheral blood mononuclear cells (PBMC), human hematopoietic stem cells (HSC), thymus cells, liver cells and / or from HLA-A2⁺ Bone marrow cells from the source are transplanted into NOD SCIDγ (NSG) mice to produce humanized NSG mice. Next, such as by rectal or vaginal vaccination of HIV-1, mice are infected with HIV. Mice are divided into at least 3 groups that receive one of: (i) no treatment; (ii) mock treatment; or (iii) anti-RTMC constructs (such as BsAb) or anti-RTMC chimeric receptor T cells (Anti-RTMC CAR T cells or anti-RTMC abTCR T cells) treatment. Monitor animals in each group for HIV-associated disease pathology, CD4⁺ T cell level, HIV viral load, body weight, and general health status (eating, walking, daily activities).Examples 11 . anti- HIV - 1 RT Compatibility and maturity of antibody agents This example describes the affinity maturation of anti-HIV-1 RT antibody agents. In particular, this example specifically describes the generation of a series of antibody variants by incorporating random mutations into representative anti-HIV-1 RT antibodies followed by screening and characterization of antibody variants. Generation of variant phage libraries DNA encoding anti-HIV-1 RT peptide / MHC scFv was subjected to random mutation induction using GeneMorph II random mutation induction kit (Agilent Technologies) according to the manufacturer's instructions. After the mutation induction, the DNA sequence is cloned into a phage plastid vector expressing scFv to establish that it contains, for example, about 5 × 10⁸ A phage library of variant human antibody phage from a unique phage pure line. On average, the variant pure line has two nucleotide mutations compared to the parental anti-HIV-1 RT peptide / MHC pure line with each scFv sequence in the range of 1 to 4 nucleotide mutations.Cell panning The human phage scFv library with mutations was used for panning for HIV-1 RT 181 peptide / HLA-A * 02: 01 complex as described in Example 2. In particular, cell panning is used. For example, a human scFv phage library is first mixed with T2 cells loaded with 20 different endogenous peptides (P20, SEQ ID NO: 255-274) pool of 50 μg / ml, and panned as a negative control. Next, the human scFv phage library lacking the negative control was mixed with T2 cells loaded with HIV-1 RT 181 peptide (1.5 μg / ml in the first round, 0.8 μg / ml in the second round, 0.4 μg / ml in the third round), Used for positive selection. To load peptides, T2 cells were pulsed overnight with peptide-free serum-free RPMI1640 medium in the presence of 20 µg / ml β2M. After prolonged washing with PBS, peptide-loaded T2 cells with bound scFv antibody phage were subjected to rapid centrifugation. Next, the combined pure line was lysed and used to infect E. coli XL1-Blue cells. Next, the pure bacteriophage expressed in bacteria was purified. Three rounds of panning were performed to enrich scFv phage pure lines that specifically bind to HIV-1 RT 181 peptide / HLA-A * 02: 01. The streptavidin ELISA plate is coated with biotin-labeled HIV-1 RT 181 peptide / HLA-A * 02: 01 complex monomer or biotin-labeled P20 control peptide / HLA-A * 02: 01 monomer. The individual phage pure lines from the enriched phage display panning pool relative to the HIV-1 RT 181 peptide / HLA-A * 02: 01 complex were cultivated in a coating dish. The binding of phage pure lines was detected by HRP-conjugated anti-M13 antibody and developed using HRP substrate. The absorbance is read at 450 nm. From the phage pure lines enriched by phage panning, positive pure lines were identified by ELISA screening. The unique pure line was identified by DNA sequencing by ELISA positive phage pure line. Using flow cytometry (FACS analysis) using HIV-1 RT 181 peptide-loaded live T2 cells to further test the binding of specific and unique pure lines to the HLA-A * 02: 01 / peptide complex on the surface of live cells . Controls include T2 cells without peptide loading (cells only) and R-PE-conjugated horse anti-mouse IgG controls (secondary antibodies only). Briefly, T2 cells loaded with HIV-1 RT 181 peptide or P20 peptide pool were first stained with purified scFv bacteriophage pure line, followed by a second staining with mouse anti-M13 mAb, and combined with R-PE from Vector Labs Zima anti-mouse IgG stained for the third time. Each staining step was performed on ice for 30 to 60 minutes and the cells were washed twice between staining steps. It was determined that it does not specifically bind to HIV-1 RT 181-loaded T2 cells and does not bind to P20 peptide pool-loaded T2 cells or peptide-free T2 cells in the case of HLA-A * 02: 01.Examples 12 . Anti-based HIV - 1 RT Characterization of bispecific antibody molecules of affinity mature variants Production of bispecific antibodies The bispecific antibody (BsAb) was generated using the