EP4587478A1 - Compositions of chimeric autoantigen-t cell receptor (catcr)-t cells and methods of making and using the same - Google Patents

Abstract

Provided are immune cells including a chimeric autoantigen-T cell receptor (CATCR) comprising: (a) a native or modified peptide of a T cell receptor-CD3 delta/ gamma/ epsilon complex protein, and (b) an autoantigenic peptide recognized by a B cell receptor (BCR). The disclosure also provides vectors, compositions, and methods of treatment using engineered immune cells including a CATCR.

Description

Attorney Docket No.: 44807-0422WO1 COMPOSITIONS OF CHIMERIC AUTOANTIGEN-T CELL RECEPTOR (CATCR)- T CELLS AND METHODS OF MAKING AND USING THE SAME CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority to U.S. Provisional Patent Application No.63/406,351, filed on September 14, 2022, which is incorporated herein by reference in its entirety. SEQUENCE LISTING This application contains a Sequence Listing that has been submitted electronically as an XML file named 44807-0422WO1_ST26_SL. The XML file, created on September 12, 2023, is 263,220 bytes in size. The material in the XML file is hereby incorporated by reference in its entirety. TECHNICAL FIELD The present disclosure relates to a cellular therapy that uses autoantigen-modified T-cell receptors (TCRs) to redirect T cells (or other immune cells) to bind and kill autoreactive cells in a subject that has an autoimmune disease. In particular, it relates to compositions of chimeric (auto)antigen-T cell receptors (CATCRs) for the selective targeting of cognate B-cell receptors (BCRs) expressed on autoreactive or pathogenic B cells, nucleic acids encoding CATCRs, and recombinant cells expressing at least one CATCR. The disclosure also includes methods of generating and using such modified T cells (or other mammalian cells) expressing at least one CATCR to treat autoimmune diseases and other B cell-mediated diseases (e.g., allergy). BACKGROUND Antiphospholipid antibody syndrome (APS) is an autoimmune disease mediated by autoantibodies against phospholipid-binding proteins that promote complement and immune activation, coagulopathy, and various forms of end-organ damage. APS can occur in isolation (primary APS) or in the context of another rheumatic disease (secondary APS), variably presenting as venous or arterial thrombosis, fetal loss, pregnancy morbidity, or disseminated coagulation with Attorney Docket No: 44807-0422WO1 multiorgan failure. In patients with systemic lupus erythematosus (SLE), thrombosis from APS is a leading cause of mortality, accounting for 27% of deaths during a 10-year period. Healthy individuals and those with certain viral infections (e.g., COVID-19) can harbor pathogenic antiphospholipid antibodies without fulfilling clinical criteria for APS but are at risk of thrombotic events (e.g., stroke, myocardial infarction, deep venous thrombosis) and pregnancy complications. Immunologically, APS is characterized by loss of B cell tolerance against self and the emergence of specific autoantibodies. To date, autoantibody systems targeting three phospholipid- binding protein/phospholipid complexes have been identified, collectively referred to as antiphospholipid antibodies: (i) anti-beta-2-glycoprotein I [β2GPI]/cardiolipin [CL]; (ii) anti- endothelial protein C receptor [EPCR]/lysobisphosphatidic acid [LBPA]; and (iii) anti- prothrombin [PT]/phosphatidylserine [PS]. These autoantibodies are directly pathogenic in vitro and in vivo. Strategies that eliminate the sources of these antibodies (e.g., B cells and plasma cells) may therefore prevent or cure APS. Autoreactive B cells and plasma cells that express surface B cell receptors (BCRs) specific for phospholipid-binding proteins are therefore ideal therapeutic targets for antigen-specific depletion strategies in patients with APS. Clinical studies have demonstrated the potential of autologous T cell therapies directed against shared B cell antigens (e.g., CD19) in the treatment of patients with autoimmune diseases. However, the expected toxicity (e.g., risk of infection, B cell aplasia, hypogammaglobulinemia) of adoptive cell therapies that eliminate the entirety of the B cell pool is prohibitive for the preventative or widespread treatment of APS. Therefore, there is a need for T cell therapies that can selectively eliminate pathogenic, autoreactive B cells targeting each of the three phospholipid- binding proteins (or their phospholipid complexes) in patients with or at risk of APS, and thereby eliminate the source of these antibodies with curative intent. These precision therapies would provide an opportunity to abrogate as well as prevent disease without impairing normal protective immunity and vaccine responses. SUMMARY Provided herein are immunoresponsive cells comprising: a recombinant chimeric autoantigen-T cell receptor (CATCR) comprising: (a) an extracellular binding domain comprising an autoantigenic peptide, wherein the autoantigenic peptide is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor- Attorney Docket No: 44807-0422WO1 CD3 delta/ gamma/ epsilon complex protein. In some embodiments, the recombinant CATCR further comprises a linker or hinge domain. In some embodiments, the recombinant CATCR further comprises an intracellular co- stimulatory, immunomodulatory, or signaling domain. In some embodiments, the recombinant CATCR is expressed from an expression cassette placed in an endogenous T cell receptor alpha constant (TRAC) locus and/or a T cell receptor beta constant 1 (TRBC1) locus and/or a T cell receptor beta constant 2 (TRBC2) locus and/or a T cell receptor gamma constant 1 (TRGC1) locus and/or a T cell receptor gamma constant 2 (TRGC2) locus and/or a T cell receptor delta constant (TRDC) locus and/or a CD3 gamma (CD3G) locus and/or a CD3 delta (CD3D) locus and/or CD3 epsilon (CD3E) locus and/or B2M locus and/or other gene locus of the immunoresponsive cell. In some embodiments, the placement of the recombinant CATCR expression cassette disrupts the endogenous expression of a TCR-CD3 complex protein comprising a native TCR alpha chain and/or a native TCR beta chain and/or a native TCR gamma and/or a native TCR delta chain and/or a native CD3 gamma chain and/or a native CD3 delta chain and/or a native CD3 epsilon chain and/or a native B2M chain in the immunoresponsive cell. In some embodiments, the placement of the recombinant CATCR expression cassette prevents mispairing between the recombinant CATCR and native TCR-CD3 complex chains in the immunoresponsive cell. In some embodiments, the CATCR complex associates with a CD3ζ chain, and wherein binding of a cognate B cell receptor to the autoantigenic peptide of the CATCR activates the CD3ζ chain, wherein the activation of the CD3ζ chain activates the immunoresponsive cell. In some embodiments, the autoantigenic peptide is derived from a phospholipid-binding protein. In some embodiments, the phospholipid-binding protein is beta-2 glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), or prothrombin (PT). In someembodiments, the autoantigenic peptide is expressed under an endogenous signal peptide. In some embodiments, the autoantigenic peptide is expressed under a non-endogenous signal peptide. In some embodiments, the autoantigenic peptide is expressed as part of a CD3 gamma (CD3 ^) chain; a CD3 epsilon (CD3ε) chain; a CD3 delta (CD3δ) chain; a T cell receptor (TCR) alpha chain; a T cell receptor (TCR) beta chain, a T cell receptor (TCR) gamma chain, or a T cell receptor (TCR) delta chain of the recombinant CATCR. In some embodiments, the autoantigenic peptide comprises: at least part of a domain of Attorney Docket No: 44807-0422WO1 β2GPI, wherein β2GPI comprises domain I (DI), domain II (DII), domain III (DIII), domain IV (DIV), or domain V (DV); an amino acid epitope comprising a sequence of RGGMR; or any combinations thereof. In some embodiments, the autoantigenic peptide comprises at least part of the endothelial protein C receptor (EPCR); the full or part of the extracellular (EC) domains of EPCR; a modified extracellular (EC) domain of EPCR; or EPCR in complex with a phospholipid. In some embodiments, the autoantigenic peptide comprises at least part of prothrombin (PT) or posttranslationally modified prothrombin. In some embodiments, the immunoresponsive cell is a human immune cell. In some embodiments, the immunoresponsive cell is a T cell. Also provided herein are nucleic acid sequences encoding a recombinant CATCR, wherein the recombinant CATCR comprises: (a) an extracellular binding domain comprising an autoantigenic peptide, wherein the autoantigenic peptide is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 delta/ gamma/ epsilon complex protein. In some embodiments, the recombinant CATCR further comprises a linker or hinge domain. In some embodiments, the recombinant CATCR further comprises an intracellular co- stimulatory, immunomodulatory, or signaling domain. In some embodiments, the recombinant CATCR comprises a recombinant T cell receptor (TCR)-CD3 protein complex. In some embodiments, the recombinant CATCR is expressed from an expression cassette placed in an endogenous T cell receptor alpha constant (TRAC) locus and/or a T cell receptor beta constant 1 (TRBC1) locus and/or a T cell receptor beta constant 2 (TRBC2) locus and/or a T cell receptor gamma constant 1 (TRGC1) locus and/or a T cell receptor gamma constant 2 (TRGC2) locus and/or a T cell receptor delta constant (TRDC) locus and/or a CD3 gamma (CD3G) locus and/or a CD3 delta (CD3D) locus and/or CD3 epsilon (CD3E) locus and/or B2M locus and/or other gene locus of the immunoresponsive cell. In some embodiments, the placement of the recombinant CATCR expression cassette disrupts the endogenous expression of a TCR-CD3 complex protein comprising a native TCR alpha chain and/or a native TCR beta chain and/or a native TCR gamma and/or a native TCR delta chain and/or a native CD3 gamma chain and/or a native CD3 delta chain and/or a native CD3 epsilon chain and/or a native B2M chain in the immunoresponsive cell. In some embodiments, the placement of the recombinant CATCR expression cassette prevents mispairing between the recombinant CATCR and native TCR-CD3 Attorney Docket No: 44807-0422WO1 complex chains in the immunoresponsive cell. In some embodiments, the CATCR complex associates with a CD3ζ chain, and wherein binding of a cognate B cell receptor to the autoantigenic peptide of the CATCR activates the CD3ζ chain, wherein the activation of the CD3ζ chain activates the immunoresponsive cell. In some embodiments, the autoantigenic peptide is derived from a phospholipid-binding protein. In some embodiments, the phospholipid-binding protein is beta-2 glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), or prothrombin (PT). In some embodiments, the autoantigenic peptide is expressed as part of a CD3 gamma (CD3 ^) chain; a CD3 epsilon (CD3ε) chain; a CD3 delta (CD3δ) chain; a T cell receptor (TCR) alpha chain; a T cell receptor (TCR) beta chain; a T cell receptor (TCR) gamma chain, or a T cell receptor (TCR) delta chain of the CATCR. In some embodiments, the autoantigenic peptide comprises: at least part of a domain of β2GPI, wherein the β2GPI comprises domain I (DI), domain II (DII), domain III (DIII), domain IV (DIV), or domain V (DV); an amino acid epitope comprising a sequence of RGGMR; or any combinations thereof. In some embodiments, the autoantigenic peptide comprises at least part of the endothelial protein C receptor (EPCR); the full or part of the extracellular (EC) domains of EPCR; a modified extracellular (EC) domain of EPCR; or EPCR in complex with a phospholipid. In some embodiments, the autoantigenic peptide comprises at least part of prothrombin (PT) or posttranslationally modified prothrombin. Also provided herein are vectors comprising any one of the nucleic acids described herein. In some embodiments, the vector further comprising a promoter. In some embodiments, the promoter is a TRAC promoter or EF1-alpha promoter. In some embodiments, the promoter is an EF1-alpha promoter, CMV promoter, hPGK promoter, RPBSA promoter, or human gene promoter. In some embodiments, the vector is a viral vector. Also provided herein are methods of producing an engineered immune cell, the method comprising: introducing into an immune cell any one of the nucleic acids or any one of the vectors described herein, thereby producing the engineered immune cell. In some embodiments, the nucleic acid is introduced into the immunoresponsive cell by using a gene-editing agent. In some embodiments, the gene-editing agent comprises CRISPR/Cas components. In some embodiments, the nucleic acid is introduced into a gene locus of the immunoresponsive cell, wherein expression of the nucleic acid is under control of the endogenous promoter of the gene locus. In some embodiments, the nucleic acid is introduced into a gene locus Attorney Docket No: 44807-0422WO1 of the immunoresponsive cell, wherein the expression of the nucleic acid is under control of an exogenous promoter. In some embodiments, the exogenous promoter is an EF1-alpha promoter, CMV promoter, hPGK promoter, RPBSA promoter, TRAC promoter, or human gene promoter. Also provided herein are engineered immune cells produced by any one of the methods described herein. Also provided herein are pharmaceutical compositions comprising any one of the engineered immune cells described herein and a pharmaceutically acceptable carrier. Also provided herein are methods of treating an autoimmune disease in a subject, the method comprising administering to the subject any one of the engineered immune cells or any one of the pharmaceutical compositions described herein. In some embodiments, the autoimmune disease is an autoimmune rheumatic disease, systemic autoimmune disease, or an organ-specific autoimmune disease. In some embodiments, the systemic autoimmune disease is rheumatoid arthritis (RA), spondyloarthropathies, ankylosing spondylitis and psoriatic arthritis, juvenile idiopathic arthritis, systemic lupus erythematosus, lupus nephritis, Sjögren’s disease, scleroderma/ systemic sclerosis, an idiopathic inflammatory myopathy, myositis, dermatomyositis, antisynthetase syndrome, an immune-mediated necrotizing myopathy, IgG4-related disease, vasculitis, granulomatosis with polyangiitis, microscopic polyangiitis, eosinophilic granulomatosis with polyangiitis, anti-glomerular basement membrane disease, Henoch-Schönlein purpura, Kawasaki disease, polyarteritis nodosa, Takayasu's arteritis, or giant cell arteritis. In some embodiments, the organ-specific autoimmune disease is acquired haemophilia, autoimmune encephalitis, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune and paraneoplastic encephalitis, Addison’s disease, celiac disease, Graves’ disease, Hashimoto thyroiditis, immune thrombocytopenia purpura, multiple sclerosis, myelin oligodendrocyte glycoprotein (MOG) antibody-related diseases, neuromyelitis optica (NMO) spectrum disorders, myasthenia gravis, Lambert-Eaton myasthenia syndrome, pemphigus vulgaris, pemphigus foliaceous, bullous pemphigoid, other autoimmune blistering diseases, autoimmune membranous nephropathy, primary membranous nephropathy, primary biliary cirrhosis, thrombotic thrombocytopenic purpura, or type I diabetes mellitus. In some embodiments, the autoimmune disease is antiphospholipid antibody syndrome (APS) or its preclinical state. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention Attorney Docket No: 44807-0422WO1 pertains. Although methods and materials similar or equivalent to those described herein can be used to practice the invention, suitable methods and materials are described below. All publications, patent applications, patents, and other references mentioned herein are incorporated by reference in their entirety. In case of conflict, the present specification, including definitions, will control. In addition, the materials, methods, and examples are illustrative only and not intended to be limiting. The details of one or more embodiments of the invention are set forth in the accompanying drawings and the description below. Other features, objects, and advantages of the invention will be apparent from the description and drawings, and from the claims. BRIEF DESCRIPTION OF DRAWINGS FIG. 1A is an exemplary schematic drawing that depicts how engineered immune cells (e.g., T cells) expressing chimeric autoantigen-T cell receptors (CATCRs) can bind and kill autoreactive B cells expressing cognate B-cell receptors (BCRs) in patients with APS and other B cell-mediated autoimmune diseases. Binding of CATCR-T cells induces immune synapse formation and selective killing of autoreactive B cells via the perforin/granzyme cytotoxicity pathway. FIG.1B-D show exemplary chimeric autoantigen-T cell receptor (CATCR)-T cell compositions for the selective depletion of autoreactive B cells in patients with APS and other B cell-mediated diseases. A T cell engineering strategy and product is described by which one or more parts of the TCR-CD3 complex are modified to express the entirety or any parts/mimotopes of an autoantigen or B-cell receptor epitope, which is targeted by autoreactive B cells and/or plasma cells in patients with APS or other organ-specific or systemic autoimmune diseases. The relevant full or partial autoantigen(s) are expressed as part of (human or murine) CD3 gamma ( ^), CD3 delta (δ), CD3 epsilon (ε), or any part of the TCR alpha constant region (C ^), TCR beta constant region (Cβ), TCR gamma constant region (C ^), TCR delta constant region (Cδ), TCR alpha variable region (V ^), TCR beta variable region (Vβ), TCR gamma variable region (V ^), TCR delta variable region (Vδ), under expression of either the endogenous promoter of the modified gene locus or under expression of an exogenous promoter (e.g., a promoter that is introduced in lieu of an endogenous promoter), with or without additional linker sequences, with or without additional intracellular and/or co-stimulatory and/or signaling domains, in addition to any needed self-cleaving peptides Attorney Docket No: 44807-0422WO1 or sequences of equivalent function, in addition to any needed poly(A) sequences or alternative terminator sequences, and in addition to any needed Stop codons, when applicable. FIG.1B shows an exemplary model representation of a native ^βTCR (bottom left) compared to engineered CATCR-T cell constructs that link antigenic sequences of an autoantigen (e.g., β2GPI EPCR or PT or any other autoantigen) to any parts of CD3 ^, CD3δ, CD3ε, Cβ, C ^, Cβ and C ^, Vβ, V ^, or Vβ and V ^, respectively (bottom right). A peptide-human leukocyte antigen (HLA) complex (top left) compared to autoreactive BCRs of any isotype (IgG, IgM, IgA, IgE, or IgD) or subclass (IgG1, IgG2, IgG3, Ig4; IgA1, IgA2) on the cell surface of autoreactive B cells (top right) targeted by CATCR-T cells are shown. FIG.1C shows an exemplary model representation of a native ^δTCR (bottom left) compared to engineered CATCR-T cell constructs that link antigenic sequences of an autoantigen (e.g., β2GPI EPCR or PT or any other autoantigen) to any parts of Cδ, C ^, Cε and C ^, Vδ, V ^, or Vδ and V ^, respectively (bottom right). In addition to ^δ-CATCR construct designs, variations applicable to any CATCR construct design comprising the addition of a linker/hinge domain (e.g., any natural or synthetic linker sequence(s) or binding/coupling domain(s), protein or other, that result in covalent or non-covalent linkage of the BCR-targeted autoantigen or parts thereof to any part of the TCR-CD3 complex such as (G4S)_n linkers, (EAAAK)_n linkers, immunoglobulin domains, protein tags, leucine zippers, or other dimerization domains) or the use of murine equivalents of any of the TCR-CD3 complex proteins (e.g., murine Cβ or murine C ^) are also described. Constructs expressing β2GPI or EPCR or PT as part of a modified second or higher generation chimeric antigen receptor (CAR) construct, comprising a hinge and/or linker domain (e.g., CD8, CD28, IgG1, IgG4), a transmembrane domain (e.g., CD8α, CD3ζ, CD4, CD28), at least one intracellular co-stimulatory or immunomodulatory domain (e.g., full or partial sequences of CD28, 4-1BB, OX40, ICOS, MYD88, 2B4, BTLA, CD2, CD22, CD27, CD30, CD3d, CD3e, CD3g, CD3z, CD4, CD40, CD79a, CD79b, CD84, CD8a, CD8b, CRACC, CRTAM, CTLA-4, DAP10, DNAM-1, DAP12, DR3, FCER1G, FCGR1A, FCGR2A, FCGR2B, FCGR3A, FCRL1, FCRL2, FCRL3, FCRL4, FCRL5, FCRL6, GITR, HVEM, ITAM, KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR3DL1, KIR3DL2, KIR3DL3, LAG3, LAT, LILRB1, LILRB2, Ly9, NKG2A, NKG2C, NKG2D, NKp30, NKp44, NKp46, PD-1, PILRB, SIRPa, SLAMF1, SLAMF6, SLAMF7, TIGIT, TIM1, TIM3, TNFL6, TLR1, TLR10, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, or their combination), and at least one intracellular Attorney Docket No: 44807-0422WO1 signaling/ signal transducer domain (e.g., CD3ζ, ZAP70, LCK, FYN, PLCG1, LCP2) in addition to the extracellular autoantigenic peptide(s), are also described in an alternative composition (bottom right). Autoreactive BCRs of any isotype (IgG, IgM, IgA, IgE, or IgD) or subclass (IgG1, IgG2, IgG3, Ig4; IgA1, IgA2) on the cell surface of autoreactive B cells (top) targeted by CATCR- T cells or β2GPI/EPCR/PT-CAR T cells are shown. FIG. 1D shows exemplary variations of CATCR construct designs described in FIGs. 1A-C including the addition of at least one intracellular co-stimulatory or other domain (e.g., full or partial sequences of CD28, 4-1BB, OX40, ICOS, MYD88, 2B4, BTLA, CD2, CD22, CD27, CD30, CD3d, CD3e, CD3g, CD3z, CD4, CD40, CD79a, CD79b, CD84, CD8a, CD8b, CRACC, CRTAM, CTLA-4, DAP10, DNAM-1, DAP12, DR3, FCER1G, FCGR1A, FCGR2A, FCGR2B, FCGR3A, FCRL1, FCRL2, FCRL3, FCRL4, FCRL5, FCRL6, GITR, HVEM, ITAM, KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR3DL1, KIR3DL2, KIR3DL3, LAG3, LAT, LILRB1, LILRB2, Ly9, NKG2A, NKG2C, NKG2D, NKp30, NKp44, NKp46, PD-1, PILRB, SIRPa, SLAMF1, SLAMF6, SLAMF7, TIGIT, TIM1, TIM3, TNFL6, TLR1, TLR10, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, ZAP70, LCK, FYN, PLCG1, LCP2, or their combination) as part of any CATCR domain is also described, in which the additional domain(s) are included as part of the autoantigen-modified chain or as part of at least one of the other chains of the TCR-CD3 complex (e.g., CD3 ^, CD3δ, CD3ε, C ^, Cβ, C ^, or Cδ). FIG. 2A shows an exemplary gene editing strategy to introduce coding sequences for CD3 ^- CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., CD3G), optional coding sequences for “self-cleaving” peptide (e.g., P2A, E2A, F2A, or T2A peptides), optional coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a, IgK, GMCSFR signal peptide) and/or optional coding sequences for signal peptide(s) endogenous to the expressed autoantigen(s), coding sequences for autoantigen (including their partial sequences, epitopes, or mimotopes), optional coding sequences for linkers (e.g., any natural or synthetic linker sequence(s) or binding/coupling domain(s) that result in covalent or non-covalent linkage of the BCR-targeted autoantigenic peptides to any part of the TCR-CD3 complex including (G4S)_n linkers, (EAAAK)_n linkers, immunoglobulin domains, protein tags, leucine zippers, or other dimerization domains), coding sequences for full or partial CD3 ^, optional stop codon or optional “self-cleaving” peptide, Attorney Docket No: 44807-0422WO1 and optional mammalian termination and polyadenylation signal sequence(s) (e.g., SV40, hGH, BGH, rbGlob poly(A) sequences). Self-cleaving peptide or stop codon/termination sequences distal to the CATCR coding sequences are introduced with the HDR template unless provided by the endogenous sequence of the targeted gene locus. Coding sequences for self-cleaving peptide(s)/signal peptide(s) proximal to the CATCR coding sequences are introduced with the repair template unless the chosen cut site introduces the CATCR coding sequences just distal to the signal peptide of the endogenous gene locus (resulting in transcription of the CATCR using the endogenous promoter and endogenous signal peptide). The editing strategy may be combined with modifications of TRAC, TRBC, or other gene loci (e.g., replacement with alternative, murine, truncated, or otherwise modified T-cell receptor domains). Coding sequences for at least one intracellular co-stimulatory or other domain may be included as shown in FIG. 1D. Several construct designs encompassing various β2GPI sushi domains (DI-DV) or combinations thereof, endothelial protein C receptor (EPCR), prothrombin (PT), and other autoantigens are shown. Shown combinations of autoantigens are exemplary. Autoantigens (including their partial sequences, epitopes, or mimotopes) can be combined in any way, and their combinations do not need to respect natural protein domains. For β2GPI, EPCR, and PT, this may include their associated phospholipids cardiolipin, lysobisphosphatidic acid, or phosphatidylserine. FIG. 2B shows an exemplary gene editing strategy to introduce coding sequences for CD3 ^- CATCRs for expression under control of an exogenous promoter using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., CD3G, not shown), exogenously introduced promoter sequences (e.g., EF1-alpha promoter, CMV promoter, hPGK promoter, RPBSA promoter, human gene promoters), Kozak consensus sequence for initiation of translation, coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a, IgK, GMCSFR signal peptide) and/or coding sequences for signal peptide(s) endogenous to the expressed autoantigen(s), coding sequences for autoantigen (including their partial sequences, epitopes, or mimotopes), optional coding sequences for linkers (e.g., any natural or synthetic linker sequence(s) or binding/coupling domain(s) that result in covalent or non-covalent linkage of the BCR-targeted autoantigenic peptides to any part of the TCR-CD3 complex including (G4S)n linkers, (EAAAK)n linkers, immunoglobulin domains, protein tags, leucine zippers, or other dimerization domains), coding sequences for full or partial CD3 ^, optional stop codon, and optional mammalian Attorney Docket No: 44807-0422WO1 termination and polyadenylation signal sequence(s) (e.g., SV40, hGH, BGH, rbGlob poly(A) sequences). Self-cleaving peptide or stop codon/termination sequences distal to the CATCR coding sequences are introduced with the HDR template unless provided by the endogenous sequence of the targeted gene locus. The editing strategy may be combined with modifications of TRAC, TRBC, or other gene loci (e.g., replacement with alternative, murine, truncated, or otherwise modified T-cell receptor domains). Coding sequences for at least one intracellular co- stimulatory or other domain may be included as shown in FIG. 1D. Several construct designs encompassing various β2GPI sushi domains (DI-DV) or combinations thereof, endothelial protein C receptor (EPCR), prothrombin (PT), and other autoantigens are shown. Shown combinations of autoantigens are exemplary. Autoantigens (including their partial sequences, epitopes, or mimotopes) can be combined in any way, and their combinations do not need to respect natural protein domains. For β2GPI, EPCR, and PT, this may include their associated phospholipids cardiolipin, lysobisphosphatidic acid, or phosphatidylserine. FIG.2C shows exemplary gene editing strategy as in FIG.2A but to introduce coding sequences for CD3ε-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., CD3E) and coding sequences for full or partial CD3ε. FIG.2D shows exemplary gene editing strategy as in FIG.2B but to introduce coding sequences for CD3ε-CATCRs for expression under control of an exogenous promoter using CRISPR/Cas- mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., CD3E) and coding sequences for full or partial CD3ε. FIG.2E shows exemplary gene editing strategy as in FIG.2A but to introduce coding sequences for CD3δ-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., CD3D) and coding sequences for full or partial CD3δ. FIG.2F shows exemplary gene editing strategy as in FIG.2B but to introduce coding sequences for CD3δ-CATCRs for expression under control of an exogenous promoter using CRISPR/Cas- mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ Attorney Docket No: 44807-0422WO1 and 3’ homology arms for the targeted gene locus (e.g., CD3D) and coding sequences for full or partial CD3δ. FIG.2G shows exemplary gene editing strategy as in FIG.2A but to introduce coding sequences for Cβ-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, TRBC), optional coding sequences for “self-cleaving” peptide (e.g., P2A, E2A, F2A, or T2A peptides), optional coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a, IgK, GMCSFR signal peptide) and/or optional coding sequences for signal peptide(s) endogenous to the expressed autoantigen(s), coding sequences for autoantigen (including their partial sequences, epitopes, or mimotopes), optional coding sequences for linkers (e.g., any natural or synthetic linker sequence(s) or binding/coupling domain(s) that result in covalent or non-covalent linkage of the BCR-targeted autoantigenic peptides to any part of the TCR-CD3 complex including (G4S)n linkers, (EAAAK)n linkers, immunoglobulin domains, protein tags, leucine zippers, or other dimerization domains), coding sequences for full or partial Cβ, optional coding sequences for “self-cleaving” peptide (e.g., P2A, E2A, F2A, or T2A peptides), optional coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a signal peptide), optional coding sequences for full or partial C ^ (required if targeting TRAC), optional stop codon or optional “self-cleaving” peptide, and optional mammalian termination and polyadenylation signal sequence(s) (e.g., SV40, hGH, BGH, rbGlob poly(A) sequences). The shown order of Cβ-linked CATCR and Cα coding sequences may be reversed. Instead of the shown human Cβ and Cα sequences, murine Cβ and Cα sequences may be introduced. If not targeting TRAC, the Cα sequences (and associated self- cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vα/Cα. Self- cleaving peptide or stop codon/termination sequences distal to the CATCR coding sequences are introduced with the HDR template unless provided by the endogenous sequence of the targeted gene locus. Coding sequences for self-cleaving peptide(s)/signal peptide(s) proximal to the CATCR coding sequences are introduced with the repair template unless the chosen cut site introduces the CATCR coding sequences just distal to the signal peptide of the endogenous gene locus (resulting in transcription of the CATCR using the endogenous promoter and endogenous signal peptide of the targeted gene locus). The editing strategy may be combined with modifications of other gene loci. Coding sequences for at least one intracellular co-stimulatory or Attorney Docket No: 44807-0422WO1 other domain may be included as shown in FIG. 1D. Several construct designs encompassing various β2GPI sushi domains (DI-DV) or combinations thereof, endothelial protein C receptor (EPCR), prothrombin (PT), and other autoantigens are shown. Shown combinations of autoantigens are exemplary. Autoantigens (including their partial sequences, epitopes, or mimotopes) can be combined in any way, and their combinations do not need to respect natural protein domains. For β2GPI, EPCR, and PT, this may include their associated phospholipids cardiolipin, lysobisphosphatidic acid, or phosphatidylserine. FIG.2H shows exemplary gene editing strategy as in FIG.2B but to introduce coding sequences for Cβ-CATCRs for expression under control of an exogenous promoter using CRISPR/Cas- mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, TRBC), exogenously introduced promoter sequences (e.g., EF1-alpha promoter, CMV promoter, hPGK promoter, RPBSA promoter, human gene promoters), Kozak consensus sequence for initiation of translation, coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a, IgK, GMCSFR signal peptide) and/or coding sequences for signal peptide(s) endogenous to the expressed autoantigen(s), coding sequences for autoantigen (including their partial sequences, epitopes, or mimotopes), optional coding sequences for linkers (e.g., any natural or synthetic linker sequence(s) or binding/coupling domain(s) that result in covalent or non-covalent linkage of the BCR-targeted autoantigenic peptides to any part of the TCR-CD3 complex including (G4S)_n linkers, (EAAAK)_n linkers, immunoglobulin domains, protein tags, leucine zippers, or other dimerization domains), coding sequences for full or partial Cβ, optional coding sequences for “self-cleaving” peptide (e.g., P2A, E2A, F2A, or T2A peptides), optional coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a signal peptide), optional coding sequences for full or partial C ^ (required if targeting TRAC), optional stop codon or optional “self-cleaving” peptide, and optional mammalian termination and polyadenylation signal sequence(s) (e.g., SV40, hGH, BGH, rbGlob poly(A) sequences). The shown order of Cβ-linked CATCR and Cα coding sequences may be reversed. Instead of the shown human Cβ and Cα sequences, murine Cβ and Cα sequences may be introduced. If not targeting TRAC, the Cα sequences (and associated self-cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vα/Cα. Self-cleaving peptide or stop codon/termination sequences distal to the CATCR coding sequences are introduced with the HDR template unless provided by the endogenous sequence of the targeted gene locus. The editing Attorney Docket No: 44807-0422WO1 strategy may be combined with modifications of other gene loci. Coding sequences for at least one intracellular co-stimulatory or other domain may be included as shown in FIG. 1D. Several construct designs encompassing various β2GPI sushi domains (DI-DV) or combinations thereof, endothelial protein C receptor (EPCR), prothrombin (PT), and other autoantigens are shown. Shown combinations of autoantigens are exemplary. Autoantigens (including their partial sequences, epitopes, or mimotopes) can be combined in any way, and their combinations do not need to respect natural protein domains. For β2GPI, EPCR, and PT, this may include their associated phospholipids cardiolipin, lysobisphosphatidic acid, or phosphatidylserine. FIG.2I shows exemplary gene editing strategy as in FIG.2G but to introduce coding sequences for Cα-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, TRBC). The shown order of Cα-linked CATCR and Cβ coding sequences may be reversed. If not targeting TRBC, the Cβ sequences (and associated self-cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vβ/Cβ. FIG.2J shows exemplary gene editing strategy as in FIG.2H but to introduce coding sequences for Cα-CATCRs for expression under control of an exogenous promoter using CRISPR/Cas- mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, TRBC). The shown order of Cα- linked CATCR and Cβ coding sequences may be reversed. If not targeting TRBC, the Cβ sequences (and associated self-cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vβ/Cβ. FIG.2K shows exemplary gene editing strategy as in FIG.2G but to introduce coding sequences for dual Cα- and Cβ-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, TRBC). The shown order of Cβ-linked CATCR and Cα-linked CATCR may be reversed. Cα sequences (and associated self-cleaving peptide/ signal peptide sequences) are not optional. Instead of the shown human Cβ and Cα sequences, murine Cβ and Cα sequences may be introduced. The strategy may be combined with knockout of endogenous TRAC and TRBC. Attorney Docket No: 44807-0422WO1 FIG.2L shows exemplary gene editing strategy as in FIG.2H but to introduce coding sequences for dual Cα- and Cβ-CATCRs for expression under control of an exogenous promoter using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, TRBC). The shown order of Cβ-linked CATCR and Cα-linked CATCR may be reversed. Cα sequences (and associated self-cleaving peptide/ signal peptide sequences) are not optional. Instead of the shown human Cβ and Cα sequences, murine Cβ and Cα sequences may be introduced. The strategy may be combined with knockout of endogenous TRAC and TRBC. FIG.2M shows exemplary gene editing strategy as in FIG.2G but to introduce coding sequences for Cδ-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRGC, TRDC). The shown order of Cδ-linked CATCR and Cγ coding sequences may be reversed. Instead of the shown human Cδ and Cγ sequences, murine Cδ and Cγ sequences may be introduced. If not targeting TRGC, the Cγ sequences (and associated self-cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vγ/Cγ. FIG.2N shows exemplary gene editing strategy as in FIG.2H but to introduce coding sequences for Cδ-CATCRs for expression under control of under control of an exogenous promoter using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRGC, TRDC). The shown order of Cδ-linked CATCR and Cγ coding sequences may be reversed. Instead of the shown human Cδ and Cγ sequences, murine Cδ and Cγ sequences may be introduced. If not targeting TRGC, the Cγ sequences (and associated self-cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vγ/Cγ. FIG.2O shows exemplary gene editing strategy as in FIG.2G but to introduce coding sequences for Cγ-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRGC, TRDC). The shown order of Cγ-linked CATCR and Cδ coding sequences may be reversed. Instead of the shown human Cδ and Cγ sequences, murine Cδ and Cγ sequences may be introduced. If not Attorney Docket No: 44807-0422WO1 targeting TRDC, the Cδ sequences (and associated self-cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vδ/Cδ. FIG.2P shows exemplary gene editing strategy as in FIG.2H but to introduce coding sequences for Cγ-CATCRs for expression under control of under control of an exogenous promoter using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRGC, TRDC). The shown order of Cγ-linked CATCR and Cδ coding sequences may be reversed. Instead of the shown human Cδ and Cγ sequences, murine Cδ and Cγ sequences may be introduced. If not targeting TRDC, the Cδ sequences (and associated self-cleaving peptide/ signal peptide sequences) may be omitted to preserve endogenous Vδ/Cδ. FIG.2Q shows exemplary gene editing strategy as in FIG.2G but to introduce coding sequences for dual Cγ- and Cδ-CATCRs for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRGC, TRDC). The shown order of Cδ-linked CATCR and Cγ-linked CATCR may be reversed. Cγ sequences (and associated self-cleaving peptide/ signal peptide sequences) are not optional. Instead of the shown human Cδ and Cγ sequences, murine Cδ and Cγ sequences may be introduced. The strategy may be combined with knockout of endogenous TRGC and TRDC. FIG.2R shows exemplary gene editing strategy as in FIG.2H but to introduce coding sequences for dual Cγ- and Cδ-CATCRs for expression under control of an exogenous promoter using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRGC, TRDC). The shown order of Cδ-linked CATCR and Cγ-linked CATCR may be reversed. Cγ sequences (and associated self-cleaving peptide/ signal peptide sequences) are not optional. Instead of the shown human Cδ and Cγ sequences, murine Cδ and Cγ sequences may be introduced. The strategy may be combined with knockout of endogenous TRGC and TRDC. FIG.2S shows exemplary gene editing strategy as in FIG.2G but to introduce coding sequences for APS autoantigen-CAR for expression under control of the endogenous promoter of the targeted gene locus using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, B2M), optional coding sequences for “self-cleaving” peptide (e.g., P2A, E2A, F2A, or T2A peptides), Attorney Docket No: 44807-0422WO1 optional coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a, IgK, GMCSFR signal peptide) and/or optional coding sequences for signal peptide(s) endogenous to the expressed autoantigen(s), coding sequences for autoantigen (e.g., β2GPI, EPCR, PT, their partial sequences, epitopes, or mimotopes), optional coding sequences for linkers (e.g., any natural or synthetic linker sequence(s) or binding/coupling domain(s) that result in covalent or non- covalent linkage of the BCR-targeted autoantigenic peptides to any part of the TCR-CD3 complex including (G4S)_n linkers, (EAAAK)_n linkers, immunoglobulin domains, protein tags, leucine zippers, or other dimerization domains), coding sequences for any hinge domain(s) (e.g., CD8, CD28, IgG1, IgG4), coding sequences for any transmembrane domain(s) (e.g., CD8α, CD3ζ, CD4, CD28), coding sequences for at least one intracellular co-stimulatory or other domain (e.g., full or partial sequences of CD28, 4-1BB, OX40, ICOS, MYD88, 