scFv sequence of the affinity-mature HIV-1 RT / HLA-A * 02: 01 phage pure line isolated in Example 10 using the method described in Example 4. The obtained single-chain bispecific antibody comprises the scFv sequence of the HIV-1 RT / HLA-A * 02: 01 specific phage pure line at the N-terminal and the anti-human CD3ε mouse monoclonal scFv at the C-terminal.Bispecific antibodies and HIV - 1 RT / HLA - A * 02 : 01 Determination of binding affinity The binding affinity of HIV-1 RT BsAb antibody (derived from affinity mature pure line) and recombinant HIV-1 RT / HLA-A * 02: 01 complex was measured by surface plasmon resonance (BiaCore). The binding parameters between HIV-1 RT BsAb and HIV-1 RT / HLA-A * 02: 01 complex are based on the manufacturer ’s protocol for multi-cycle kinetic measurements using the Biotin CAPture kit (GE Healthcare, catalog number 28920233) measured on Biacore X100 (GE Healthcare). All proteins used for analysis were diluted with HBS-E operating buffer. 5 µg / mL biotin-labeled HIV-1 RT 181 / HLA-A * 02: 01 / β2M complex was flowed through the flow cell at 5 µL / min by holding the solution for 75 seconds (captured ~ 120 RU MHC per cycle The complex) is fixed to the sensor chip CAP pre-functionalized with streptavidin (capture ~ 3,800 RU streptavidin). The binding to HIV-1 RT BsAb was analyzed at 150 nM, 75 nM, 37.5 nM, 18.8 nM and 9.4 nM. Each run consisted of a 2 minute binding and a 10 minute dissociation at 30 µL / min. At the end of the cycle, the surface was regenerated using regeneration buffer from the Biotin CAPture kit. The data was analyzed using BiaCore X-100 evaluation software using a 1: 1 binding site pattern. Next, calculate the binding parameter (binding rate constant k_a , Dissociation constant k_d And equilibrium dissociation constant K_d ).HIV - 1 RT Bispecific antibodies target multiple HLA - A02 Dual gene cross-reactivity and binding affinity As described in Example 5 above, the different subtypes of the HLA-A02 group are quite conservative, and cross-reactivity against multiple HLA-A02 subtypes is highly desirable. Therefore, experiments were conducted to determine whether the bispecific antibody (BsAb) produced by the parental pure line and the affinity matured variant cross-reacted with the non-HLA-A * 02: 01 subtype of the HLA-A02 group. Specifically, various types of HIV-1 RT 181 / MHC class I complexes with the HLA-A02 dual gene are generated, and the Pet ForteBio LLC (Menlo Park, CA) Octet® QKe system (which uses biolayer interference The measurement method (Biolayer Interferometry; BLI) technique was used to determine its binding affinity with HIV-1 RT 181 / HLA-A * 02: 01 specific antibody. The tested BsAbs include the parent pure line and the affinity mature variant pure line. Load the 5 µg / mL biotin-labeled HIV-1 RT 181 peptide / HLA-A02 complex with the varying subtype of HLA-A02 onto the streptavidin biosensor. After washing off excess antigen (HIV-1 RT peptide / HLA-A02 complex), the binding and dissociation kinetics of BsAb were tested at 10 µg / mL. The binding parameters were calculated using a 1: 1 binding site and a partially fitted model.Peptide binding specificity analysis To confirm the specificity of the peptide recognized by the affinity matured variant antibody, FACS analysis was performed by T2 cells loaded with HIV-1 RT 181 peptide, P20 peptide pool or without peptide load.Epitope localization through alanine walking To accurately study the sensitive residues of the HIV-1 RT 181 peptide recognized by the BsAb affinity mature variant, the alanine walking experiment as described above was performed.Sequence Listing

Figure 1 shows a single alanine substitution for HIV-1 RT 181 peptide (WT, M184V, M184I, Y181C or Y181C / M184V) or at positions 1, 2, 3, 4, 5, 6, 7, 8, or 9 Results of BB7.2 FACS binding analysis of HIV-1 RT 181 peptide T2 cells. Including only unloaded cells (T2 cells), only 2 ° antibody BB7.2 (second antibody), and unloaded cells and 2 ° antibody BB7.2 (T cells + second antibody) were used as controls. Figure 2 shows the killing of HIV-1 RT 181 M184V-loaded T2 cells by anti-HIV-1 RT 181 / HLA-A * 02: 01 bispecific antibody prepared from various bacteriophage pure lines. Negative controls included T2 cells loaded with a mixture of P20 control peptides. Figure 3 shows parental SK-Hep1 cells mediated by anti-HIV-1 RT 181 / MHC bispecific antibody (BsAb) and transduced to express HIV-1 RT 181 WT, HIV-1 RT 181 M184V or HIV -1 T cell killing of SK-Hep1 cells of RT 181 M184I. Figure 4 shows mock-transfected and stained T cells transduced with anti-HIV CAR 10, anti-HIV CAR 14 or HIV-1 RT 181-189 peptide / HLA-A * 02: 01 tetramer Analysis of flow cytometry. Figure 5 shows the killing of SK-HEP-1 and SK-HEP-1-MG cell lines mediated by T cells expressing anti-HIV CAR 10 or anti-HIV CAR 14.