2B4, BTLA, CD2, CD22, CD27, CD30, CD3d, CD3e, CD3g, CD3z, CD4, CD40, CD79a, CD79b, CD84, CD8a, CD8b, CRACC, CRTAM, CTLA-4, DAP10, DNAM-1, DAP12, DR3, FCER1G, FCGR1A, FCGR2A, FCGR2B, FCGR3A, FCRL1, FCRL2, FCRL3, FCRL4, FCRL5, FCRL6, GITR, HVEM, ITAM, KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR3DL1, KIR3DL2, KIR3DL3, LAG3, LAT, LILRB1, LILRB2, Ly9, NKG2A, NKG2C, NKG2D, NKp30, NKp44, NKp46, PD-1, PILRB, SIRPa, SLAMF1, SLAMF6, SLAMF7, TIGIT, TIM1, TIM3, TNFL6, TLR1, TLR10, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, ZAP70, LCK, FYN, PLCG1, LCP2, or their combination), coding sequences for CD3ζ signaling domains, optional stop codon or optional “self-cleaving” peptide, and optional stop codon/ mammalian termination and polyadenylation signal sequence(s) (e.g., SV40, hGH, BGH, rbGlob poly(A) sequences). Self-cleaving peptide or stop codon/termination sequences distal to the CAR coding sequences are introduced with the HDR template unless provided by the endogenous sequence of the targeted gene locus. Coding sequences for self-cleaving peptide(s)/signal peptide(s) proximal to the CAR coding sequences are introduced with the repair template unless the chosen cut site introduces the CAR coding sequences just distal to the signal peptide of the endogenous gene locus (resulting in transcription of the CAR using the endogenous promoter and endogenous signal peptide). The editing strategy may be combined with modifications of other gene loci. Several construct designs encompassing various β2GPI sushi domains (DI-DV) or combinations thereof, endothelial protein C receptor (EPCR), prothrombin (PT) are shown. Shown combinations of autoantigens are exemplary. Autoantigens (including their partial sequences, epitopes, or mimotopes) can be combined in any Attorney Docket No: 44807-0422WO1 way, and their combinations do not need to respect natural protein domains. For β2GPI, EPCR, and PT, this may include their associated phospholipids cardiolipin, lysobisphosphatidic acid, or phosphatidylserine. FIG.2T shows exemplary gene editing strategy as in FIG.2H but to introduce coding sequences for APS autoantigen-CAR for expression under control of an exogenous promoter using CRISPR/Cas-mediated homology directed repair (HDR). The homology-directed repair template comprises 5’ and 3’ homology arms for the targeted gene locus (e.g., TRAC, B2M), exogenously introduced promoter sequences (e.g., EF1-alpha promoter, CMV promoter, hPGK promoter, RPBSA promoter, human gene promoters), Kozak consensus sequence for initiation of translation, coding sequences for signal peptide(s) for cell surface expression (e.g., CD8a, IgK, GMCSFR signal peptide) and/or coding sequences for signal peptide(s) endogenous to the expressed autoantigen(s), coding sequences for autoantigen (e.g., β2GPI, EPCR, PT, their partial sequences, epitopes, or mimotopes), optional coding sequences for linkers (e.g., any natural or synthetic linker sequence(s) or binding/coupling domain(s) that result in covalent or non-covalent linkage of the BCR-targeted autoantigenic peptides to any part of the TCR-CD3 complex including (G4S)n linkers, (EAAAK)_n linkers, immunoglobulin domains, protein tags, leucine zippers, or other dimerization domains), coding sequences for any hinge domain(s) (e.g., CD8, CD28, IgG1, IgG4), coding sequences for any transmembrane domain(s) (e.g., CD8α, CD3ζ, CD4, CD28), coding sequences for at least one intracellular co-stimulatory or other domain (e.g., full or partial sequences of CD28, 4-1BB, OX40, ICOS, MYD88, 2B4, BTLA, CD2, CD22, CD27, CD30, CD3d, CD3e, CD3g, CD3z, CD4, CD40, CD79a, CD79b, CD84, CD8a, CD8b, CRACC, CRTAM, CTLA-4, DAP10, DNAM-1, DAP12, DR3, FCER1G, FCGR1A, FCGR2A, FCGR2B, FCGR3A, FCRL1, FCRL2, FCRL3, FCRL4, FCRL5, FCRL6, GITR, HVEM, ITAM, KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR3DL1, KIR3DL2, KIR3DL3, LAG3, LAT, LILRB1, LILRB2, Ly9, NKG2A, NKG2C, NKG2D, NKp30, NKp44, NKp46, PD-1, PILRB, SIRPa, SLAMF1, SLAMF6, SLAMF7, TIGIT, TIM1, TIM3, TNFL6, TLR1, TLR10, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, ZAP70, LCK, FYN, PLCG1, LCP2, or their combination), coding sequences for CD3ζ signaling domains, optional stop codon or optional “self-cleaving” peptide, and optional stop codon/ mammalian termination and polyadenylation signal sequence(s) (e.g., SV40, hGH, BGH, rbGlob poly(A) sequences). Self-cleaving peptide or stop codon/termination sequences distal to the CAR coding sequences are introduced with the Attorney Docket No: 44807-0422WO1 HDR template unless provided by the endogenous sequence of the targeted gene locus. The editing strategy may be combined with modifications of other gene loci. Several construct designs encompassing various β2GPI sushi domains (DI-DV) or combinations thereof, endothelial protein C receptor (EPCR), prothrombin (PT) are shown. Shown combinations of autoantigens are exemplary. Autoantigens (including their partial sequences, epitopes, or mimotopes) can be combined in any way, and their combinations do not need to respect natural protein domains. For β2GPI, EPCR, and PT, this may include their associated phospholipids cardiolipin, lysobisphosphatidic acid, or phosphatidylserine. FIG.2U and 2V shows exemplary variations of the CATCR construct designs described in FIGs. 2A-2T comprising the addition of at least one co-stimulatory domain(s), immune activating domain(s), immune signaling domain(s), inhibitory domain(s), or intracellular domain(s) containing the latter (e.g., full or partial sequences of CD28, 4-1BB, OX40, ICOS, MYD88, TNFL6; 2B4, 4–1BB, CD2, CD27, CD28, CD30, CD40, CD84, CRTAM, DAP10, DNAM-1, DR3, GITR, HVEM, ICOS, OX40, SLAMF1, TIM1; CD3d, CD3d ITAM, CD3e, CD3e ITAM, CD3g, CD3g ITAM, CD3z, CD3z ITAM1, CD3z ITAM2, CD3z ITAM3, CD79a, CD79a ITAM, CD79b, CD79b ITAM, DAP12, DAP12 ITAM, FCER1G, FCER1G ITAM; CD22, CD4, CD8a, CD8b, CRACC, FCGR1A, FCGR2A, FCGR2B, FCGR3A, FCRL1, FCRL2, FCRL3, FCRL4, FCRL5, FCRL6, LAT, Ly9, NKG2A, NKG2C, NKG2D, NKp30, NKp44, NKp46, NTB-A, PILRB, TLR1, TLR10, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9; BTLA, CTLA-4, KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR3DL1 KIR3DL2, KIR3DL3, LAG3 LILRB1, LILRB2, PD-1, SIRPa, TIGIT, TIM3, ZAP70, LCK, FYN, PLCG1, LCP2; or any combination thereof) in an intracellular domain of a CATCR. Constructs for expression under control of the endogenous promoter are shown in (U), constructs for expression under control of an exogenous promoter are shown in (V). FIG. 2W shows an exemplary gene editing workflow for the introduction of CATCR- or CAR- coding sequences into the human genome using CRISPR/Cas-mediated homology directed repair. One exemplary approach to generate CATCR-T cells is shown using dsDNA HDR template (HDRT) with gene locus-specific homology arms (HAs) and ribonucleoprotein (RNP) complexes of Cas enzyme (e.g., Cas9, Cpf1/Cas12a) with matching sgRNA. HDRT, RNP complexes, and enhancers can be electroporated into activated primary human T cells to induce editing of the target gene locus (exemplarily shown for CD3G). After integration into the target gene locus (shown for Attorney Docket No: 44807-0422WO1 a construct that is expressed under control of the endogenous gene promoter), mRNA encoding for CATCRs is transcribed, spliced, and translated to express CATCR protein on the cell surface. CATCRs may be generated using any gene editing strategy (e.g., CRISPR using any Cas nuclease, TALEN), any kind of template (e.g., dsDNA, ssDNA, RNA, other nucleic acids), any form of Cas RNP / HDRT vehicle/ delivery system (e.g., DNA, RNA, or protein via electroporation, microinjection, cell-penetrating peptides, any form of transfection, viral transduction), with any additional enhancers of delivery or gene editing (e.g., HDR enhancers, truncated Cas9 target sequences sequences), and using any of the construct designs described in FIGs.1A-1D and FIGs. 2A-2W. FIG. 3A shows exemplary construct designs to introduce conventional or self-amplifying messenger RNA (mRNA) encoding for one or more of the described CATCR proteins into mammalian cells. FIG.3B shows an exemplary workflow for the introduction of CATCR- or CAR-coding sequences into the human genome using mRNA. For the cellular expression of CATCR protein from mRNA, CATCR mRNA (including RNA using nucleotide/nucleoside analogs) may be generated by any means (e.g., de-novo RNA synthesis, in-vitro transcription and post-transcriptional capping/tailing of RNA from any DNA template) and may be introduced into cells by any means (e.g., any form of electroporation, transfection using any lipids, any lipid-based nanoparticle formulations, any polymer-based nanoparticle formulations such as polyamines, dendrimers, copolymers, cationic polymers including polyethylenimine (PEI), polyamidoamine (PAMAM) dendrimer, polysaccharides, anionic polymers, or any lipid–polymer hybrid formulations, any peptide-based delivery systems including, but not limited to, protamine, cell-penetrating peptides, pore-forming agents/proteins, any virus-like replicon particles/viral particles, any cationic nanoemulsion, naked RNA, among other), either ex vivo or in vivo, by any route of administration (e.g., intravenous, intradermal, subcutaneous, intramuscular, intranodal, intraosseous, oral, into autoimmune target tissues). FIG. 4A and 4B show exemplary transfer vectors for lentiviral production and transduction of mammalian cells with CATCRs (A) or APS autoantigen-CARs (B), using the APS autoantigens as B cell-receptor (BCR)-targeting domains. CATCRs or APS autoantigen-CARs may be introduced and expressed in mammalian cells (e.g., T cells, other cytotoxic cells) using any viral vectors (e.g., lentiviral expression systems, adeno-associated virus systems, adenoviral systems, Attorney Docket No: 44807-0422WO1 retroviral systems, herpesviral vector systems, among others). This strategy may be applied to express any CATCR constructs shown in FIGs. 1A-1D and FIGs. 2A-2V, or their variants, in mammalian cells. FIG.5A shows the expression of CATCRs in isolated primary human T cells that were modified using CRISPR/Cas-mediated homology directed repair (HDR) technology. Flow cytometric staining and analysis of engineered human T cells (modified with Cas RNP and HDRT, top row) showing cell surface expression of CATCRs incorporating autoantigenic peptides of β2GPI as detected by an anti-β2GPI monoclonal antibody (clone H219) and anti-nerve growth factor (NGFR) antibody (top right panel, quadrant Q2). Coding sequences for truncated NGFR were incorporated into the CATCR HDRT to allow for autoantigen-independent detection and enrichment. Flow cytometric staining and analysis of mock-edited human T cells (modified with Cas RNP in the absence of HDRT) showing no CATCR expression are shown in comparison (bottom right panel, quadrant Q2). Representative examples are shown. FIG.5B shows the expression of two other representative CATCRs in isolated primary human T cells that were modified using CRISPR/Cas-mediated homology directed repair (HDR) technology. Flow cytometric staining and analysis of engineered human T cells (modified with Cas RNP and HDRT, top and middle row) showing cell surface expression of CATCRs incorporating autoantigenic peptides of β2GPI as detected by patient-derived monoclonal anti-β2GPI antibody (clone P1-117) and anti-nerve growth factor (NGFR) antibody. Flow cytometric staining and analysis of mock-edited human T cells (modified with Cas RNP in the absence of HDRT) showing no CATCR expression are shown in comparison (bottom row). Representative examples are shown. FIG.5C shows exemplary results of cell surface staining and flow cytometric analysis of human T cells engineered to express a CATCR incorporating autoantigenic peptides of EPCR. In this example, primary human T cells were modified by electroporation of Cas nuclease/sgRNA RNPs and dsDNA homology directed repair template (HDRT) to generate EPCR-CATCR-T cells. Gating on engineered CD4+ T cells (top right panel) and CD8+ T cells (bottom right panel) is shown. Successful editing and expression of CATCRs was determined using an antibody specific for nerve growth factor, introduced as an editing control, and an antibody for CD3ε. CD3ε cell surface expression is lost with TRAC knock-out, but surface re-expression is observed with successful introduction of a CATCR. Representative examples are shown. Attorney Docket No: 44807-0422WO1 FIG.6 shows representative examples of co-culture experiments of autoreactive human Ramos B cells engineered to express monoclonal anti-β2GPI BCRs or wild-type human Ramos B cells expressing irrelevant BCRs with either β2GPI-CATCR-T cells or mock-edited T cells (control). Flow cytometric staining with APC anti-CD19 (detecting all B cells) and DyLight 488 StrepTactin XT (detecting anti-β2GPI BCRs) at the end of the experiment (40 hours) are shown (effector:target cell [E:T] ratio at start of experiment was 10:1). Neither mock-edited T cells (top left panel) nor β2GPI-CATCR-T cells (top right panel) killed wild-type (CD19+, anti-β2GPI BCR-) Ramos B cells (shown in Q3). In contrast, β2GPI-CATCR-T efficiently and selectively depleted autoreactive (CD19+, anti-β2GPI BCR+) Ramos B cells (Q2, bottom right panel). These cells were not depleted by mock-edited T cells (Q2, bottom left panel). FIGs.7A-7B show a summary of a representative co-culture experiment for one β2GPI-CATCR- T cell as shown in FIG. 6 across different effector:target cell [E:T] ratios. Graphs show the absolute B cell numbers remaining at the end of a co-culture experiment of β2GPI-CATCR-T cells with either different autoreactive, anti-β2GPI BCR+ Ramos B cell clones (M1 and M9, FIG.7A) or normal Ramos B cell clones expressing irrelevant B cell receptors (FIG. 7B). Autoreactive, anti-β2GPI BCR+ B cells were killed in a dose-dependent manner as the effector:target cell [E:T] ratios increased. No off-target killing against normal B cells was observed. FIG.8 shows a summary of a representative co-culture experiment for one β2GPI-CATCR-T cell with autoreactive B cells across different effector:target cell [E:T] ratios. Cytotoxicity (in %) of autoreactive Ramos B cell clones expressing different patient-derived pathogenic anti-β2GPI BCRs (M1 and M9, respectively) is shown. Cytotoxicity data for three single cell clones (cl) for each patient-derived BCR are shown. FIG.9 shows a summary of a representative co-culture experiment for one β2GPI-CATCR-T cell with autoreactive B cells across different effector:target cell [E:T] ratios. Anti-B2GPI autoantibody levels, as quantified by custom B2GPI ELISA, at the end of a co-culture experiment of β2GPI-CATCR-T cells with autoreactive, anti-β2GPI BCR+ Ramos B cell clones are shown. β2GPI-CATCR-T cells abrogate autoantibody production in a dose-dependent manner. DETAILED DESCRIPTION This disclosure describes immune cells (e.g., T cells, NK cells, macrophages) engineered with chimeric autoantigen-T cell receptors (CATCRs) that bind and kill autoreactive B cells and/or Attorney Docket No: 44807-0422WO1 plasma cells that carry B cell receptors (BCRs) specific for an autoantigen (e.g., the phospholipid- binding proteins β2GPI, EPCR, or PT), as well as methods of making and using the same. Provided herein are immune cells that include a recombinant chimeric autoantigen-T cell receptor (CATCR) comprising: (a) an extracellular binding domain comprising an autoantigenic peptide (or complex containing the latter), wherein the autoantigenic peptide (or complex containing the latter) is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 delta/ gamma/ epsilon complex protein. Also provided herein are nucleic acid sequences encoding a recombinant CATCR that includes (a) an extracellular binding domain comprising an autoantigenic peptide, wherein the autoantigenic peptide is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 delta/ gamma/ epsilon complex protein. This disclosure also provides methods of generating, vectors, compositions, and methods of treatment using engineered immune cells that include a CATCR comprising (a) an extracellular binding domain comprising an autoantigenic peptide, wherein the autoantigenic peptide is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 delta/ gamma/ epsilon complex protein. Various non-limiting aspects of these immune cells are described herein, and can be used in any combination without limitation. Additional aspects of various components of methods of making and using the immune cells are known in the art. It must be noted that, as used in the specification and the appended claims, the singular forms “a,” “an” and “the” include plural referents unless the context clearly dictates otherwise. As used herein, the term “about”, when used herein in reference to a value, refers to a value that is similar, in context to the referenced value. In general, those skilled in the art, familiar with the context, will appreciate the relevant degree of variance encompassed by “about” in that context. For example, in some embodiments, the term “about” may encompass a range of values that are within 25%, 20%, 19%, 18%, 17%, 16%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, or less of the referred value. As used herein, the term “administration” typically refers to the administration of a composition to a subject or system to achieve delivery of an agent that is, or is included in, the Attorney Docket No: 44807-0422WO1 composition. Those of ordinary skill in the art will be aware of a variety of routes that may, in appropriate circumstances, be utilized for administration to a subject, for example a human. For example, in some embodiments, administration may be ocular, oral, parenteral, etc. In some particular embodiments, administration may be bronchial (e.g., by bronchial instillation), buccal, dermal (which may be or comprise, for example, one or more of topical to the dermis, intradermal, transdermal, etc.), enteral, intra-arterial, intragastric, intramedullary, intramuscular, intranasal, intraperitoneal, intrathecal, intravenous, intraventricular, within a specific organ (e.g., intrahepatic), mucosal, nasal, oral, rectal, subcutaneous, sublingual, topical, tracheal (e.g., by intratracheal instillation), vaginal, vitreal, etc. In some embodiments, administration may involve only a single dose. In some embodiments, administration may involve application of a fixed number of doses. In some embodiments, administration may involve dosing that is intermittent (e.g., a plurality of doses separated in time) and/or periodic (e.g., individual doses separated by a common period of time) dosing. In some embodiments, administration may involve continuous dosing (e.g., perfusion) for at least a selected period of time. As used herein, the term “antigen” refers to a molecule or molecular structure that binds to a specific antibody, B-cell receptor, or T-cell receptor. As used herein, the term “autoantigen” refers to a human molecule or molecular structure that is a normal bodily constituent in health or disease and binds to a specific antibody, B-cell receptor, or T-cell receptor. In some embodiments, an (auto)antigen binds to an antibody, B-cell receptor, or T-cell receptor and may or may not induce a particular physiological response in an organism. In general, an antigen may be or include any chemical entity such as, for example, a small molecule, a nucleic acid sequence (e.g., DNA or RNA), a peptide, a polypeptide, a protein, a carbohydrate, a glycoprotein, a lipid or phospholipid, a lipoprotein, a polymer (including biologic polymers [e.g., nucleic acid and/or amino acid polymers] and polymers other than biologic polymers [e.g., other than a nucleic acid or amino acid polymer]), etc. In some embodiments, an antigen is or comprises a polypeptide. In some embodiments, an antigen is or comprises a glycan. In some embodiments, an antigen is or comprises a phospholipid. In some embodiments, an antigen is or comprises a phospholipid- protein complex. Those of ordinary skill in the art will appreciate that, in general, an antigen may be provided in isolated or pure form, or alternatively may be provided in crude form (e.g., together with other materials, for example in an extract such as a cellular extract or other relatively crude preparation of an antigen-containing source). In some certain embodiments, an antigen is present Attorney Docket No: 44807-0422WO1 in a cellular context (e.g., an antigen is expressed on the surface of a cell in the context of a CATCR or expressed in a cell). In some embodiments, an antigen is a recombinant antigen. As used herein, an “antigen-binding domain” refers to a fusion protein or portion thereof that specifically binds to a target moiety or entity (e.g., a B-cell receptor or a T-cell receptor). Typically, the interaction between an antigen-binding domain and its target is non-covalent. In some embodiments, a target moiety or entity can be of any chemical class including, for example, a carbohydrate, a lipid, a nucleic acid, a metal, a polypeptide, or a small molecule. In some embodiments, an antigen binding domain may be or comprise a polypeptide (or complex thereof). In some embodiments, an antigen binding domain is part of a fusion polypeptide. In some embodiments, an antigen-binding domain is part of a chimeric antigen T-cell receptor (CATCR) which binds its target (e.g., the cognate B-cell receptor). It will be understood that the term “binding”, as used herein, typically refers to a non- covalent association between or among two or more entities. “Direct” binding involves physical contact between entities or moieties; indirect binding involves physical interaction by way of physical contact with one or more intermediate entities. Binding between two or more entities can typically be assessed in any of a variety of contexts – including where interacting entities or moieties are studied in isolation or in the context of more complex systems (e.g., while covalently or otherwise associated with a carrier entity and/or in a biological system or cell). As used herein, in general, the term “engineered” refers to the aspect of having been manipulated by the hand of man. For example, a polypeptide is considered to be “engineered” when the polypeptide sequence manipulated by the hand of man. For example, in some embodiments of the present invention, an engineered polypeptide comprises a sequence that includes one or more amino acid mutations, truncations, deletions, and/or insertions that have been introduced by the hand of man into a reference polypeptide sequence. In some embodiments, an engineered polypeptide includes a polypeptide that has been fused (e.g., covalently linked) to one or more additional polypeptides by the hand of man, to form a fusion polypeptide that would not naturally occur in vivo. Comparably, a cell or organism is considered to be “engineered” if it has been manipulated so that its genetic information is altered (e.g., new genetic material not previously present has been introduced, for example by transformation, mating, somatic hybridization, transfection, transduction, electroporation, or other mechanism, or previously present genetic material is altered or removed, for example by substitution or deletion mutation, Attorney Docket No: 44807-0422WO1 or by mating protocols). As is common practice and is understood by those in the art, derivatives and/or progeny of an engineered polypeptide or cell are typically still referred to as “engineered” even though the actual manipulation was performed on a prior entity. As used herein, the term “pharmaceutical composition” refers to a composition in which an active agent is formulated together with one or more pharmaceutically acceptable carriers. In some embodiments, the composition is suitable for administration to a human or animal subject. In some embodiments, the active agent is present in unit dose amount appropriate for administration in a therapeutic regimen that shows a statistically significant probability of achieving a predetermined therapeutic effect when administered to a relevant population. As used herein, the term “specific binding” refers to an ability to discriminate between possible binding partners in the environment in which binding is to occur. A binding agent that interacts with one particular target when other potential targets are present is said to “bind specifically” to the target with which it interacts. In some embodiments, specific binding is assessed by detecting or determining degree of association between the binding agent and its partner; in some embodiments, specific binding is assessed by detecting or determining degree of dissociation of a binding agent-partner complex; in some embodiments, specific binding is assessed by detecting or determining ability of the binding agent to compete an alternative interaction between its partner and another entity. In some embodiments, specific binding is assessed by performing such detections or determinations across a range of concentrations. As used herein, the term “subject” refers an organism, typically a mammal (e.g., a human). In some embodiments, a subject is suffering from a relevant disease, disorder, or condition. In some embodiments, a subject is susceptible to a disease, disorder, or condition. In some embodiments, a subject displays one or more signs or symptoms or characteristics of a disease, disorder, or condition. In some embodiments, a subject does not display any symptom or characteristic of a disease, disorder, or condition. In some embodiments, a subject is someone with one or more features characteristic of susceptibility to or risk of a disease, disorder, or condition. In some embodiments, a subject is a patient. In some embodiments, a subject is an individual to whom diagnosis and/or therapy is and/or has been administered. As used herein, a “vector” refers to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a “plasmid”, which refers to a circular double stranded DNA loop into which additional DNA segments may be ligated. Another Attorney Docket No: 44807-0422WO1 type of vector is a viral vector, wherein additional DNA segments may be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors). Other vectors (e.g., non-episomal mammalian vectors) can be integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively linked. Such vectors are referred to herein as “expression vectors.” Standard techniques may be used for recombinant DNA, oligonucleotide synthesis, and tissue culture and transformation (e.g., electroporation, lipofection). Enzymatic reactions and purification techniques may be performed according to manufacturer's specifications or as commonly accomplished in the art or as described herein. The foregoing techniques and procedures may be generally performed according to conventional methods well known in the art and as described in various general and more specific references that are cited and discussed throughout the present specification. See e.g., Sambrook et al., Molecular Cloning: A Laboratory Manual 2^nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. (1989)), which is incorporated herein by reference for any purpose. Engineered Immune Cells Provided herein are immune cells that include a recombinant chimeric autoantigen-T cell receptor (CATCR) comprising: (a) an extracellular binding domain comprising an autoantigenic peptide (or complex containing the latter), wherein the autoantigenic peptide (or complex containing the latter) is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 complex protein. In some embodiments, the CATCR comprises at least one (a) autoantigenic epitope, peptide, or protein recognized by a B cell receptor (BCR) and at least one (b) native or modified peptide of a T cell receptor-CD3 complex protein (e.g., a T cell receptor alpha chain, beta chain, gamma chain, delta chain, a CD3 gamma subunit, a CD3 delta subunit, or a CD3 epsilon subunit, or any part thereof), and may include (c) a linker/ hinge peptide(s) or sequence(s), and/or (d) additional intracellular domains (e.g., co-stimulatory domains, immune regulatory domains). As used herein, “immune cells” or “immunoresponsive cells” refer to cells of the immune system which can be categorized as lymphocytes (e.g., T cells, B cells, and natural killer [NK] Attorney Docket No: 44807-0422WO1 cells), dendritic cells, monocytes/macrophages, granulocytes (e.g., neutrophils, eosinophils, basophils), mast cells, and their subsets. In some embodiments, the immune cell is a T cell. In some embodiments, the immune cell is a αβ-T cell. In some embodiments, the immune cell is a γδ-T cell. In some embodiments, the immune cell is an NK cell. In some embodiments, the immune cell is an NKT cell. In some embodiments, the immune cell is a monocyte or macrophage. In some embodiments, the cell is a precursor to these cells (e.g., a pluripotent stem cell) that is subsequently differentiated. In some embodiments, an immune cell is an engineered immune cell, which means the immune cell has been genetically modified to express a non-naturally occurring protein (e.g., a CATCR or an autoantigen-chimeric antigen receptor [CAR]), or modified to include a non-coded amino acid, or modified to include posttranslational modifications, or modified to include an exogenous nucleic acid. The immune cells (e.g., T cells) may be modified in one or more than one manner. The modified immune cells (e.g., T cells) may express at least one non-natural molecule that is a receptor (e.g., a CATCR or autoantigen-CAR) for an antigen that is present on the surface of one or more types of cells (in this case, a subset of B-cell receptors that bind the autoantigen incorporated into the CATCR or autoantigen-CAR). In some embodiments, immune cells include immune cells (e.g., T cells) that are not found in nature because they are engineered to comprise or express at least one synthetic molecule that is not found in nature. In specific embodiments, the immune cell can be a T cell, e.g., a αβ-T cell, a γδ-T cell, a CD4⁺ T cell, a CD8⁺ T cell, a CD3+CD4-CD8- double-negative (DN) T cell, a Treg cell, a Th1 T cell, a Th2 T cell, a Th17 T cell, another subset of T cells, or a population of T cells that comprises a combination of any of the foregoing. In some embodiments, the immune cells (e.g., T cells) are engineered to express a chimeric autoantigen-T cell receptor (CATCR), including a CATCR that binds specifically to a B cell receptor (BCR) that targets an autoantigen. In some embodiments, the immune cells (e.g., T cells) are engineered to express a chimeric antigen-T cell receptor that binds specifically to a B cell receptor (BCR) that targets an allergen. As used herein, a “chimeric autoantigen-T cell receptor” refers to a T-cell receptor that has been genetically engineered to produce an artificial autoantigen-directed T-cell receptor for use in immunotherapy. A T-cell receptor (TCR) is a protein complex found on the surface of T cells or T lymphocytes, wherein the TCR is responsible for recognizing presented antigen, immune synapse formation, inducing intracellular signaling, and initiating target cell killing. The TCR can Attorney Docket No: 44807-0422WO1 include an extracellular antigen-binding domain, a transmembrane domain, and an intracellular signaling domain. In some embodiments, the TCR includes a CD3 gamma (CD3 ^) chain, a CD3 epsilon (CD3ε) chain, a CD3 delta (CD3δ) chain, a T cell receptor (TCR) alpha chain (with variable [V] and/or constant [C] regions), a T cell receptor (TCR) beta chain (with variable [V] and/or constant [C] regions), a T cell receptor (TCR) gamma chain (with variable [V] and/or constant [C] regions), and a T cell receptor (TCR) delta chain (with variable [V] and/or constant [C] regions). In some embodiments, the TCR can further include a CD3 zeta (CD3ζ) chain. In some embodiments, a chimeric autoantigen-T cell receptor (CATCR) can include (a) an autoantigenic epitope, peptide, or protein recognized by a B cell receptor (BCR) and (b) native or modified peptide of a T cell receptor-CD3 complex protein (e.g., a modified T cell receptor alpha chain, beta chain, gamma chain, delta chain, a CD3 gamma chain, a CD3 delta chain, or a CD3 epsilon chain, or any part thereof), and additionally may include (c) linker/ hinge peptide(s) or sequence(s), (d) additional intracellular domains (e.g., co-stimulatory domains, immune regulatory domains). In some embodiments, a CATCR comprises a modified CD3-TCR protein complex that is expressed on the surface of the engineered immune cell. Autoantigens As used herein, the term “autoantigen” refers to an antigen that, despite being a normal tissue constituent in health or disease, is the target of a humoral or cell-mediated immune response. In some embodiments, an autoantigen is an endogenous self-antigen that stimulates autoantibody production that evokes an immune response by the host. In some embodiments, the autoantigen is a peptide, polypeptide, domain, or other part derived from phospholipid-binding proteins that are targeted in APS. In some embodiments, an autoantigen is the full protein or the protein- phospholipid complex. In some embodiments, the autoantigen is the phospholipid binding protein beta-2 glycoprotein I (β2GPI) or any part thereof, endothelial protein C receptor (EPCR) or any part thereof, or prothrombin (PT) or any part thereof. In some embodiments, the autoantigen is the murine or another mammalian version of β2GPI, EPCR, or PT. In some embodiments, the autoantigen is a bacterial, viral, or synthetic mimotope of β2GPI, EPCR, or PT. In certain embodiments, the chimeric autoantigen-T-cell receptor (CATCR) comprises autoantigenic peptides of and targets B-cell receptors (BCRs) that bind one or more of the following: beta-2-glycoprotein 1/ B2GPI (Gene Name: APOH, UniProt ID: P02749), endothelial Attorney Docket No: 44807-0422WO1 protein C receptor/ EPCR (PROCR, Q9UNN8), prothrombin (F2, P00734), cardiolipin, lysobisphosphatidic acid, phosphatidylserine, annexin A2 (ANXA2, P07355), Annexin A5 (ANXA5, P08758); histone H1.0 (H10, P07305), histone H1.1 (H1-1, Q02539), histone H1.2 (H1- 2, P16403), histone H1.3 (H1-3, P16402), histone H1.4 (H1-4, P10412), histone H1.5 (H1-5, P16401), histone H1t (H1-6, P22492), testis-specific H1 histone (H1-7, Q75WM6), histone H1.8 (H1-8, Q8IZA3), histone H1.10 (H1-10, Q92522), histone H2A proteins, histone H2B proteins, histone H3 proteins, histone H4 (H4C1, P62805), hnRNP-A0 (HNRNPA0, Q13151), hnRNP-A1 (HNRNPA1, P09651), hnRNP-A1-like 2 (HNRNPA1L2, Q32P51), hnRNP-A2/B1 (HNRNPA2B1, P22626), hnRNP-A3 (HNRNPA3, P51991), hnRNP-A/B (HNRNPAB, Q99729), hnRNP-C1/C2 (HNRNPC, P07910), hnRNP-C-like 1 (HNRNPCL1, O60812), hnRNP-C-like 2 (HNRNPCL2, B2RXH8), hnRNP-D0 (HNRNPD, Q14103), hnRNP-DL (HNRNPDL, O14979), hnRNP-E1, hnRNP-F (HNRNPF, P52597), hnRNP-H (HNRNPH1, P31943), hnRNP-H2 (HNRNPH2, P55795), hnRNP-H3 (HNRNPH3, P31942), hnRNP-I (PTBP1, P26599), hnRNP K (HNRNPK, P61978), hnRNP-L (HNRNPL, P14866), hnRNP-L-like (HNRNPLL, Q8WVV9), hnRNP-M (HNRNPM, P52272), hnRNP-Q (HNRPQ, O60506), hnRNP-R (HNRNPR, O43390), hnRNP-U (HNRNPU, Q00839), hnRNP-U-like protein 1 (HNRNPUL1, Q9BUJ2), Protein- arginine deiminase type-1/ PAD1 (Q9ULC6), Protein-arginine deiminase type-2/ PAD2 (PADI2, Q9Y2J8), Protein-arginine deiminase type-3/ PAD3 (PADI3, 9ULW8), Protein-arginine deiminase type-4/ PAD4 (PADI4, Q9UM07), vimentin (VIM, P08670), filaggrin (FLG, P20930), filaggrin-2 (FLG2, Q5D862), fibrinogen alpha chain (FGA, P02671), fibrinogen beta chain (FGB, P02675), fibrinogen gamma chain (FGG, P02679), fibronectin (FN1, P02751), alpha-enolase (ENO1, P06733), elongation factor 1-alpha 1 (EEF1A1, P68104), elongation factor 1-alpha 2 (EEF1A2, Q05639), beta-actin (ACTB, P60709), gamma-actin (ACTG1, P63261), alpha-1 type I collagen (COL1A1, P02452), alpha-2 type I collagen (COL1A2, P08123), alpha-1 type II collagen (COL2A1, P02458), fructose-bisphosphate aldolase A (ALDOA, P04075), fructose-bisphosphate aldolase B (ALDOB, P05062), fructose-bisphosphate aldolase C (ALDOC, P09972), heat shock 60 kDa proteins (HSP60), heat shock 70 kDa proteins (HSP70), heat shock protein HSP 90 proteins (HSP90), immunoglobulin gamma-1 heavy chain (IGHG1, P01857), immunoglobulin heavy constant gamma 2 (IGHG2, P01859), immunoglobulin heavy constant gamma 3 (IGHG3, P01860), immunoglobulin heavy constant gamma 4 (IGHG4, P01861); myeloblastin/ proteinase 3 (PRTN3, P24158), myeloperoxidase (MPO, P05164), neutrophil elastase (ELANE, P08246), Attorney Docket No: 44807-0422WO1 lysosome-associated membrane glycoprotein 2 (LAMP2, P13473), collagen alpha-3(IV) chain (COL4A3, Q01955), secretory phospholipase A2 receptor (PLA2R1, Q13018), thrombospondin type-1 domain-containing protein 7A (THSD7A, Q9UPZ6); histone H3-like centromeric protein A/ CENP-A (CENPA, P49450), major centromere autoantigen B/ CENP-B (CENPB, P07199), centromere protein C/ CENP-C (CENPC, Q03188), DNA topoisomerase 1/ Scl-70 (TOP1, P11387), exosome complex component RRP45/ PM/Scl-75 (EXOSC9, Q06265), exosome component 10/ PM/Scl-100 (EXOSC10, Q01780), DNA-directed RNA polymerase III subunit RPC1 (POLR3A, O14802), DNA-directed RNA polymerase III subunit RPC2 (POLR3B, Q9NW08), DNA-directed RNA polymerase III subunit RPC3 (POLR3C, POLR3C), DNA- directed RNA polymerase III subunit RPC4 (POLR3D, P05423), DNA-directed RNA polymerase III subunit RPC5 (POLR3E, Q9NVU0), DNA-directed RNA polymerase III subunit RPC6 (POLR3F, Q9H1D9), DNA-directed RNA polymerase III subunit RPC7 (POLR3G, O15318), DNA-directed RNA polymerase III subunit RPC8 (POLR3H, Q9Y535), DNA-directed RNA polymerase III subunit RPC9 (CRCP, O75575), DNA-directed RNA polymerase III subunit RPC10 (POLR3K, Q9Y2Y1), DNA-directed RNA polymerases I and III subunit RPAC1 (POLR1C, O15160), DNA-directed RNA polymerases I and III subunit RPAC2 (POLR1D, P0DPB6), DNA-directed RNA polymerases I, II, and III subunit RPABC1 (POLR2E, P19388), DNA-directed RNA polymerases I, II, and III subunit RPABC2 (POLR2F, P61218), DNA- directed RNA polymerases I, II, and III subunit RPABC3 (POLR2H, P52434), DNA-directed RNA polymerases I, II, and III subunit RPABC4 (POLR2K, P53803), DNA-directed RNA polymerases I, II, and III subunit RPABC5 (POLR2L, P62875), RNA Binding Region Containing 3/ RNPC3 (RNPC3, Q96LT9), ribonuclease P protein subunit p25/ Th/To antigen (RPP25, Q9BUL9), translation initiation factor eIF-2B subunit alpha (EIF2B1, Q14232), translation initiation factor eIF-2B subunit beta (EIF2B2, P49770), translation initiation factor eIF-2B subunit gamma (EIF2B3, Q9NR50), translation initiation factor eIF-2B subunit delta (EIF2B4, Q9UI10), translation initiation factor eIF-2B subunit epsilon (EIF2B5, Q13144), gamma-interferon- inducible protein 16 (IFI16, Q16666), protein bicaudal D homolog 2 (BICD2, Q8TD16), fibrillin- 1 (FBN1, P35555), rRNA 2'-O-methyltransferase fibrillarin/ fibrillarin 34 kDa (FBL, P22087), X- ray repair cross-complementing protein 6/ 70 kDa subunit of Ku antigen (XRCC6, P12956), X- ray repair cross-complementing protein 5/ 86 kDa subunit of Ku antigen (XRCC5, P13010); interferon-induced helicase C domain-containing protein 1/ melanoma differentiation-associated Attorney Docket No: 44807-0422WO1 protein 5 (IFIH1, Q9BYX4), chromodomain-helicase-DNA-binding protein 4/ Mi-2 antigen (CHD4, Q14839), chromodomain-helicase-DNA-binding protein 3/ Mi-2 antigen (CHD3, Q12873), histidine--tRNA ligase, cytoplasmic/ Jo-1 antigen (HARS1, P12081), histidine--tRNA ligase, mitochondrial (HARS2, P49590), threonine--tRNA ligase 1, cytoplasmic/ PL-7 antigen (TARS1, P26639), threonine--tRNA ligase, mitochondrial (TARS2, Q9BW92), threonine--tRNA ligase 2, cytoplasmic (TARS3, A2RTX5), alanine--tRNA ligase, cytoplasmic/ PL-12 antigen (AARS1, P49588), alanine--tRNA ligase, mitochondrial (AARS2, Q5JTZ9), glycine--tRNA ligase/ EJ antigen (GARS1, P41250), isoleucine--tRNA ligase, cytoplasmic/ OJ antigen (IARS1, P41252), isoleucine--tRNA ligase, mitochondrial (IARS2, Q9NSE4), asparagine--tRNA ligase, cytoplasmic/ KS antigen (NARS1, O43776), probable asparagine--tRNA ligase, mitochondrial (NARS2, Q96I59), phenylalanine--tRNA ligase alpha subunit/ ZO antigen (FARSA, Q9Y285), phenylalanine--tRNA ligase beta subunit (FARSB, Q9NSD9), phenylalanine--tRNA ligase, mitochondrial (FARS2, O95363), tyrosine--tRNA ligase, cytoplasmic/ HA antigen (YARS1, P54577), tyrosine--tRNA ligase, mitochondrial (YARS2, Q9Y2Z4), 3-hydroxy-3-methylglutaryl- coenzyme A reductase (HMGCR, P04035), signal recognition particle subunit SRP72 (SRP72, O76094), signal recognition particle subunit SRP68 (SRP68, Q9UHB9), signal recognition particle 54 kDa protein (SRP54, P61011), signal recognition particle 14 kDa protein (SRP14, P37108), signal recognition particle 19 kDa protein (SRP19, SRP19), signal recognition particle 9 kDa protein (SRP9, P49458), E3 ubiquitin-protein ligase TRIM33/ Transcription intermediary factor 1-gamma (TRIM33, Q9UPN9), MORC family CW-type zinc finger protein 3/ nuclear matrix protein 2 (MORC3, Q14149), SUMO-activating enzyme subunit 1/ SAE antigen (SAE1, Q9UBE0), SUMO-activating enzyme subunit 2/ SAE antigen (UBA2, Q9UBT2), cytosolic 