Claims (30)

An isolated anti-RTMC construct that includes an antibody portion that specifically binds to human immunodeficiency virus 1 (HIV-1) reverse transcriptase (RT) peptide and major histocompatibility (MHC) class I protein (" RTMC "). The isolated anti-RTMC construct of claim 1, wherein the MHC class I protein is H HLA-A * 02: 01. The isolated anti-RTMC construct of claim 1 or 2, wherein the HIV-1 RT peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 5-18. The isolated anti-RTMC construct of claim 3, wherein the HIV-1 RT peptide has an amino acid sequence selected from the group consisting of SEQ ID NO: 5-9. The isolated anti-RTMC construct of claim 1 or 2, wherein the antibody portion specifically binds to one or more of the following: i) comprises an HIV-1 RT peptide containing the amino acid sequence SEQ ID NO: 5 And the complex of the MHC class I protein; ii) the complex containing the HIV-1 RT peptide containing the amino acid sequence SEQ ID NO: 6 and the MHC class I protein; iii) the complex containing the amino acid sequence SEQ ID NO: a complex of HIV-1 RT peptide of 7 and the MHC class I protein; iv) a complex of HIV-1 RT peptide containing the amino acid sequence SEQ ID NO: 8 and the MHC class I protein; And v) a complex comprising the HIV-1 RT peptide containing the amino acid sequence SEQ ID NO: 9 and the MHC class I protein. The isolated anti-RTMC construct of any one of claims 1 to 5, wherein the antibody portion is a full-length antibody, Fab, Fab ', (Fab') 2, Fv, or single chain Fv (scFv). The isolated anti-RTMC construct of any one of claims 1 to 6, wherein the isolated anti-RTMC construct binds to the HIV-1 RT / MHC class I complex with a Kd of about 0.1 pM to about 500 nM. The isolated anti-RTMC construct of any one of claims 1 to 7, wherein the antibody portion comprises: i) a heavy chain variable domain comprising: a heavy chain complementarity decision comprising an amino acid sequence SEQ ID NO: 240 Region (HC-CDR) 1, or variants containing up to about 3 amino acid substitutions, HC-CDR2 containing the amino acid sequence of any of SEQ ID NOs: 241-244, or up to about Variants with 3 amino acid substitutions, and HC-CDR3 containing the amino acid sequence of any one of SEQ ID NOs: 245-246, or variants with up to about 3 amino acid substitutions; And ii) a light chain variable domain comprising: a light chain complementarity determining region (LC-CDR) 1 comprising the amino acid sequence of any one of SEQ ID NOs: 247-249, or up to about 3 amines Variants thereof, and LC-CDR3 comprising the amino acid sequence of any one of SEQ ID NOs: 250-253, or variants comprising up to about 3 amino acid substitutions. The isolated anti-RTMC construct of any one of claims 1 to 7, wherein the antibody portion comprises: i) a heavy chain variable domain comprising: an amine comprising any one of SEQ ID NO: 75-96 HC-CDR1 of the amino acid sequence, or a variant thereof containing up to about 5 amino acid substitutions, HC-CDR2 comprising the amino acid sequence of any of SEQ ID NOs: 97-124, or up to about Variants of 5 amino acid substitutions, and HC-CDR3 comprising the amino acid sequence of any of SEQ ID NOs: 125-163, or variants of up to about 5 amino acid substitutions; And ii) a light chain variable domain comprising: LC-CDR1 comprising the amino acid sequence of any one of SEQ ID NO: 164-189, or a variant thereof comprising up to about 5 amino acid substitutions, LC-CDR2 comprising the amino acid sequence of any one of SEQ ID NO: 190-207, or a variant thereof comprising up to about 3 amino acid substitutions, and any of SEQ ID NO: 208-239 LC-CDR3 of the amino acid sequence of one, or a variant thereof containing up to about 5 amino acid substitutions. The isolated anti-RTMC construct of claim 8 or 9, wherein the antibody portion comprises: a) a heavy chain variable domain comprising the amino acid sequence of any one of SEQ ID NOs: 19-46, or ID NO: any of its variants having a sequence identity of at least about 95% in any of 19-46; and b) the light chain variable comprising the amino acid sequence of any of SEQ ID NO: 47-74 Domain, or a variant thereof that has at least about 95% sequence identity with any of SEQ ID NOs: 47-74. The isolated anti-RTMC construct