5'- nucleotidase 1A (NT5C1A, Q9BXI3), cell division cycle and apoptosis regulator protein 1 (CCAR1, Q8IX12), transcription factor SOX-5 (SOX5, P35711); E3 ubiquitin-protein ligase TRIM21/ Ro-52 kDa (TRIM21, P19474), RNA-binding protein RO60/ Ro-60 kDa (RO60, P10155), E3 ubiquitin-protein ligase TRIM68 (TRIM68, Q6AZZ1), Lupus La protein/ La (SSB, P05455); double-stranded DNA (dsDNA), single-stranded DNA (ssDNA), messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA), or their protein complexes; small nuclear ribonucleoprotein Sm D1 (SNRPD1, P62314), small nuclear ribonucleoprotein Sm D2 (SNRPD2, P62316), small nuclear ribonucleoprotein Sm D3 (SNRPD3, P62318); small nuclear ribonucleoprotein Sm E (SNRPE, P62304), small nuclear ribonucleoprotein Sm F (SNRPF, Attorney Docket No: 44807-0422WO1 P62306), small nuclear ribonucleoprotein Sm G (SNRPG, P62308), small nuclear ribonucleoprotein-associated proteins B and B' (SNRPB, P14678), small nuclear ribonucleoprotein-associated protein N/ Sm-N (SNRPN, P63162), U1 small nuclear ribonucleoprotein 70 kDa (SNRNP70, P08621), U1 small nuclear ribonucleoprotein C (SNRPC, P09234), U1 small nuclear ribonucleoprotein A (SNRPA, P09012), U2 small nuclear ribonucleoprotein A' (SNRPA1, P09661), U2 small nuclear ribonucleoprotein B'' (SNRPB2, P08579), 60S acidic ribosomal protein P0 (RPLP0, P05388), 60S acidic ribosomal protein P1 (RPLP1, P05386), 60S acidic ribosomal protein P2 (RPLP2, P05387), plasma protease C1 inhibitor (SERPING1, P05155), complement C1q subcomponent subunit A (C1QA, P02745), complement C1q subcomponent subunit B (C1QB, P02746), complement C1q subcomponent subunit C (C1QC, P02747), glycosylphosphatidylinositol-anchored high density lipoprotein- binding protein 1 (GPIHBP1, Q8IV16); a disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAMTS13, Q76LX8), complement factor H (CFH, P08603), complement factor I (CFI, P05156), von Willebrand factor (VWF, P04275), coagulation factor VIII (F8, P00451), integrin alpha-IIb (GPIIb) (ITGA2B, P08514), integrin beta-3 (GPIIIa) (ITGB3, P05106), platelet glycoprotein Ib alpha chain (GPIb) (GP1BA, P07359), platelet glycoprotein Ib beta chain (GP1BB, P13224), platelet glycoprotein IX (GP9, P14770), integrin alpha-2 (ITGA2, P17301), integrin beta-1 (ITGB1, P05556), platelet glycoprotein 4 (CD36, P16671), platelet glycoprotein V (GP5, P40197), P-selectin (SELP, Q14242), platelet factor 4 (PF4, P02776); aquaporin-4 M1 (AQP4, P55087), aquaporin-4 M23 (AQP4, P55087), aquaporin-4 orthogonal arrays, myelin proteolipid protein (PLP1, P60201), myelin-oligodendrocyte glycoprotein (MOG, Q16653), myelin basic protein (MBP, P02686), myelin-associated oligodendrocyte basic protein (MOBP, Q13875), myelin-associated glycoprotein (MAG, P20916), alpha-crystallin B chain (CRYAB, P02511), glial fibrillary acidic protein (GFAP, P14136), claudin-11 (Claudin-11, O75508), endoplasmic reticulum chaperone BiP (HSPA5, P11021); acetylcholine receptor subunit alpha (CHRNA1, P02708), acetylcholine receptor subunit beta (CHRNB1, P11230), acetylcholine receptor subunit gamma (CHRNG, P07510), acetylcholine receptor subunit delta (CHRND, Q07001), acetylcholine receptor subunit epsilon (CHRNE, Q04844), muscle skeletal receptor tyrosine- protein kinase (MUSK, O15146), low-density lipoprotein receptor-related protein 4 (LRP4, O75096), agrin (AGRN, O00468), acetylcholinesterase collagenic tail peptide (COLQ, Q9Y215), α-subunit of the voltage-gated potassium channel Kv1.4, titin (TTN, Q8WZ42), ryanodine Attorney Docket No: 44807-0422WO1 receptor 1 (RYR1, P21817), ryanodine receptor 2 (RYR2, Q92736), ryanodine receptor 3 (RYR3, Q15413), A-kinase anchor protein 12 (AKAP12, Q02952); glutamate receptor ionotropic, NMDA 1/ GluN1 (GRIN1, Q05586), glutamate receptor ionotropic, NMDA 2A/ GluN2A (GRIN2A, Q12879), glutamate receptor ionotropic, NMDA 2B/ GluN2B (GRIN2B, Q13224), glutamate receptor ionotropic, NMDA 2C/ GluN2C (GRIN2C, Q14957), glutamate receptor ionotropic, NMDA 2D/ GluN2D (GRIN2D, O15399), cerebellar degeneration-related protein 2/ Yo antigen (CDR2, Q01850), ELAV-like protein 1 (ELAV-like protein 1, Q15717), ELAV-like protein 2 (ELAVL2, Q12926), ELAV-like protein 3 (ELAVL3, Q14576), ELAV-like protein 4 (ELAVL4, P26378), leucine-rich glioma-inactivated protein 1 (LGI1, O95970), contactin-associated protein- like 2/ CASPR2 (CNTNAP2, Q9UHC6), contactin-2 (CNTN2, Q02246), dihydropyrimidinase- related protein 5/ CRMP5 (DPYSL5, Q9BPU6), glutamate receptor 1/ GluA1 (GRIA1, P42261), glutamate receptor 2/ GluA2 (GRIA2, P42262), glutamate receptor 3/ GluA3 (GRIA3, P42263), glutamate receptor 4/ GluA4 (GRIA4, P48058), gamma-aminobutyric acid receptor subunit alpha- 1 (GABRA1, P14867), gamma-aminobutyric acid receptor subunit beta-3 (GABRB3, P28472), gamma-aminobutyric acid type B receptor subunit 1 (GABBR1, Q9UBS5), gamma-aminobutyric acid type B receptor subunit 2 (GABBR2, O75899), gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2, P18507), metabotropic glutamate receptor 1 (GRM1, Q13255), metabotropic glutamate receptor 5 (GRM5, P41594), amphiphysin (AMPH, P49418), adenylate kinase isoenzyme 5 / AK5 (AK5, AK5), dipeptidyl aminopeptidase-like protein 6 (DPP6, P42658), delta and Notch-like epidermal growth factor-related receptor (DNER, Q8NFT8), neurexin-3 (NRXN3, Q9Y4C0), RNA-binding protein Nova-1/ Ri antigen (NOVA1, P51513), paraneoplastic antigen Ma1 (PNMA1, Q8ND90), paraneoplastic antigen Ma2 (PNMA2, Q9UL42), paraneoplastic antigen Ma3 (PNMA3, Q9UL41), modulator of apoptosis 1/ Ma4 (MOAP1, Q96BY2), microtubule-associated protein 1B (MAP1B, P46821), dihydropyrimidinase-related protein 1 (CRMP1, Q14194); ganglioside GM1, ganglioside GM1b, ganglioside GD1a, ganglioside GD1b, ganglioside GQ1b, ganglioside GT1a; protein-glutamine gamma- glutamyltransferase 2 (TGM2, P21980), protein-glutamine gamma-glutamyltransferase E (TGM3, Q08188), protein-glutamine gamma-glutamyltransferase 6 (TGM6, O95932); thyroid peroxidase (TPO, P07202), thyrotropin receptor (TSHR, P16473), thyroglobulin (TG, P01266); islet cell autoantigen 1 (ICA1, Q05084); islet cell autoantigen 1-like protein (ICA1L, Q8NDH6); glutamate decarboxylase 1 (GAD1, Q99259), glutamate decarboxylase 2 (GAD-65) (GAD2, Q05329); Attorney Docket No: 44807-0422WO1 receptor-type tyrosine-protein phosphatase-like N / IA2 (PTPRN, Q16849); receptor-type tyrosine-protein phosphatase N2/ IAR (PTPRN2, Q92932), zinc transporter 8 (SLC30A8, Q8IWU4); steroid 21-hydroxylase (CYP21A2, P08686), steroid 17-alpha-hydroxylase/17,20 lyase (CYP17A1, P05093), 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 (HSD3B2, P26439), adrenocorticotropic hormone receptor (MC2R, Q01718), NACHT, LRR and PYD domains-containing protein 5 (NLRP5, P59047), testis-specific gene 10 protein (TSGA10, Q9BZW7), hyaluronidase PH-20 (SPAM1, P38567), disintegrin and metalloproteinase domain- containing protein 2 (ADAM2, Q99965), follicle-stimulating hormone receptor (FSHR, P23945), follitropin subunit beta (FSHB, P01225), glycoprotein hormones alpha chain (CGA, P01215), lutropin-choriogonadotropic hormone receptor (LHCGR, P22888), lutropin subunit beta (LHB, P01229); cholesterol side-chain cleavage enzyme, mitochondrial (CYP11A1, P05108); cobalamin binding intrinsic factor (CBLIF, P27352), potassium-transporting ATPase alpha chain 1 (ATP4A, P20648), potassium-transporting ATPase subunit beta (ATP4B, P51164); desmoglein-1 (DSG1, Q02413), desmoglein-3 (DSG3, P32926), collagen alpha-1(XVII) chain/ 180 kDa bullous pemphigoid antigen (COL17A1, Q9UMD9), dystonin/ 230 kDa bullous pemphigoid antigen (DST, Q03001), collagen alpha-1(VII) chain (COL7A1, Q02388), envoplakin (EVPL, Q92817), epiplakin (EPPK1, P58107), periplakin (PPL, O60437), plectin (PLEC, Q15149), desmoplakin (DSP, P15924), desmocollin-1 (DSC1, Q08554), laminin gamma-1, laminin 5, laminin 6, ladinin- 1 (LAD1, O00515), integrin alpha-4 (ITGA4, P13612), integrin beta-6 (ITGB6, P18564), neuronal acetylcholine receptor subunit alpha-9 (CHRNA9, Q9UGM1); tumor necrosis factor (TNF, P01375), lymphotoxin-alpha (LTA, P01374), granulocyte-macrophage colony-stimulating factor (CSF2, P04141), granulocyte colony-stimulating factor (CSF3, P09919), interleukin-1 alpha (IL1A, P01583), interleukin-1 beta (IL1B, P01584), interleukin-6 (IL6, P05231), interleukin-17A (IL17A, Q16552), interleukin-17F (IL17F, Q96PD4), interferon alpha-1/13 (IFNA1, P01562), interferon alpha-2 (IFNA2, P01563), interferon alpha-4 (IFNA4, P05014), interferon alpha-5 (IFNA5, P01569), interferon alpha-6 (IFNA6, P05013), interferon alpha-7 (IFNA7, P01567), interferon alpha-8 (IFNA8, P32881), interferon alpha-10 (IFNA10, P01566), interferon alpha-14 (IFNA14, P01570), interferon alpha-16 (IFNA16, P48551), interferon alpha-17 (IFNA17, P01571), interferon alpha-21 (IFNA21, P01568), interferon omega-1 (IFNW1, P05000), interferon kappa (IFNK, Q9P0W0), interferon lambda-1 (IFNL1, Q8IU54), interferon lambda-2 (IFNL2, Q8IZJ0), interferon lambda-3 (IFNL3, Q8IZI9), interferon lambda-4 (IFNL4, K9M1U5), Attorney Docket No: 44807-0422WO1 interferon gamma (IFNG, P01579); cytochrome P450 2D6/ LKM-1 (CYP2D6, P10635), cytochrome P450 2C9 (CYP2C9, P11712), cytochrome P450 2A6 (CYP2A6, P11509), UDP- glucuronosyltransferase 1A (UGT1A1, P22309), cytochrome P450 1A2 (CYP1A2, P05177), formimidoyltransferase-cyclodeaminase (FTCD, O95954), dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial/ PDC-E2 (DLAT, P10515), dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial/ OGDC-E2 (DLST, P36957), lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial/ BCOADC- E2 (DBT, P11182), pyruvate dehydrogenase complex protein X component, mitochondrial (PDX1, P16451), dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (DLAT, P10515), nuclear autoantigen Sp-100 (SP100, P23497), coilin (COIL, P38432), nuclear pore membrane glycoprotein 210 (NUP210, Q8TEM1), lamin-B receptor (LBR, Q8MLV1), nuclear pore glycoprotein p62 (NUP62, P37198), o- phosphoseryl-tRNA(Sec) selenium transferase (SEPSECS, Q9HD40), or any parts thereof, any of their isoforms, any of their splicing variants, any autoantigenic complexes with other proteins, nucleic acids, lipids, or carbohydrates containing the same, in either their unmodified or in their post-translationally modified (e.g., citrullinated, carbamylated, acetylated, glycosylated, γ- carboxylated, among many other), or proteolytically processed forms. In certain embodiments, the chimeric autoantigen-T-cell receptor (CATCR) comprises autoantigenic peptides that are citrullinated or carbamylated, in which the modified peptide binds to anti-citrullinated protein or anti-carbamylated protein B-cell receptors (BCRs). In certain embodiments, the chimeric autoantigen-T-cell receptor (CATCR) comprises autoantigenic peptides with at least 85% sequence identity, at least 90% sequence identity, at least 95% sequence identity, at least 96% sequence identity, at least 97% sequence identity, at least 98% sequence identity, or at least 99% sequence identity to the Uniprot consensus protein sequences of the foregoing autoantigens, or their splice variants, or any parts thereof. In certain embodiments, the chimeric antigen-T-cell receptor targets B-cell receptors (BCRs) that bind to other autoantigens. In certain embodiments, the chimeric antigen-T-cell receptor targets B-cell receptors (BCRs) that bind to allergens or haptens. For example, in some embodiments, the chimeric autoantigen-T-cell receptor (CATCR) can comprise an autoantigenic peptide having a sequence from SEQ ID NO: 1-20 (Table 1). In Attorney Docket No: 44807-0422WO1 some embodiments, the CATCR can comprise a sequence having at least 75% sequence identity, at least 80% sequence identity, at least 85% sequence identity, at least 90% sequence identity, at least 95% sequence identity, at least 96% sequence identity, at least 97% sequence identity, at least 98% sequence identity, or at least 99% sequence identity to an autoantigenic peptide provided in Table 1, or fragments thereof, and/or may optionally comprise up to one or up to two or up to three conservative amino acid substitutions.

Attorney Docket No: 44807-0422WO1 [Table 1] Examples of autoantigenic peptides incorporated into CATCRs or CARs SEQ ID  UniProt  Name  Amino Acid Sequence (unless specified otherwise)  NO.  ID   1  P02749  APOH_HUMAN  MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGG TC AT GA AG AA TC TT AC GA CT AT TA GG AA O: Attorney Docket No: 44807-0422WO1 P02749  APOH_HUMAN  GRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKC Domain I (Beta‐ TPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAP 2‐glycoprotein  IICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPE CREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPS q  TC AT GA AA AA TC CT AT GG TT TT TG AG AA O: TG AA TG CC GG TT CA GT CG AG Attorney Docket No: 44807-0422WO1 17  Q9UNN8  EPCR_HUMAN  SQDASDGLQRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTIIQLQPLQEPE (Endothelial  SWARTQSGLQSYLLQFHGLVRLVHQERTLAFPLTIRCFLGCELPPEGSRAHVFFEVAVNG protein C  SSFVSFRPERALWQADTQVTSGVVTFTLQQLNAYNRTRYELREFLEDTCVQYVQKHISAE NTKGSQTSRSYTS [SEQ ID NO. 17] CA TT CC GA CG CT CA GG TG CT CT CT GG AG AA CA AG AT GT AA CC CA AA GA TC TT A E Q G D D H I L In some embodiments, the CATCR includes an epitope/ autoantigenic peptide/ autoantigen recognized by a B-cell receptor. In some embodiments, the autoantigen is expressed as part of a Attorney Docket No: 44807-0422WO1 modified CD3 gamma (CD3 ^) chain; as part of a modified CD3 epsilon (CD3ε) chain; as part of a modified CD3 delta (CD3δ) chain; as part of a modified T cell receptor (TCR) alpha chain; as part of a modified T cell receptor (TCR) beta chain; as part of a modified T cell receptor (TCR) gamma chain; or as part of a modified T cell receptor (TCR) delta chain of the CATCR. In some embodiments, the epitope/ autoantigenic peptide/ autoantigen is expressed at the N-terminus of the CD3 gamma (CD3 ^) chain. In some embodiments, the autoantigenic peptide is expressed as part of the extracellular domain of the CD3 gamma (CD3 ^) fusion protein. In some embodiments, the autoantigenic peptide is expressed at the N-terminus of the CD3 epsilon (CD3ε) chain. In some embodiments, the autoantigenic peptide is expressed as part of the extracellular domain of the CD3 epsilon (CD3ε) fusion protein. In some embodiments, the autoantigenic peptide is expressed at the N-terminus of the CD3 delta (CD3δ) chain. In some embodiments, the autoantigenic peptide is expressed as part of the extracellular domain of the CD3 delta (CD3δ) fusion protein. In some embodiments, the autoantigenic peptide is expressed at the N-terminus of the T cell receptor (TCR) alpha chain. In some embodiments, the autoantigenic peptide is expressed as part of the extracellular domain of the T cell receptor (TCR) alpha chain fusion protein. In some embodiments, the autoantigenic peptide is expressed at the N-terminus of the T cell receptor (TCR) beta chain. In some embodiments, the autoantigenic peptide is expressed as part of the extracellular domain of the T cell receptor (TCR) beta chain fusion protein. In some embodiments, the autoantigenic peptide is expressed at the N-terminus of the T cell receptor (TCR) gamma chain. In some embodiments, the autoantigenic peptide is expressed as part of the extracellular domain of the T cell receptor (TCR) gamma chain fusion protein. In some embodiments, the autoantigenic peptide is expressed at the N-terminus of the T cell receptor (TCR) delta chain. In some embodiments, the autoantigenic peptide is expressed as part of the extracellular domain of the T cell receptor (TCR) delta chain fusion protein. In some embodiments, the autoantigenic peptide is linked to the constant region of the T cell receptor (TCR) alpha (Cα), beta (Cβ), gamma (C ^), or delta (Cδ) chain. In some embodiments, the autoantigenic peptide is linked to the variable region of the T cell receptor (TCR) alpha (Vα), beta (Vβ), gamma (V ^), or delta (Vδ) chain. For example, in some embodiments, the CATCR can comprise a peptide of a T cell receptor-CD3 complex protein including a sequence from SEQ ID NOs: 21-44 (Table 2). Attorney Docket No: 44807-0422WO1 [Table 2] Examples of TCR-CD3 complex domains incorporated into CATCRs SEQ ID  UniProt ID   Name  Amino Acid Sequence (unless specified otherwise)  NO.  21  P09693  CD3G_HUMAN  MEQGKGLAVLILAIILLQGTLAQSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGK TG TA GC TG AG TT CT AT ] CC CA GC CT CT CT AG CT GG GA AT TG CA AT TG CT AG Q Attorney Docket No: 44807-0422WO1 27  P20963  CD3Z_HUMAN  MKWKALFTAAILQAQLPITEAQSFGLLDPKLCYLLDGILFIYGVILTALFLRVKFSRSAD (CD3ζ)  APAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPQRRKNPQEGLYNELQKDKMA EAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR [SEQ ID NO 27] CA AT CG AT AC TT CA D CT TG TG AA AA AA AV LK   TC AG TC CC AG GG TC TG Attorney Docket No: 44807-0422WO1 Nucleotide sequence T cell receptor beta constant 2/ TRBC2 (Ensembl ENSG00000211772;  RefSeq NG_001333):  NAGGACCTGAAAAACGTGTTCCCACCCAAGGTCGCTGTGTTTGAGCCATCAGAAGCAGAGATC AG TC CC AG GG TC TG PL AW AI GF CC CG TT AC AC TT AI GF AY AD 8] TT AG AC AC GG AC TC TC AY AD AY AD 0] TT AG AC AC GG AC TC Attorney Docket No: 44807-0422WO1 CTACTGGGGAAGGCCACCCTATATGCTGTGCTGGTCAGTGGCCTGGTGCTGATGGCCATGGTC AAGAAAAAAAATTCCTGA [SEQ ID NO: 232] 41 TRBC2 MOUSE EDLRNVTPPKVSLFEPSKAEIANKQKATLVCLARGFFPDHVELSWWVNGKEVHSGVCTDPQAY AD 1] 9;  AA TT TG AA TT AT TC GC 1;  AA TT TG AA TT AT TG AT CA GT CA AA CT AG TG TG In some embodiments, the autoantigenic peptide is directly linked to a TCR chain (alpha, beta, gamma, or delta) or CD3 subunit (gamma, delta, or epsilon). In some embodiments, the autoantigenic peptide is indirectly linked to a TCR chain (alpha, beta, gamma, or delta) or CD3 subunit (gamma, delta, or epsilon) via one or more linker, hinge, or dimerization sequences. In some embodiments, the TCR or CD3 fusion protein comprises one or more additional intracellular Attorney Docket No: 44807-0422WO1 domains (e.g., a co-stimulatory domain, an immune regulatory domain, an inhibitory domain, a signaling domain, or combinations thereof). In some embodiments, the TCR or CD3 fusion protein sequence can comprise a self-cleaving peptide sequence. In some embodiments, the self-cleaving peptide sequence can include a sequence from SEQ ID NOs: 45-48 (Table 3), including or excluding the furin recognition site. In some embodiments, the TCR or CD3 fusion protein can comprise a signal peptide sequence. In some embodiments, the signal peptide can include a sequence from SEQ ID NOs: 49-57 (Table 4). In some embodiments, the signal peptide is an endogenous signal peptide sequence from beta-2-glycoprotein 1/ B2GPI (Gene Name: APOH, UniProt ID: P02749), endothelial protein C receptor/ EPCR (PROCR, Q9UNN8), prothrombin (F2, P00734), cardiolipin, lysobisphosphatidic acid, phosphatidylserine, annexin A2 (ANXA2, P07355), Annexin A5 (ANXA5, P08758); histone H1.0 (H10, P07305), histone H1.1 (H1-1, Q02539), histone H1.2 (H1-2, P16403), histone H1.3 (H1-3, P16402), histone H1.4 (H1-4, P10412), histone H1.5 (H1-5, P16401), histone H1t (H1-6, P22492), testis-specific H1 histone (H1-7, Q75WM6), histone H1.8 (H1-8, Q8IZA3), histone H1.10 (H1-10, Q92522), histone H2A proteins, histone H2B proteins, histone H3 proteins, histone H4 (H4C1, P62805), hnRNP-A0 (HNRNPA0, Q13151), hnRNP-A1 (HNRNPA1, P09651), hnRNP-A1-like 2 (HNRNPA1L2, Q32P51), hnRNP-A2/B1 (HNRNPA2B1, P22626), hnRNP-A3 (HNRNPA3, P51991), hnRNP- A/B (HNRNPAB, Q99729), hnRNP-C1/C2 (HNRNPC, P07910), hnRNP-C-like 1 (HNRNPCL1, O60812), hnRNP-C-like 2 (HNRNPCL2, B2RXH8), hnRNP-D0 (HNRNPD, Q14103), hnRNP- DL (HNRNPDL, O14979), hnRNP-E1, hnRNP-F (HNRNPF, P52597), hnRNP-H (HNRNPH1, P31943), hnRNP-H2 (HNRNPH2, P55795), hnRNP-H3 (HNRNPH3, P31942), hnRNP-I (PTBP1, P26599), hnRNP K (HNRNPK, P61978), hnRNP-L (HNRNPL, P14866), hnRNP-L-like (HNRNPLL, Q8WVV9), hnRNP-M (HNRNPM, P52272), hnRNP-Q (HNRPQ, O60506), hnRNP-R (HNRNPR, O43390), hnRNP-U (HNRNPU, Q00839), hnRNP-U-like protein 1 (HNRNPUL1, Q9BUJ2), Protein-arginine deiminase type-1/ PAD1 (Q9ULC6), Protein-arginine deiminase type-2/ PAD2 (PADI2, Q9Y2J8), Protein-arginine deiminase type-3/ PAD3 (PADI3, 9ULW8), Protein-arginine deiminase type-4/ PAD4 (PADI4, Q9UM07), vimentin (VIM, P08670), filaggrin (FLG, P20930), filaggrin-2 (FLG2, Q5D862), fibrinogen alpha chain (FGA, P02671), fibrinogen beta chain (FGB, P02675), fibrinogen gamma chain (FGG, P02679), fibronectin (FN1, P02751), alpha-enolase (ENO1, P06733), elongation factor 1-alpha 1 (EEF1A1, P68104), elongation factor 1-alpha 2 (EEF1A2, Q05639), beta-actin (ACTB, P60709), gamma-actin Attorney Docket No: 44807-0422WO1 (ACTG1, P63261), alpha-1 type I collagen (COL1A1, P02452), alpha-2 type I collagen (COL1A2, P08123), alpha-1 type II collagen (COL2A1, P02458), fructose-bisphosphate aldolase A (ALDOA, P04075), fructose-bisphosphate aldolase B (ALDOB, P05062), fructose-bisphosphate aldolase C (ALDOC, P09972), heat shock 60 kDa proteins (HSP60), heat shock 70 kDa proteins (HSP70), heat shock protein HSP 90 proteins (HSP90), immunoglobulin gamma-1 heavy chain (IGHG1, P01857), immunoglobulin heavy constant gamma 2 (IGHG2, P01859), immunoglobulin heavy constant gamma 3 (IGHG3, P01860), immunoglobulin heavy constant gamma 4 (IGHG4, P01861); myeloblastin/ proteinase 3 (PRTN3, P24158), myeloperoxidase (MPO, P05164), neutrophil elastase (ELANE, P08246), lysosome-associated membrane glycoprotein 2 (LAMP2, P13473), collagen alpha-3(IV) chain (COL4A3, Q01955), secretory phospholipase A2 receptor (PLA2R1, Q13018), thrombospondin type-1 domain-containing protein 7A (THSD7A, Q9UPZ6); histone H3-like centromeric protein A/ CENP-A (CENPA, P49450), major centromere autoantigen B/ CENP-B (CENPB, P07199), centromere protein C/ CENP-C (CENPC, Q03188), DNA topoisomerase 1/ Scl-70 (TOP1, P11387), exosome complex component RRP45/ PM/Scl- 75 (EXOSC9, Q06265), exosome component 10/ PM/Scl-100 (EXOSC10, Q01780), DNA- directed RNA polymerase III subunit RPC1 (POLR3A, O14802), DNA-directed RNA polymerase III subunit RPC2 (POLR3B, Q9NW08), DNA-directed RNA polymerase III subunit RPC3 (POLR3C, POLR3C), DNA-directed RNA polymerase III subunit RPC4 (POLR3D, P05423), DNA-directed RNA polymerase III subunit RPC5 (POLR3E, Q9NVU0), DNA-directed RNA polymerase III subunit RPC6 (POLR3F, Q9H1D9), DNA-directed RNA polymerase III subunit RPC7 (POLR3G, O15318), DNA-directed RNA polymerase III subunit RPC8 (POLR3H, Q9Y535), DNA-directed RNA polymerase III subunit RPC9 (CRCP, O75575), DNA-directed RNA polymerase III subunit RPC10 (POLR3K, Q9Y2Y1), DNA-directed RNA polymerases I and III subunit RPAC1 (POLR1C, O15160), DNA-directed RNA polymerases I and III subunit RPAC2 (POLR1D, P0DPB6), DNA-directed RNA polymerases I, II, and III subunit RPABC1 (POLR2E, P19388), DNA-directed RNA polymerases I, II, and III subunit RPABC2 (POLR2F, P61218), DNA-directed RNA polymerases I, II, and III subunit RPABC3 (POLR2H, P52434), DNA-directed RNA polymerases I, II, and III subunit RPABC4 (POLR2K, P53803), DNA- directed RNA polymerases I, II, and III subunit RPABC5 (POLR2L, P62875), RNA Binding Region Containing 3/ RNPC3 (RNPC3, Q96LT9), ribonuclease P protein subunit p25/ Th/To antigen (RPP25, Q9BUL9), translation initiation factor eIF-2B subunit alpha (EIF2B1, Q14232), Attorney Docket No: 44807-0422WO1 translation initiation factor eIF-2B subunit beta (EIF2B2, P49770), translation initiation factor eIF- 2B subunit gamma (EIF2B3, Q9NR50), translation initiation factor eIF-2B subunit delta (EIF2B4, Q9UI10), translation initiation factor eIF-2B subunit epsilon (EIF2B5, Q13144), gamma- interferon-inducible protein 16 (IFI16, Q16666), protein bicaudal D homolog 2 (BICD2, Q8TD16), fibrillin-1 (FBN1, P35555), rRNA 2'-O-methyltransferase fibrillarin/ fibrillarin 34 kDa (FBL, P22087), X-ray repair cross-complementing protein 6/ 70 kDa subunit of Ku antigen (XRCC6, P12956), X-ray repair cross-complementing protein 5/ 86 kDa subunit of Ku antigen (XRCC5, P13010); interferon-induced helicase C domain-containing protein 1/ melanoma differentiation-associated protein 5 (IFIH1, Q9BYX4), chromodomain-helicase-DNA-binding protein 4/ Mi-2 antigen (CHD4, Q14839), chromodomain-helicase-DNA-binding protein 3/ Mi-2 antigen (CHD3, Q12873), histidine--tRNA ligase, cytoplasmic/ Jo-1 antigen (HARS1, P12081), histidine--tRNA ligase, mitochondrial (HARS2, P49590), threonine--tRNA ligase 1, cytoplasmic/ PL-7 antigen (TARS1, P26639), threonine--tRNA ligase, mitochondrial (TARS2, Q9BW92), threonine--tRNA ligase 2, cytoplasmic (TARS3, A2RTX5), alanine--tRNA ligase, cytoplasmic/ PL-12 antigen (AARS1, P49588), alanine--tRNA ligase, mitochondrial (AARS2, Q5JTZ9), glycine--tRNA ligase/ EJ antigen (GARS1, P41250), isoleucine--tRNA ligase, cytoplasmic/ OJ antigen (IARS1, P41252), isoleucine--tRNA ligase, mitochondrial (IARS2, Q9NSE4), asparagine- -tRNA ligase, cytoplasmic/ KS antigen (NARS1, O43776), probable asparagine--tRNA ligase, mitochondrial (NARS2, Q96I59), phenylalanine--tRNA ligase alpha subunit/ ZO antigen (FARSA, Q9Y285), phenylalanine--tRNA ligase beta subunit (FARSB, Q9NSD9), phenylalanine- -tRNA ligase, mitochondrial (FARS2, O95363), tyrosine--tRNA ligase, cytoplasmic/ HA antigen (YARS1, P54577), tyrosine--tRNA ligase, mitochondrial (YARS2, Q9Y2Z4), 3-hydroxy-3- methylglutaryl-coenzyme A reductase (HMGCR, P04035), signal recognition particle subunit SRP72 (SRP72, O76094), signal recognition particle subunit SRP68 (SRP68, Q9UHB9), signal recognition particle 54 kDa protein (SRP54, P61011), signal recognition particle 14 kDa protein (SRP14, P37108), signal recognition particle 19 kDa protein (SRP19, SRP19), signal recognition particle 9 kDa protein (SRP9, P49458), E3 ubiquitin-protein ligase TRIM33/ Transcription intermediary factor 1-gamma (TRIM33, Q9UPN9), MORC family CW-type zinc finger protein 3/ nuclear matrix protein 2 (MORC3, Q14149), SUMO-activating enzyme subunit 1/ SAE antigen (SAE1, Q9UBE0), SUMO-activating enzyme subunit 2/ SAE antigen (UBA2, Q9UBT2), cytosolic 5'-nucleotidase 1A (NT5C1A, Q9BXI3), cell division cycle and apoptosis regulator Attorney Docket No: 44807-0422WO1 protein 1 (CCAR1, Q8IX12), transcription factor SOX-5 (SOX5, P35711); E3 ubiquitin-protein ligase TRIM21/ Ro-52 kDa (TRIM21, P19474), RNA-binding protein RO60/ Ro-60 kDa (RO60, P10155), E3 ubiquitin-protein ligase TRIM68 (TRIM68, Q6AZZ1), Lupus La protein/ La (SSB, P05455); double-stranded DNA (dsDNA), single-stranded DNA (ssDNA), messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA), or their protein complexes; small nuclear ribonucleoprotein Sm D1 (SNRPD1, P62314), small nuclear ribonucleoprotein Sm D2 (SNRPD2, P62316), small nuclear ribonucleoprotein Sm D3 (SNRPD3, P62318); small nuclear ribonucleoprotein Sm E (SNRPE, P62304), small nuclear ribonucleoprotein Sm F (SNRPF, P62306), small nuclear ribonucleoprotein Sm G (SNRPG, P62308), small nuclear ribonucleoprotein-associated proteins B and B' (SNRPB, P14678), small nuclear ribonucleoprotein-associated protein N/ Sm-N (SNRPN, P63162), U1 small nuclear ribonucleoprotein 70 kDa (SNRNP70, P08621), U1 small nuclear ribonucleoprotein C (SNRPC, P09234), U1 small nuclear ribonucleoprotein A (SNRPA, P09012), U2 small nuclear ribonucleoprotein A' (SNRPA1, P09661), U2 small nuclear ribonucleoprotein B'' (SNRPB2, P08579), 60S acidic ribosomal protein P0 (RPLP0, P05388), 60S acidic ribosomal protein P1 (RPLP1, P05386), 60S acidic ribosomal protein P2 (RPLP2, P05387), plasma protease C1 inhibitor (SERPING1, P05155), complement C1q subcomponent subunit A (C1QA, P02745), complement C1q subcomponent subunit B (C1QB, P02746), complement C1q subcomponent subunit C (C1QC, P02747), glycosylphosphatidylinositol-anchored high density lipoprotein- binding protein 1 (GPIHBP1, Q8IV16); a disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAMTS13, Q76LX8), complement factor H (CFH, P08603), complement factor I (CFI, P05156), von Willebrand factor (VWF, P04275), coagulation factor VIII (F8, P00451), integrin alpha-IIb (GPIIb) (ITGA2B, P08514), integrin beta-3 (GPIIIa) (ITGB3, P05106), platelet glycoprotein Ib alpha chain (GPIb) (GP1BA, P07359), platelet glycoprotein Ib beta chain (GP1BB, P13224), platelet glycoprotein IX (GP9, P14770), integrin alpha-2 (ITGA2, P17301), integrin beta-1 (ITGB1, P05556), platelet glycoprotein 4 (CD36, P16671), platelet glycoprotein V (GP5, P40197), P-selectin (SELP, Q14242), platelet factor 4 (PF4, P02776); aquaporin-4 M1 (AQP4, P55087), aquaporin-4 M23 (AQP4, P55087), aquaporin-4 orthogonal arrays, myelin proteolipid protein (PLP1, P60201), myelin-oligodendrocyte glycoprotein (MOG, Q16653), myelin basic protein (MBP, P02686), myelin-associated oligodendrocyte basic protein (MOBP, Q13875), myelin-associated glycoprotein (MAG, P20916), alpha-crystallin B chain (CRYAB, P02511), Attorney Docket No: 44807-0422WO1 glial fibrillary acidic protein (GFAP, P14136), claudin-11 (Claudin-11, O75508), endoplasmic reticulum chaperone BiP (HSPA5, P11021); acetylcholine receptor subunit alpha (CHRNA1, P02708), acetylcholine receptor subunit beta (CHRNB1, P11230), acetylcholine receptor subunit gamma (CHRNG, P07510), acetylcholine receptor subunit delta (CHRND, Q07001), acetylcholine receptor subunit epsilon (CHRNE, Q04844), muscle skeletal receptor tyrosine- protein kinase (MUSK, O15146), low-density lipoprotein receptor-related protein 4 (LRP4, O75096), agrin (AGRN, O00468), acetylcholinesterase collagenic tail peptide (COLQ, Q9Y215), α-subunit of the voltage-gated potassium channel Kv1.4, titin (TTN, Q8WZ42), ryanodine receptor 1 (RYR1, P21817), ryanodine receptor 2 (RYR2, Q92736), ryanodine receptor 3 (RYR3, Q15413), A-kinase anchor protein 12 (AKAP12, Q02952); glutamate receptor ionotropic, NMDA 1/ GluN1 (GRIN1, Q05586), glutamate receptor ionotropic, NMDA 2A/ GluN2A (GRIN2A, Q12879), glutamate receptor ionotropic, NMDA 2B/ GluN2B (GRIN2B, Q13224), glutamate receptor ionotropic, NMDA 2C/ GluN2C (GRIN2C, Q14957), glutamate receptor ionotropic, NMDA 2D/ GluN2D (GRIN2D, O15399), cerebellar degeneration-related protein 2/ Yo antigen (CDR2, Q01850), ELAV-like protein 1 (ELAV-like protein 1, Q15717), ELAV-like protein 2 (ELAVL2, Q12926), ELAV-like protein 3 (ELAVL3, Q14576), ELAV-like protein 4 (ELAVL4, P26378), leucine-rich glioma-inactivated protein 1 (LGI1, O95970), contactin-associated protein- like 2/ CASPR2 (CNTNAP2, Q9UHC6), contactin-2 (CNTN2, Q02246), dihydropyrimidinase- related protein 5/ CRMP5 (DPYSL5, Q9BPU6), glutamate receptor 1/ GluA1 (GRIA1, P42261), glutamate receptor 2/ GluA2 (GRIA2, P42262), glutamate receptor 3/ GluA3 (GRIA3, P42263), glutamate receptor 4/ GluA4 (GRIA4, P48058), gamma-aminobutyric acid receptor subunit alpha- 1 (GABRA1, P14867), gamma-aminobutyric acid receptor subunit beta-3 (GABRB3, P28472), gamma-aminobutyric acid type B receptor subunit 1 (GABBR1, Q9UBS5), gamma-aminobutyric acid type B receptor subunit 2 (GABBR2, O75899), gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2, P18507), metabotropic glutamate receptor 1 (GRM1, Q13255), metabotropic glutamate receptor 5 (GRM5, P41594), amphiphysin (AMPH, P49418), adenylate kinase isoenzyme 5 / AK5 (AK5, AK5), dipeptidyl aminopeptidase-like protein 6 (DPP6, P42658), delta and Notch-like epidermal growth factor-related receptor (DNER, Q8NFT8), neurexin-3 (NRXN3, Q9Y4C0), RNA-binding protein Nova-1/ Ri antigen (NOVA1, P51513), paraneoplastic antigen Ma1 (PNMA1, Q8ND90), paraneoplastic antigen Ma2 (PNMA2, Q9UL42), paraneoplastic antigen Ma3 (PNMA3, Q9UL41), modulator of apoptosis 1/ Ma4 (MOAP1, Attorney Docket No: 44807-0422WO1 Q96BY2), microtubule-associated protein 1B (MAP1B, P46821), dihydropyrimidinase-related protein 1 (CRMP1, Q14194); ganglioside GM1, ganglioside GM1b, ganglioside GD1a, ganglioside GD1b, ganglioside GQ1b, ganglioside GT1a; protein-glutamine gamma- glutamyltransferase 2 (TGM2, P21980), protein-glutamine gamma-glutamyltransferase E (TGM3, Q08188), protein-glutamine gamma-glutamyltransferase 6 (TGM6, O95932); thyroid peroxidase (TPO, P07202), thyrotropin receptor (TSHR, P16473), thyroglobulin (TG, P01266); islet cell autoantigen 1 (ICA1, Q05084); islet cell autoantigen 1-like protein (ICA1L, Q8NDH6); glutamate decarboxylase 1 (GAD1, Q99259), glutamate decarboxylase 2 (GAD-65) (GAD2, Q05329); receptor-type tyrosine-protein phosphatase-like N / IA2 (PTPRN, Q16849); receptor-type tyrosine-protein phosphatase N2/ IAR (PTPRN2, Q92932), zinc transporter 8 (SLC30A8, Q8IWU4); steroid 21-hydroxylase (CYP21A2, P08686), steroid 17-alpha-hydroxylase/17,20 lyase (CYP17A1, P05093), 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 (HSD3B2, P26439), adrenocorticotropic hormone receptor (MC2R, Q01718), NACHT, LRR and PYD domains-containing protein 5 (NLRP5, P59047), testis-specific gene 10 protein (TSGA10, Q9BZW7), hyaluronidase PH-20 (SPAM1, P38567), disintegrin and metalloproteinase domain- containing protein 2 (ADAM2, Q99965), follicle-stimulating hormone receptor (FSHR, P23945), follitropin subunit beta (FSHB, P01225), glycoprotein hormones alpha chain (CGA, P01215), lutropin-choriogonadotropic hormone receptor (LHCGR, P22888), lutropin subunit beta (LHB, P01229); cholesterol side-chain cleavage enzyme, mitochondrial (CYP11A1, P05108); cobalamin binding intrinsic factor (CBLIF, P27352), potassium-transporting ATPase alpha chain 1 (ATP4A, P20648), potassium-transporting ATPase subunit beta (ATP4B, P51164); desmoglein-1 (DSG1, Q02413), desmoglein-3 (DSG3, P32926), collagen alpha-1(XVII) chain/ 180 kDa bullous pemphigoid antigen (COL17A1, Q9UMD9), dystonin/ 230 kDa bullous pemphigoid antigen (DST, Q03001), collagen alpha-1(VII) chain (COL7A1, Q02388), envoplakin (EVPL, Q92817), epiplakin (EPPK1, P58107), periplakin (PPL, O60437), plectin (PLEC, Q15149), desmoplakin (DSP, P15924), desmocollin-1 (DSC1, Q08554), laminin gamma-1, laminin 5, laminin 6, ladinin- 1 (LAD1, O00515), integrin alpha-4 (ITGA4, P13612), integrin beta-6 (ITGB6, P18564), neuronal acetylcholine receptor subunit alpha-9 (CHRNA9, Q9UGM1); tumor necrosis factor (TNF, P01375), lymphotoxin-alpha (LTA, P01374), granulocyte-macrophage colony-stimulating factor (CSF2, P04141), granulocyte colony-stimulating factor (CSF3, P09919), interleukin-1 alpha (IL1A, P01583), interleukin-1 beta (IL1B, P01584), interleukin-6 (IL6, P05231), interleukin-17A Attorney Docket No: 44807-0422WO1 (IL17A, Q16552), interleukin-17F (IL17F, Q96PD4), interferon alpha-1/13 (IFNA1, P01562), interferon alpha-2 (IFNA2, P01563), interferon alpha-4 (IFNA4, P05014), interferon alpha-5 (IFNA5, P01569), interferon alpha-6 (IFNA6, P05013), interferon alpha-7 (IFNA7, P01567), interferon alpha-8 (IFNA8, P32881), interferon alpha-10 (IFNA10, P01566), interferon alpha-14 (IFNA14, P01570), interferon alpha-16 (IFNA16, P48551), interferon alpha-17 (IFNA17, P01571), interferon alpha-21 (IFNA21, P01568), interferon omega-1 (IFNW1, P05000), interferon kappa (IFNK, Q9P0W0), interferon lambda-1 (IFNL1, Q8IU54), interferon lambda-2 (IFNL2, Q8IZJ0), interferon lambda-3 (IFNL3, Q8IZI9), interferon lambda-4 (IFNL4, K9M1U5), interferon gamma (IFNG, P01579); cytochrome P450 2D6/ LKM-1 (CYP2D6, P10635), cytochrome P450 2C9 (CYP2C9, P11712), cytochrome P450 2A6 (CYP2A6, P11509), UDP- glucuronosyltransferase 1A (UGT1A1, P22309), cytochrome P450 1A2 (CYP1A2, P05177), formimidoyltransferase-cyclodeaminase (FTCD, O95954), dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial/ PDC-E2 (DLAT, P10515), dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial/ OGDC-E2 (DLST, P36957), lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial/ BCOADC- E2 (DBT, P11182), pyruvate dehydrogenase complex protein X component, mitochondrial (PDX1, P16451), dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (DLAT, P10515), nuclear autoantigen Sp-100 (SP100, P23497), coilin (COIL, P38432), nuclear pore membrane glycoprotein 210 (NUP210, Q8TEM1), lamin-B receptor (LBR, Q8MLV1), nuclear pore glycoprotein p62 (NUP62, P37198), or o- phosphoseryl-tRNA(Sec) selenium transferase (SEPSECS, Q9HD40). In some embodiments, the TCR or CD3 fusion protein can comprise a linker and/or hinge sequence. In some embodiments, the linker and/or hinge sequence can include a sequence from SEQ ID NOs: 58-73 (Table 5). In some embodiments, the TCR or CD3 fusion protein can comprise a terminator sequence. In some embodiments, the terminator sequence can include a sequence from SEQ ID NOs: 74-76 (Table 6). In some embodiments, the TCR or CD3 fusion protein sequences can comprise an exogenous promoter sequence. In some embodiments, the exogenous promoter sequence can include a sequence from SEQ ID NOs: 77-81 (Table 7). In some embodiments, the CATCR can comprise an intracellular/co-stimulatory domain or a signaling/ signal transducer domain. In some embodiments, the intracellular/co-stimulatory domain can include a sequence from SEQ ID NOs: Attorney Docket No: 44807-0422WO1 82-170 (Table 8). In some embodiments, the signaling/ signal transducer domain includes a sequence from ZAP70 [P43403], LCK [P06239], FYN [P06241], PLCG1 [P19174], LCP2 [Q13094]. [Table 3] Examples of self-cleaving peptides SEQ ID  UniProt ID   Name  Amino Acid Sequence (unless specified otherwise)  NO.  4_{5    Furin/ P2A peptide}  ^{RAKRSGSGATNFSLLKQAGDVEENPGP [SEQ ID NO. 45]} SEQ  UniProt ID   Name  Amino Acid Sequence (unless specified otherwise)  ID  NO.  SEQ  UniProt ID   Name  Amino Acid Sequence (unless specified otherwise)  ID  ] E ] S Attorney Docket No: 44807-0422WO1 SEQ    Name  Nucleotide Sequence  ID  NO.  AC AC CA TC GT CA AG TG TG GC CC GG TG SEQ    Name  Nucleotide Sequence  ID  NO A C C C G C C A A G T G T A G G C T T G C G C G G C A C G T A Attorney Docket No: 44807-0422WO1 CATGACCTTATGGGACTTTCCTACTTGGCAGTACATCTACGTATTAGTCATCGCTATTACCAT GGTGATGCGGTTTTGGCAGTACATCAATGGGCGTGGATAGCGGTTTGACTCACGGGGATTTCC AAGTCTCCACCCCATTGACGTCAATGGGAGTTTGTTTTGGCACCAAAATCAACGGGACTTTCC AAAATGTCGTAACAACTCCGCCCCATTGACGCAAATGGGCGGTAGGCGTGTACGGTGGGAGGT G T G C T C A A T C A C C C T C A A r CARs SEQ  UniProt ID   Name  Amino Acids  ID  NO Attorney Docket No: 44807-0422WO1 P_{40259  CD79b ITAM}  ^185-213 Q_{9UIB8  CD84}  ^247-345 P_{01732  CD8A_HUMAN}  ^204-235 Attorney Docket No: 44807-0422WO1 1_{67  Q9Y2C9  TLR6}  ^608-796 1_{68  Q9NYK1  TLR7}  ^861-1049 1_{69  Q9NR97  TLR8}  ^849-1031 or domain derived from an autoantigen, part of an autoantigen, the entire autoantigen, or the autoantigen in complex with another molecule. In some embodiments, the autoantigenic peptide is derived from a phospholipid-binding protein. In some embodiments, the phospholipid binding protein is beta-2 glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), or prothrombin (PT), or their mammalian analogs. In some embodiments, the autoantigenic peptide comprises one or at least part of one domain of β2GPI, including domain I (DI), domain II (DII), domain III (DIII), domain IV (DIV), or domain V (DV). In some embodiments, the autoantigenic peptide comprises a combination of domain I (DI) with other domains of β2GPI, including – but not limited to – β2GPI DI-DII, β2GPI DI-DIII, β2GPI DI-DIV, or β2GPI DI-DV. In some embodiments, the autoantigenic peptide comprises two consecutive domains of β2GPI (or parts thereof), including β2GPI DI-DII, β2GPI DII-DIII, β2GPI DIII-DIV, or β2GPI DIV-DV. In some embodiments, the autoantigenic peptide comprises three consecutive domains of β2GPI (or parts thereof), including β2GPI DI-DIII, β2GPI DII-DIV, or β2GPI DIII-DV. In some embodiments, the autoantigenic peptide comprises four consecutive domains of β2GPI (or parts thereof), including β2GPI DI-DIV or β2GPI DII-DV. In some embodiments, the autoantigenic peptide comprises domains of β2GPI (or parts thereof) that are mutated to increase binding specificity. In some embodiments, the autoantigenic peptide comprises any combination of the domains of β2GPI or their parts. In some embodiments, the autoantigenic peptide comprises the epitope R39-R43 “Arg Gly Gly Met Arg”, either in isolation or embedded in another protein sequence. In some embodiments, the autoantigenic peptide comprises a bacterial or viral mimotope of this epitope. In some embodiments, the autoantigenic peptide comprises at least part of the endothelial protein C receptor (EPCR). In some embodiments, the autoantigenic peptide comprises the extracellular (EC) domains of EPCR. In some embodiments, the extracellular domain of EPCR has been modified by introduction of a Flag tag or other protein tag sequence. In some embodiments, EPCR has been complexed/ “loaded” with its associated phospholipid LBPA to produce a phospholipid-binding protein/phospholipid complex. Attorney Docket No: 44807-0422WO1 In some embodiments, the autoantigenic peptide comprises at least part of prothrombin (PT). In some embodiments, the autoantigenic peptide comprises prothrombin (PT) expressed in the presence of its natural propeptide and vitamin K to facilitate processing and modification. In some embodiments, the autoantigenic