of any one of claims 1 to 10, wherein the isolated anti-RTMC construct is multispecific. The isolated anti-RTMC construct of claim 11, wherein the isolated anti-RTMC construct is a tandem scFv, a bifunctional antibody (diabody; Db), a single chain bifunctional antibody (single chain diabody; scDb), a double affinity Dual-affinity retargeting (DART) antibody, dual variable domain (DVD) antibody, pestle-mortar (KiH) antibody, docking lock (DNL) antibody, chemically cross-linked antibody, heteromultimeric antibody or heteroconjugate antibody. The isolated anti-RTMC construct of claim 11 or 12, wherein the isolated anti-RTMC construct further comprises a second antibody portion that specifically binds to the second antigen. The isolated anti-RTMC construct of claim 13, wherein the second antigen is selected from the group consisting of CD3γ, CD3δ, CD3ε, CD3ζ, CD28, OX40, GITR, CD137, CD27, CD40L, and HVEM. The isolated anti-RTMC construct of claim 14, wherein the second antigen is CD3ε, and wherein the isolated anti-RTMC construct is an N-terminal scFv specific for HIV-1 RT / MHC class I complex and Tandem scFv of C-terminal scFv specific for CD3ε. The isolated anti-RTMC construct according to any one of claims 1 to 10, wherein the isolated anti-RTMC construct is a chimeric antigen receptor (CAR). The isolated anti-RTMC construct of any one of claims 1 to 10, wherein the isolated anti-RTMC construct is a chimeric antibody / T cell receptor (abTCR), which includes an extracellular domain containing the antibody portion and containing The T cell receptor (TCR) module (TCRM) of the TCR transmembrane domain. The isolated anti-RTMC construct according to any one of claims 1 to 10, wherein the isolated anti-RTMC construct is an immunoconjugate comprising the antibody portion and an effector molecule, wherein the effector molecule is selected from the group consisting of Therapeutic agents: drugs, toxins, radioisotopes, proteins, peptides and nucleic acids. The isolated anti-RTMC construct of any one of claims 1 to 10, wherein the isolated anti-RTMC construct is an immunoconjugate comprising the antibody portion and a label. A host cell expressing the isolated anti-RTMC construct according to any one of claims 1 to 19. A nucleic acid encoding one or more polypeptides contained in the isolated anti-RTMC construct of any one of claims 1 to 19. A vector comprising the nucleic acid according to claim 21. An effector cell that behaves as an isolated anti-RTMC construct of claim 16 or 17. The effector cell according to claim 23, wherein the effector cell is a T cell. A pharmaceutical composition comprising the isolated anti-RTMC construct as in any one of claims 1 to 19, the nucleic acid as in claim 21, the vector as in claim 22, or the effector cells as in claims 23 or 24. A method for detecting a cell presenting a complex on the surface of a cell, the complex comprising HIV-1 RT peptide and MHC class I protein, the method comprising subjecting the cell to the isolated anti-RTMC construct of claim 19 Contact and detect the presence of markers on the cell. A method of treating an individual suffering from HIV-1 infection, comprising administering to the individual: a) an effective amount of a pharmaceutical composition as claimed in item 25, or b) an effective amount of an effector cell as claimed in item 23 or 24 . A method of diagnosing an individual with HIV-1 infection, comprising: a) administering to the individual an effective amount of the isolated anti-RTMC construct as claimed in item 19; and b) measuring the content of the marker in the individual, The content of the mark above the threshold level indicates that the individual has the HIV-1 infection. A method for diagnosing an individual with HIV-1 infection, comprising: a) contacting a sample derived from the individual with the isolated anti-RTMC construct as in claim 19; and b) measuring the separation from the isolated sample in the sample The number of cells bound to the anti-RTMC construct, wherein the value of the number of cells bound to the isolated anti-RTMC construct is higher than the threshold level indicates that the individual has the HIV-1 infection. The method of any one of claims 27 to 29, wherein the individual is a human.