peptide comprises partial sequences of β2GPI, EPCR, and/or PT. In some embodiments, the autoantigenic peptide is expressed as part of a modified second or higher generation chimeric antigen receptor (CAR) construct, wherein the CAR construct comprises a hinge and/or linker domain (e.g., CD8, CD28, IgG1, IgG4), a transmembrane domain (e.g., CD8α, CD3ζ, CD4, CD28), at least one intracellular co-stimulatory or immunomodulatory domain (e.g., full or partial sequences of CD28, 4-1BB, OX40, ICOS, MYD88, 2B4, BTLA, CD2, CD22, CD27, CD30, CD3d, CD3e, CD3g, CD3z, CD4, CD40, CD79a, CD79b, CD84, CD8a, CD8b, CRACC, CRTAM, CTLA-4, DAP10, DNAM-1, DAP12, DR3, FCER1G, FCGR1A, FCGR2A, FCGR2B, FCGR3A, FCRL1, FCRL2, FCRL3, FCRL4, FCRL5, FCRL6, GITR, HVEM, ITAM, KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR3DL1, KIR3DL2, KIR3DL3, LAG3, LAT, LILRB1, LILRB2, Ly9, NKG2A, NKG2C, NKG2D, NKp30, NKp44, NKp46, PD-1, PILRB, SIRPa, SLAMF1, SLAMF6, SLAMF7, TIGIT, TIM1, TIM3, TNFL6, TLR1, TLR10, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, or their combination), and at least one intracellular signaling/ signal transducer domain (e.g., CD3ζ, ZAP70, LCK, FYN, PLCG1, LCP2) in addition to the extracellular autoantigenic peptide(s). In some embodiments, the CAR construct can include a sequence from SEQ ID NOs: 29, 68, 83, 88, 171-177 (Table 9). [Table 9] Examples of CAR domains SEQ  UniProt ID   Name  Amino Acid Sequence (unless specified otherwise)  ID  G G C G C C A Attorney Docket No: 44807-0422WO1 CCGGCGCCCACCATCGCGTCGCAGCCCCTGTCCCTGCGCCCAGAGGCGTGCCGGCCAGCGGCG GGGGGCGCAGTGCACACGAGGGGGCTGGACTTCGCCTGTGATATCTACATCTGGGCGCCCTTG GCCGGGACTTGTGGGGTCCTTCTCCTGTCACTGGTTATCACCCTTTACTGCAACCACAGGAAC CGAAGACGTGTTTGCAAATGTCCCCGGCCTGTGGTCAAATCGGGAGACAAGCCCAGCCTTTCG ] T T G C C G C G T C A T C A T C T A C C A A Attorney Docket No: 44807-0422WO1 177  P20963  CD3Z_HUMAN   LCYLLDGILFIYGVILTALFL [SEQ ID NO. 177] Transmembrane  Domain  ple, immune cells (e.g., T cells) can be differentiated in vitro from a hematopoietic stem cell population, or immune cells (e.g., T cells) can be obtained from a subject (e.g., from the patient as an autologous source or from another subject as an allogeneic source). T cells or other immune cells can be obtained from peripheral whole blood, peripheral blood mononuclear cells (PBMCs), bone marrow, cord blood, lymph nodes, spleen, thymus, ascites, pleural effusion, target tissues of the autoimmune response, or tumors. In addition, immune cells (e.g., T cells) can be derived from one or more immune cell lines available in the art. In addition, immune cells (e.g., T cells) can be engineered to generate universal donor cells for CATCR expression. In some embodiments, T cells can be obtained from blood collected from a subject using any number of techniques known to the skilled artisan, such as FICOLL™ separation, negative or positive cell selection using magnetic or other beads, and/or apheresis. Additional methods of isolating T cells for a T cell therapy are disclosed in U.S. Patent Publication No.2013/0287748, which is incorporated by reference in its entirety. Other non-limiting examples can be found in International Application No. PCT/US2015/014520 (published as WO2015/120096) and in International Application No. PCT/US2016/057983 (published as WO2017/070395), each of which is herein incorporated by reference in its entirety. Phospholipid Binding Proteins and Antiphospholipid Antibody Syndrome (APS) Phospholipid-binding proteins are proteins that form complexes with phospholipids and play a regulatory function in controlling biological functions. Examples of phospholipid-binding proteins can include, but are not limited to, beta-2-glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), prothrombin (PT), annexin V, and annexin II. Antiphospholipid antibody syndrome (APS) is a multisystem autoimmune disease associated with disease-causing autoantibodies directed against phospholipid-binding proteins and their complexes with specific phospholipids. Immunologically, APS is characterized by loss of B cell tolerance against self and the emergence of autoantibodies. In some embodiments, Attorney Docket No: 44807-0422WO1 autoantibody systems that target phospholipid-binding protein/phospholipid complexes can be referred to as antiphospholipid antibodies. In some embodiments, these antiphosphoplipid antibodies can include (i) anti-beta-2-glycoprotein I [β2GPI]/ cardiolipin [CL], (ii) anti-endothelial protein C receptor [EPCR]/ lysobisphosphatidic acid [LBPA], and (iii) anti-prothrombin [PT]/ phosphatidylserine [PS]. In some embodiments, these autoantibodies can be directly pathogenic in vitro and in vivo. Therefore, strategies that eliminate the sources of these antibodies (e.g., B cells and plasma cells) may be used to prevent or cure APS. Autoreactive B cells and plasma cells that express surface B cell receptors (BCRs) specific for phospholipid-binding proteins are therefore ideal therapeutic targets for antigen-specific depletion strategies. Nucleic Acids Provided herein are nucleic acids encoding a recombinant CATCR that includes (a) an extracellular binding domain comprising an autoantigenic peptide (or complex containing the latter), wherein the autoantigenic peptide (or complex containing the latter) is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 complex protein. In some embodiments, the recombinant CATCR includes at least one (a) autoantigenic epitope, peptide, or protein recognized by a B cell receptor (BCR) and at least one (b) native or modified peptide of a T cell receptor-CD3 complex protein (e.g., a T cell receptor alpha chain, beta chain, gamma chain, delta chain, a CD3 gamma subunit, a CD3 delta subunit, or a CD3 epsilon subunit, or any part thereof); CATCRs may include (c) linker/ hinge peptide(s) or sequence(s) and (d) additional intracellular domains (e.g., co-stimulatory domains, immune regulatory domains). As used herein, “nucleic acid” is used to include any compound and/or substance that comprise a polymer of nucleotides. In some embodiments, a polymer of nucleotides is referred to as polynucleotides. Exemplary nucleic acids or polynucleotides can include, but are not limited to, ribonucleic acids (RNAs) and/or deoxyribonucleic acids (DNAs). In some embodiments, nucleic acid constructs include regions that encode a CATCR. In some embodiments, the CATCR comprises an engineered T-cell receptor (TCR)-CD3 protein complex. In some embodiments, the autoantigenic peptides of the CATCR is derived from a phospholipid-binding protein. In some embodiments, the phospholipid binding protein is beta-2 glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), or prothrombin (PT). In some Attorney Docket No: 44807-0422WO1 embodiments, the autoantigenic peptides are derived from any other autoantigen that is targeted by disease-causing autoantibodies/ B cells in a systemic or organ-specific autoimmune disease. In some embodiments, the autoantigenic peptides are expressed as part of a CD3 gamma (CD3 ^) chain; a CD3 epsilon (CD3ε) chain; a CD3 delta (CD3δ) chain; a T cell receptor (TCR) alpha chain; or a T cell receptor (TCR) beta chain, a T cell receptor (TCR) gamma chain, a T cell receptor (TCR) delta chain of the CATCR. In some embodiments, the autoantigenic peptide encodes for a phospholipid-binding protein. In some embodiments, the phospholipid binding protein is beta-2 glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), or prothrombin (PT), or their mammalian analogs. In some embodiments, the autoantigenic peptide encodes for one or at least part of one domain of β2GPI, including domain I (DI), domain II (DII), domain III (DIII), domain IV (DIV), or domain V (DV). In some embodiments, the autoantigenic peptide encodes for a combination of domain I (DI) with other domains of β2GPI, including – but not limited to – β2GPI DI-DII, β2GPI DI-DIII, β2GPI DI-DIV, or β2GPI DI-DV. In some embodiments, the autoantigenic peptide encodes for two consecutive domains of β2GPI (or parts thereof), including β2GPI DI-DII, β2GPI DII-DIII, β2GPI DIII-DIV, or β2GPI DIV-DV. In some embodiments, the autoantigenic peptide encodes for three consecutive domains of β2GPI (or parts thereof), including β2GPI DI-DIII, β2GPI DII-DIV, or β2GPI DIII-DV. In some embodiments, the autoantigenic peptide encodes for consecutive domains of β2GPI (or parts thereof), including β2GPI DI-DIV or β2GPI DII-DV. In some embodiments, the autoantigenic peptide encodes for β2GPI (or parts thereof) that are mutated to increase binding specificity. In some embodiments, the autoantigenic peptide encodes for any combination of the domains of β2GPI or their parts. In some embodiments, the autoantigenic peptide encodes for the epitope R39-R43 “Arg Gly Gly Met Arg”, either in isolation or embedded in another protein sequence. In some embodiments, the autoantigenic peptide encodes for a bacterial or viral mimotope of this epitope. In some embodiments, the autoantigenic peptide encodes for at least part of the endothelial protein C receptor (EPCR). In some embodiments, the autoantigenic peptide encodes for the extracellular (EC) domains of EPCR. In some embodiments, the autoantigenic peptide encodes for at least part of a prothrombin (PT), with or without its natural propeptide. In some embodiments, the autoantigenic peptide encodes for partial sequences of β2GPI, EPCR, and/or PT in any combination. Attorney Docket No: 44807-0422WO1 In some embodiments, the autoantigenic peptide is expressed as part of a modified second or higher generation chimeric antigen receptor (CAR) construct, wherein the CAR construct comprises a hinge and/or linker domain (e.g., CD8, CD28, IgG1, IgG4), a transmembrane domain (e.g., CD8α, CD3ζ, CD4, CD28), at least one intracellular co-stimulatory or immunomodulatory domain (e.g., full or partial sequences of CD28, 4-1BB, OX40, ICOS, MYD88, 2B4, BTLA, CD2, CD22, CD27, CD30, CD3d, CD3e, CD3g, CD3z, CD4, CD40, CD79a, CD79b, CD84, CD8a, CD8b, CRACC, CRTAM, CTLA-4, DAP10, DNAM-1, DAP12, DR3, FCER1G, FCGR1A, FCGR2A, FCGR2B, FCGR3A, FCRL1, FCRL2, FCRL3, FCRL4, FCRL5, FCRL6, GITR, HVEM, ITAM, KIR2DL1, KIR2DL2, KIR2DL3, KIR2DL4, KIR2DL5A, KIR2DL5B, KIR3DL1, KIR3DL2, KIR3DL3, LAG3, LAT, LILRB1, LILRB2, Ly9, NKG2A, NKG2C, NKG2D, NKp30, NKp44, NKp46, PD-1, PILRB, SIRPa, SLAMF1, SLAMF6, SLAMF7, TIGIT, TIM1, TIM3, TNFL6, TLR1, TLR10, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, or their combination), and at least one intracellular signaling/ signal transducer domain (e.g., CD3ζ, ZAP70, LCK, FYN, PLCG1, LCP2) in addition to the extracellular autoantigenic peptide(s). In some embodiments, nucleic acid constructs may be inserted into an expression vector or viral vector by methods known to the art, and nucleic acid molecules may be operably linked to an expression control sequence. Non-limiting examples of expression vectors include plasmid vectors, transposon vectors, cosmid vectors, and viral vectors (e.g., any lentiviral vectors, adenoviral vectors (AV), adeno-associated virus (AAV), cytomegaloviral (CMV) vectors, simian viral (SV40) vectors, and retroviral vectors). In some embodiments, the expression vector is a viral vector. In some embodiments, nucleic acid molecules are inserted into a vector that is able to express a CATCR of the present disclosure when introduced into an appropriate cell. In some embodiments, an appropriate cell is a T cell. Additional sequences can be added to such cloning and/or expression sequences to optimize their function in cloning and/or expression, to aid in isolation of the polynucleotide, or to improve the introduction of the polynucleotide into a cell. Use of cloning vectors, expression vectors, adapters, and linkers is well known in the art. In some embodiments, mRNA nucleic acid sequences encoding for CATCRs may be generated by in-vitro transcription or de-novo RNA synthesis and introduced into immune cells by electroporation or transfection by methods known to the art. In these embodiments, mRNA Attorney Docket No: 44807-0422WO1 encoding CATCRs will be translated by the cell to produce CATCR fusion protein which will be expressed on the cell surface in the context of the TCR-CD3 complex. In some embodiments, nucleic acid sequences encoding for CATCRs will be permanently introduced into immune cells (e.g., T cells) by gene editing. In some embodiments, the nucleic acid sequence is introduced into the immune cell by using a gene-editing agent. In some embodiments, the gene-editing agent comprises CRISPR/Cas components. As used herein, the term “gene-editing agent” can refer to an agent that allows for changing the DNA or RNA (e.g., mRNA) in the genome. In some embodiments, gene-editing can include insertion, deletion, modification, or replacement of the DNA or RNA. In some embodiments, a gene-editing agent can include a nuclease-based gene editing platform. In some embodiments, a gene-editing agent can include zinc finger nucleases (ZFNs), transcription activator-like effector nucleases (TALENs), engineered meganucleases, or a clustered regularly interspaced short palindromic repeats (CRISPR) system. In some embodiments, a gene-editing agent can include RNA interference (e.g., short hairpin RNA (shRNA), small interfering RNA (siRNA), antisense oligonucleotide (ASO), or microRNA mimics). In some embodiments, the gene-editing agent can include CRISPR components. For example, in some embodiments, CRISPR components can include, but are not limited to, a guide RNA and a CRISPR-associated endonuclease (Cas protein). As used herein, a “CRISPR-associated endonuclease” or “CRISPR-associated protein” can refer to an enzyme or protein that uses CRISPR sequences as a guide to recognize and cleave specific nucleic acid strands that are complementary to the CRISPR sequence. In some embodiments, a gene-editing agent can include a CRISPR-associated protein. In some embodiments, the gene-editing agent can be a Cas9 endonuclease that makes a double-stranded break in a target DNA sequence. In some embodiments, the gene-editing agent can be a Cas12a nuclease that also makes a double-stranded break in a target DNA sequence. In some embodiments, the gene-editing agent can be a Cas13 nuclease which targets RNA. In some embodiments, the gene-editing agent can include a Cas9 or Cas12a protein. In some embodiments, gene editing will be performed using CRISPR/Cas nuclease- mediated homology directed repair using dsDNA homology directed repair template (HDRT) comprising the coding sequences of the CATCR and homology arms for the target gene locus of interest, ribonucleoprotein (RNP) complexes of Cas nuclease and matching sgRNA, and means of introducing them into the cell (e.g., electroporation, transduction, transfection). In some Attorney Docket No: 44807-0422WO1 embodiments, dsDNA or ssDNA HDRT will be generated by PCR-based amplification from a plasmid containing the relevant nucleic acid sequences. In some embodiments, nucleic acid sequences encoding for a CATCR will be introduced into the CD3G gene locus; CD3D locus; CD3E locus; TRAC locus, TRBC1 locus, TRBC2 locus, TRGC locus, TRDC locus, B2M locus, or other genetic loci using sgRNA for the targeted nucleotide sequence and Cas nuclease. In some embodiments, CRISPR will be performed using Cas9, Cpf1 (Cas12a), or other Cas nucleases. In some embodiments, other gene editing technologies may be used to the same end. Production of CATCR-engineered immune cells Provided herein are methods of producing an engineered immune cell comprising a chimeric autoantigen-T cell receptor (CATCR). In some embodiments, the immune cell where a CATCR is introduced therein is a human immune cell. In some embodiments, the immune cell is an autologous human immune cell. In some embodiments, the immune cell is an allogeneic human immune cell. In some embodiments, the immune cell is a T cell. In some embodiments, the immune cell is a αβ-T cell (a T cell expressing TCR alpha and beta chains), a γδ-T cell (a T cell expressing TCR gamma and delta chains), CD4⁺ T cell (helper T cell, T_H cell), a CD8⁺ T cell (cytotoxic T cell, CTL), CD3+CD4-CD8- double-negative (DN) T cell, a memory T cell, a regulatory T cell (Treg cell), but is not limited thereto. In some embodiments, the present disclosure provides methods of producing an engineered immune cell, comprising: introducing into an immune cell (i) nucleic acids encoding a CATCR, comprising a T cell receptor or a modified T cell receptor and an autoantigenic peptide recognized by a B cell receptor, or (ii) a vector comprising the nucleic acid encoding a CATCR, comprising a T cell receptor or a modified T cell receptor and an autoantigenic peptides recognized by a B cell receptor, or (iii) nucleic acids HDR template encoding a CATCR and homology arms and Cas RNP for introduction of CATCR coding sequences into desired parts of the human genome. Any method known in the art for expressing a CATCR in immune cells can be used in the context of the present disclosure. For example, there are various nucleic acid vectors for expression known in the art, such as linear polynucleotides, polynucleotides to which an ionic or amphiphilic compound is bound, plasmids, or viral vectors, though the present disclosure is not limited thereto. In some embodiments, a vector for expression of a CATCR in immune cells may be or include an autonomously replicating plasmid or virus or derivative thereof. Viral vectors Attorney Docket No: 44807-0422WO1 can include, but are not limited to adenovirus vector, adeno-associated viral vector, retrovirus vector, etc. In some embodiments, a lentivirus vector, which is a retroviral vector, can be used. In some embodiments, a vector is a non-plasmid and a non-viral compound, such as, for example, a liposome. In some embodiments, gene editing with CRISPR/Cas homology directed repair or other technologies may be used to introduce CATCR coding sequences. The present disclosure encompasses the recognition that engineered immune cells including a CATCR, generated by the methods described herein, may be therapeutically useful (e.g., for the treatment of various autoimmune diseases including antiphospholipid antibody syndrome). Therapeutic Applications Provided herein are methods of treating an autoimmune disease in a subject, wherein the method comprises administering to a subject a composition that comprises or delivers an engineered immune or other cell expressing at least one CATCR. An “autoimmune disease” is a disease that arises from an abnormal immune response to a functioning body part, wherein a body’s immune system attacks and damages its own normal healthy cells or tissues. In some embodiments, in response to an unknown or known trigger, the immune system may begin producing antibodies (e.g., autoantibodies) and self-antigen-directed immune cells that, instead of fighting infections or cancer, attack the body’s own tissues. Systemic or organ-specific autoimmune diseases suitable for treatment by a method of the present disclosure can include, but are not limited to Addison’s disease, (adult-onset) Still’s disease, alopecia areata/ autoimmune hair loss, antiphospholipid syndrome (APS), APS-related fetal loss, and catastrophic antiphospholipid syndrome (CAPS), autoimmune angioedema, autoimmune dysautonomia, autoimmune encephalitis (including anti-NMDAR encephalitis), autoimmune hepatitis, autoimmune inner ear disease, autoimmune myocarditis or pericarditis, autoimmune oophoritis, autoimmune orchitis, autoimmune pancreatitis, autoimmune paraneoplastic syndromes, autoimmune retinopathy, autoimmune urticaria, autoimmune uveitis, axonal & neuronal neuropathy (AMAN), Baló disease, Behcet’s disease, benign mucosal pemphigoid (mucous membrane pemphigoid), bullous pemphigoid, celiac disease, acute or chronic inflammatory demyelinating polyneuropathy, eosinophilic granulomatosis with polyangiitis (EGPA, formerly Churg-Strauss syndrome), cicatricial pemphigoid, Cogan’s syndrome, cold agglutinin disease, Attorney Docket No: 44807-0422WO1 autoantibody-mediated congenital heart block, CREST syndrome, Crohn’s disease, cryoglobulinemia/ cryoglobulinemic vasculitis, dermatitis herpetiformis, various subtypes of dermatomyositis, neuromyelitis optica (NMO) spectrum disorders, discoid and other forms of cutaneous lupus, Dressler’s syndrome, eosinophilic fasciitis and eosinophilic myositis, Evans syndrome, fibromyalgia, fibrosing alveolitis, giant cell arteritis (temporal arteritis), giant cell myocarditis, antibody-mediated forms of glomerulonephritis, Goodpasture’s syndrome (anti- glomerular basement membrane disease), granulomatosis with polyangiitis (GPA), Graves’ disease, Guillain-Barre syndrome, Hashimoto’s thyroiditis, hemolytic anemia, Henoch-Schönlein purpura (HSP), herpes gestationis or pemphigoid gestationis, hidradenitis suppurativa, IgA nephropathy and IgA vasculitis, IgG4-related disease, autoimmune interstitial lung disease, immune thrombocytopenic purpura (ITP), inclusion body myositis (IBM), various forms of juvenile idiopathic arthritis, type 1 diabetes mellitus, juvenile myositis, Kawasaki disease, Lambert-Eaton myasthenia syndrome, lichen planus, lichen sclerosus, ligneous conjunctivitis, systemic lupus erythematosus (SLE), lupus nephritis, and drug-induced lupus, Meniere’s disease, microscopic polyangiitis (MPA), mixed connective tissue disease (MCTD), multifocal motor neuropathy (MMN), multiple sclerosis, myasthenia gravis, myelin oligodendrocyte glycoprotein (MOG) antibody-related diseases, idiopathic inflammatory myopathies, immune-mediated necrotizing myopathies, antisynthetase syndrome, narcolepsy, neonatal lupus, autoimmune neutropenia, autoimmune lymphopenia, ocular cicatricial pemphigoid, optic neuritis, palindromic rheumatism, paraneoplastic cerebellar degeneration, pars planitis (peripheral uveitis), pemphigus vulgaris, pemphigus vulgaris foliaceous, IgA pemphigus, paraneoplastic pemphigus, autoimmune peripheral neuropathies, pernicious anemia, POEMS syndrome, polyarteritis nodosa, polymyalgia rheumatica, polymyositis, primary biliary cirrhosis, primary membranous nephropathy, primary sclerosing cholangitis, psoriasis, psoriatic arthritis, Raynaud’s phenomenon, reactive arthritis, relapsing polychondritis, retroperitoneal fibrosis, rheumatic fever, rheumatoid arthritis, sarcoidosis, scleritis, scleroderma/ limited cutaneous and diffuse cutaneous systemic sclerosis, Sjögren’s disease, Stiff person syndrome spectrum disorders, Susac’s syndrome, sympathetic ophthalmia, Takayasu's arteritis, thyroid eye disease, transverse myelitis, ulcerative colitis, vasculitis, vitiligo, Vogt-Koyanagi-Harada disease, or warm or cold autoimmune hemolytic anemia, and any autoantibody-mediated pathology. Attorney Docket No: 44807-0422WO1 An autoimmune rheumatic disease refers to a systemic disease characterized by an abnormal immune response to normal cells and tissues, wherein the abnormal immune response is often directed against multiple tissues and organ systems of the body, such as the joints, muscles, kidneys, lungs, the skin, and/or other connective tissue. Some examples of autoimmune rheumatic diseases can include, but are not limited to rheumatoid arthritis (RA), spondyloarthropathies (e.g., ankylosing spondylitis and psoriatic arthritis), juvenile idiopathic arthritis, systemic lupus erythematosus, Sjögren’s disease, scleroderma/ systemic sclerosis, idiopathic inflammatory myopathies (e.g., dermatomyositis, antisynthetase syndrome, immune-mediated necrotizing myopathies), vasculitis (e.g., granulomatosis with polyangiitis, microscopic polyangiitis, eosinophilic granulomatosis with polyangiitis, Henoch-Schönlein purpura, Kawasaki disease, polyarteritis nodosa, Takayasu's arteritis, giant cell arteritis). In some embodiments, the autoimmune disease can be an autoimmune rheumatic disease. In some embodiments, the autoimmune disease is an organ-specific autoimmune disease such as Addison’s disease, celiac disease, Graves’ disease, Hashimoto thyroiditis, multiple sclerosis, myelin oligodendrocyte glycoprotein (MOG) antibody-related diseases, neuromyelitis optica (NMO) spectrum disorders, myasthenia gravis, pernicious anemia, primary biliary cirrhosis, primary membranous nephropathy, or type I diabetes mellitus. In some embodiments, the autoimmune disease is antiphospholipid antibody syndrome (APS). In some embodiments, the methods can be applied – through introduction of an allergen or other BCR ligand into the CATCR – to the treatment of other B cell- and antibody-mediated diseases including type I allergies (e.g., any IgE-dependent allergic reactions, allergic asthma, urticaria, angioedema, allergic rhinitis), type II allergies (e.g., immune cytopenias, chronic idiopathic urticaria), and type III allergies (e.g., serum sickness and serum sickness-like reactions), B cell cancers, and B cell dyscrasias (for B cell clones expressing B cell receptors). Pharmaceutical Compositions In some embodiments, the present disclosure provides pharmaceutical compositions that include an engineered immune cell comprising a CATCR, wherein the CATCR includes a native or modified peptide of a T cell receptor-CD3 complex protein, and at least one antigenic peptide recognized by a B cell receptor (BCR), and a pharmaceutically acceptable carrier. In some embodiments, the present disclosure provides pharmaceutical compositions that include an Attorney Docket No: 44807-0422WO1 engineered immune cell comprising a nucleic acid and/or vector encoding a CATCR and a pharmaceutically acceptable carrier. In some embodiments, a pharmaceutical composition can include a buffer, a diluent, solubilizer, emulsifier, preservative, adjuvant, an excipient, or any combination thereof. In some embodiments, a composition, if desired, can also contain one or more additional therapeutically active substances. In some embodiments, compositions are formulated for parenteral administration. For example, a pharmaceutical composition provided herein may be provided in a sterile injectable form (e.g., a form that is suitable for subcutaneous injection, intramuscular injection, or intravenous infusion). For example, in some embodiments, a pharmaceutical composition is provided in a liquid dosage form that is suitable for injection. In some embodiments, a pharmaceutical composition is provided as powders (e.g., lyophilized and/or sterilized), optionally under vacuum, which can be reconstituted with an aqueous diluent (e.g., water, buffer, salt solution, etc.) prior to injection. In some embodiments, a pharmaceutical composition is diluted and/or reconstituted in water, sodium chloride solution, sodium acetate solution, benzyl alcohol solution, phosphate buffered saline, etc. In some embodiments, a powder should be mixed gently with the aqueous diluent (e.g., not shaken). In some embodiments, an engineered immune cell comprising a CATCR and/or a nucleic acid encoding a CATCR of the present disclosure is formulated with a pharmaceutically acceptable parenteral vehicle. Examples of such vehicles are water, saline, Ringer’s solution, dextrose solution, and 1-10% human serum albumin. Liposomes and nonaqueous vehicles such as fixed oils can also be used. A vehicle or lyophilized powder can contain additives that maintain isotonicity (e.g., sodium chloride, mannitol) and chemical stability (e.g., buffers and preservatives). In some embodiments, a formulation is sterilized by known or suitable techniques. A pharmaceutical composition may additionally comprise a pharmaceutically acceptable excipient, which, as used herein, includes any and all solvents, dispersion media, diluents, or other liquid vehicles, dispersion or suspension aids, surface active agents, isotonic agents, thickening, or emulsifying agents, preservatives, solid binders, lubricants and the like, as suited to the particular dosage form desired. Remington’s The Science and Practice of Pharmacy, 21st Edition, A. R. Gennaro (Lippincott, Williams & Wilkins, Baltimore, MD, 2006) discloses various excipients used in formulating pharmaceutical compositions and known techniques for the preparation thereof. Except insofar as any conventional excipient medium is incompatible with a substance or its Attorney Docket No: 44807-0422WO1 derivatives, such as by producing any undesirable biological effect or otherwise interacting in a deleterious manner with any other component(s) of the pharmaceutical composition, its use is contemplated to be within the scope of this disclosure. EXAMPLES The disclosure is further described in the following examples, which do not limit the scope of the disclosure described in the claims. Example 1 – Chimeric autoantigen-T cell receptor and related autoantigen-directed T cell therapies The present disclosure encompasses an antigen-specific immunotherapeutic strategy and its application for the treatment of autoimmune diseases and antiphospholipid syndrome (APS) in particular. The disclosed approach involves the expression of an autoantigen-modified T cell receptor (TCR), hereafter named chimeric autoantigen-TCRs (CATCRs), in human T cells, other cytotoxic cells, or other immune cells, that redirects the engineered cells to selectively kill B cells and plasma cells carrying a cognate B cell receptor (BCRs). This is achieved by incorporating all or partial antigenic sequences of the autoantigen of interest (e.g., β2GPI, EPCR, PT) into any part of the TCR-CD3 protein complex, which thereby acquires the ability to bind cognate BCRs, resulting in immune synapse formation, TCR signaling, and cytotoxic killing of autoreactive B cells expressing cognate BCRs (FIG.1A). In this example, CATCR T cells were modified to express antigenic sequences of the phospholipid-binding proteins β2GPI and/or EPCR and/or PT as part of either CD3 gamma (CD3ɣ), CD3 delta (CD3δ), CD3 epsilon (CD3ε), the TCR alpha and/or beta chains, or the TCR gamma and/or delta chains on the cell surface (FIGs. 1B-1D). Engineered cytotoxic cells expressing various CATCRs can be generated by several means through genetic modification of T cell, including but not limited to CRISPR/Cas-mediated homology directed repair (HDR) of the TRAC, TRBC, TRGC, TRDC, CD3G, CD3D, CD3E, and B2M gene loci. In this example, CATCR T cells were generated through CRISPR/Cas-mediated homology directed repair (HDR) using HDR templates (HDRT) containing nucleotide sequences encoding gene locus-specific 5’ and 3’ homology arms, domains of a relevant autoantigen which define binding to autoreactive B cells (e.g., β2GPI DI, I-II, I-III, I-IV, I-V, EPCR, or PT), domains of a Attorney Docket No: 44807-0422WO1 TCR-CD3 complex protein, and/or a linker/hinge, and/or a intracellular/co-stimulatory domain, and any additional sequences needed for successful expression (e.g., promoter sequences, Kozak sequences, signal peptide sequences, stop codon, terminator sequences, self-cleaving peptide sequences) under either control of an exogenous promoter or under control of the endogenous promoter of the targeted gene locus (FIGs.2A-2R, 2U-W, Tables 10-11, 14-22). In an alternative example, the disclosure involves the expression of phospholipid-binding proteins in the context of a first or higher generation chimeric antigen receptor (CAR) in immune cells under either control of an exogenous promoter or under control of the endogenous promoter of the targeted gene locus (FIGs.2S-2T, Tables 12-13, 23). [Table 10] Non-limiting compositions for CATCRs under exogenous promoter control #  Components  Possible SEQ ID NOs.  1  Promoter Sequence  SEQ ID NO. 77, 78, 79, 80, 81, or other  2 K z kS n e,    ns  [Table 11] Non-limiting compositions for CATCRs under endogenous promoter control #  Components  Possible SEQ ID NOs.  1  Optional Self‐cleaving Peptide  SEQ ID NO. 45, 46, 47, or 48, or other  e,    ns  Attorney Docket No: 44807-0422WO1 9  Stop Codon*    10  Terminator Sequence*  SEQ ID NO. 74, 75, or 76, or other  *may use endogenous stop codon and termination sequences instead with or without self-cleaving peptide control #  Components  Possible SEQ ID NOs.  1  Promoter Sequence  SEQ ID NO. 77, 78, 79, 80, 81, or other  2  Kozak Sequence    [Table 13] Non-limiting compositions for APS-autoantigen CARS endogenous promoter control # Components Possible SEQ ID NOs. r y [Table 14] Exemplary sequences for dual Cα/Cβ CATCRs SEQ    Name  Amino Acid Sequence (unless specified otherwise)  ID  u o u g s o r s l Attorney Docket No: 44807-0422WO1 Cys Thr Asp Pro Gln Pro Leu Lys Glu Gln Pro Ala Leu Asn Asp Ser Arg Tyr Cys Leu Ser Ser Arg Leu Arg Val Ser Ala Thr Phe Trp Gln Asn Pro Arg Asn His Phe Arg Cys Gln Val Gln Phe Tyr Gly Leu Ser Glu Asn Asp Glu Trp Thr Gln Asp Arg Ala Lys Pro Val Thr Gln Ile lu eu eu eu ro lu rg ys la eu er sp la he he he eu GA TC CC CC TG GC GC AA AA AG CT CG CT AA CG GG AC CT CT GA AG AG CT CC AC AG TG TG AA CC Attorney Docket No: 44807-0422WO1 ACCATCCTGTACGAGATCCTGCTGGGCAAAGCCACTCTGTACGCCGTGCTGGTGTCTGCCCTG GTGCTGATGGCCATGGTCAAGCGGAAGGACAGCAGAGGCAGAGCTAAAAGATCTGGCTCCGGC GCCACCAACTTCTCACTGCTTAAACAGGCCGGCGACGTGGAAGAGAACCCTGGACCTATGGCA Furin/ P2A peptide A G G C T C C C C G A e C C C T G T G C G C C G C C A T u o u g s a s u a e l p o r e r p l u g Attorney Docket No: 44807-0422WO1 β2GPI DI-II_EAAAK-Cα (287 AA) Met Ala Leu Pro Val Thr Ala Leu Leu Leu Pro Leu Ala Leu Leu Leu His Ala Ala Arg Pro Gly Arg Thr Cys Pro Lys Pro Asp Asp Leu Pro Phe Ser Thr Val Val Pro Leu Lys Thr Phe Tyr Glu Pro Gly Glu Glu g s a s u a p r p a n r u s A C C C G C C A A G T G T A G G C T T A G G C C G G A G G G G C G G A Attorney Docket No: 44807-0422WO1 CTGCTTAAACAGGCCGGCGACGTGGAAGAGAACCCTGGACCTATGGCACTGCCAGTTACTGCC CTGCTTCTTCCACTGGCACTGCTGCTCCATGCTGCTAGACCCGGAAGAACATGCCCCAAGCCA CD8α Signal Peptide C G T C A C C G C G G G C C C T C C C C T G C T T G C G T u o u g s a s u s o s r a u s l u g g n y u r Attorney Docket No: 44807-0422WO1 Ala Val Leu Val Ser Ala Leu Val Leu Met Ala Met Val Lys Arg Lys Asp Ser Arg Gly [SEQ ID NO. 184] β2GPI DI-III EAAAK-Cα (350 AA) u o u g s a s u s o s r a r n s l n s n l u o u g s a s u s o s r o o r p u a y u o r n s s e l y u o u g s a Attorney Docket No: 44807-0422WO1 Val Arg Tyr Thr Thr Phe Glu Tyr Pro Asn Thr Ile Ser Phe Ser Cys Asn Thr Gly Phe Tyr Leu Asn Gly Ala Asp Ser Ala Lys Cys Thr Glu Glu Gly Lys Trp Ser Pro Glu Leu Pro Val Cys Ala Pro Ile Ile Cys Pro Pro Pro Ser Ile Pro Thr Phe Ala Thr Leu Arg Val Tyr Lys Pro s r o o r p n p r p n o u u n u o u g s a s u s o s r o o r p s e n y e s o u n s u s p g r a p u o u g s a s u Attorney Docket No: 44807-0422WO1 Glu Gly Lys Trp Ser Pro Glu Leu Pro Val Cys Ala Pro Ile Ile Cys Pro Pro Pro Ser Ile Pro Thr Phe Ala Thr Leu Arg Val Tyr Lys Pro Ser Ala Gly Asn Asn Ser Leu Tyr Arg Asp Thr Ala Val Phe Glu Cys Leu Pro Gln His Ala Met Phe Gly Asn Asp Thr Ile Thr Cys Thr Thr o o r p s e n y e s s r s a r p e a [ a e ] xempary sequences or a ua murne α β SEQ    Name  Amino Acid Sequence (unless specified otherwise)  ID  NO o u n s a e o y u r . u o u g s a u r p r p t u r u o Attorney Docket No: 44807-0422WO1 e_xemplary  ^{Phe Ser Thr Val Val Pro Leu Lys Thr Phe Tyr Glu Pro Gly Glu Glu} Ile Thr Tyr Ser Cys Lys Pro Gly Tyr Val Ser Arg Gly Gly Met Arg Lys Phe Ile Cys Pro Leu Thr Gly Leu Trp Pro Ile Asn Thr Leu Lys Cys Thr Pro Arg Val Cys Pro Phe Ala Gly Ile Leu Glu Asn Gly Ala s u a e l p a l l o p r u u o u g s a s u a p r p a s r n e u o u g s a s u s o s r o o r p s e n y e s o u n s a e Attorney Docket No: 44807-0422WO1 His Gly Leu Ser Glu Glu Asp Lys Trp Pro Glu Gly Ser Pro Lys Pro Val Thr Gln Asn Ile Ser Ala Glu Ala Trp Gly Arg Ala Asp Cys Gly Ile Thr Ser Ala Ser Tyr Gln Gln Gly Val Leu Ser Ala Thr Ile Leu Tyr Glu Ile Leu Leu Gly Lys Ala Thr Leu Tyr Ala Val Leu Val Ser O. eu ro lu rg ys la ys lu ys ro ys hr ro ro yr rp ys he sn ly he ys rg le ys la hr hr eu eu [Table 16] Exemplary sequences for a Cα CATCR SEQ    Name  Amino Acid Sequence (unless specified otherwise)  ID  u o u g s a u r p a e e e u Attorney Docket No: 44807-0422WO1 Met Ala Leu Pro Val Thr Ala Leu Leu Leu Pro Leu Ala Leu Leu Leu His Ala Ala Arg Pro Gly Arg Thr Cys Pro Lys Pro Asp Asp Leu Pro Phe Ser Thr Val Val Pro Leu Lys Thr Phe Tyr Glu Pro Gly Glu Glu Ile Thr Tyr Ser Cys Lys Pro Gly Tyr Val Ser Arg Gly Gly Met Arg s a s u y p r p a n r u s u o u g s a s u s o s r o o r p s e n y e r s r s a r p e a u u r y o n e y e l n n Attorney Docket No: 44807-0422WO1 Tyr Val Gln Lys Asp Tyr Lys Asp Asp Asp Asp Lys Gly Ser Gln Thr Ser Arg Ser Tyr Thr Ser Gly Gly Gly Gly Ser Asp Ile Gln Asn Pro Asp Pro Ala Val Tyr Gln Leu Arg Asp Ser Lys Ser Ser Asp Lys Ser Val Cys Leu Phe Thr Asp Phe Asp Ser Gln Thr Asn Val Ser Gln Ser g r p u l u SEQ    Name  Amino Acid Sequence (unless specified otherwise)  ID  NO.  u o u g s o r s l r n r e u u u u o u g s a s u y e l p o r e r p l u g u o Attorney Docket No: 44807-0422WO1 Phe Ser Thr Val Val Pro Leu Lys Thr Phe Tyr Glu Pro Gly Glu Glu Ile Thr Tyr Ser Cys Lys Pro Gly Tyr Val Ser Arg Gly Gly Met Arg Lys Phe Ile Cys Pro Leu Thr Gly Leu Trp Pro Ile Asn Thr Leu Lys Cys Thr Pro Arg Val Cys Pro Phe Ala Gly Ile Leu Glu Asn Gly Ala s u s o s r o o r p s e n y e r o u n s u s p g r a p u u r y o n e y e l n n r n e r s u r r l e r a [Table 18] Exemplary sequences for a Cδ CATCR Attorney Docket No: 44807-0422WO1 SEQ Name Amino Acid Sequence (unless specified otherwise) ID NO. 204 2GPI DIVCδ 2GPI DIV G4SCδ 506 AA u o u g s a s u s o s r o o r p s e n y e r y g e r r l s u n [Table 19] Exemplary sequences for a C ^ CATCR SEQ    Name  Amino Acid Sequence (unless specified otherwise)  ID  u o u g s a s u s o s r o o r p s e n y e r u Attorney Docket No: 44807-0422WO1 Pro Ser Ile Ala Glu Thr Lys Leu Gln Lys Ala Gly Thr Tyr Leu Cys Leu Leu Glu Lys Phe Phe Pro Asp Val Ile Lys Ile His Trp Gln Glu Lys Lys Ser Asn Thr Ile Leu Gly Ser Gln Glu Gly Asn Thr Met Lys Thr Asn Asp Thr Tyr Met Lys Phe Ser Trp Leu Thr Val Pro Glu Lys s l r u u . SEQ.  Comprising  Name  Amino Acid Sequence (unless specified otherwise)  No.  SEQ. IDs.  206    β2GPI‐CD3 ^ CATCR  β2GPI DI EAAAK‐CD3 ^ CATCR (248 AA) u o u g s u s e a r u e l n u u o u g s a s u a r n p t r r y r s g u o u g Attorney Docket No: 44807-0422WO1 Lys Phe Ile Cys Pro Leu Thr Gly Leu Trp Pro Ile Asn Thr Leu Lys Cys Thr Pro Arg Val Cys Pro Phe Ala Gly Ile Leu Glu Asn Gly Ala Val Arg Tyr Thr Thr Phe Glu Tyr Pro Asn Thr Ile Ser Phe Ser Cys Asn Thr Gly Phe Tyr Leu Asn Gly Ala Asp Ser Ala Lys Cys Thr Glu s o s r a n e s r r y l p p g e p a y seque ces o s SEQ. Comprising Name Amino Acid Sequence No. SEQ. IDs. 209 β2GPI-CD3δ β2GPI DI (G4S) -CD3ε CATCR (248 AA) u o u g s y l u o u u r y n u u o u g s a s u y o e g s s a y a g g Attorney Docket No: 44807-0422WO1 Signal Peptide is underlined 211 β2GPI-CD3δ β2GPI DI-III (G4S) -CD3 CATCR (369 AA) u o u g s a s u s o s r y e r u n r y l p p n [Table 22] Exemplary sequences for CD3ε CATCRs SEQ.  Comprising  Name  Amino Acid Sequence (unless specified otherwise)  No.  SEQ. IDs.  u o u g s y e n p y e p y s y o g u o u g s a s u y r Attorney Docket No: 44807-0422WO1 Lys Val Ser Ile Ser Gly Thr Thr Val Ile Leu Thr Cys Pro Gln Tyr Pro Gly Ser Glu Ile Leu Trp Gln His Asn Asp Lys Asn Ile Gly Gly Asp Glu Asp Asp Lys Asn Ile Gly Ser Asp Glu Asp His Leu Ser Leu Lys Glu Phe Ser Glu Leu Glu Gln Ser Gly Tyr Tyr Val Cys Tyr Pro a r l g o g u o u g s a s u s o s r y s o p s g g e r y o p [Table 23] Exemplary APS-CAR sequences SEQ.  Comprising  Name  Amino Acid Sequence (unless specified otherwise)  No.  SEQ. IDs.  u o u g s o o u y e n r r r s s a s r Attorney Docket No: 44807-0422WO1 [SEQ ID NO. 215] Signal Peptide is underlined T C G G C A C A C A A C G C T u o u g s a s u a r a e r g o e o y o u e r t u o u g s a s u Attorney Docket No: 44807-0422WO1 Glu Gly Lys Trp Ser Pro Glu Leu Pro Val Cys Ala Pro Ile Ile Cys Pro Pro Pro Ser Ile Pro Thr Phe Ala Thr Leu Arg Val Tyr Lys Pro Ser Ala Gly Asn Asn Ser Leu Tyr Arg Asp Thr Ala Val Phe Glu Cys Leu Pro Gln His Ala Met Phe Gly Asn Asp Thr Ile Thr Cys Thr Thr ro ro yr rp ys he sn ly he ys la ly he eu rg ro la yr rg et sn et ly la

Claims

Attorney Docket No: 44807-0422WO1 WHAT IS CLAIMED IS: 1. An immunoresponsive cell comprising: a recombinant chimeric autoantigen-T cell receptor (CATCR) comprising: (a) an extracellular binding domain comprising an autoantigenic peptide, wherein the autoantigenic peptide is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 delta/ gamma/ epsilon complex protein. 2. The immunoresponsive cell of claim 1, wherein the recombinant CATCR further comprises a linker or hinge domain. 3. The immunoresponsive cell of claim 1 or 2, wherein the recombinant CATCR further comprises an intracellular co-stimulatory, immunomodulatory, or signaling domain. 4. The immunoresponsive cell of any one of claims 1-3, wherein the recombinant CATCR is expressed from an expression cassette placed in an endogenous T cell receptor alpha constant (TRAC) locus and/or a T cell receptor beta constant 1 (TRBC1) locus and/or a T cell receptor beta constant 2 (TRBC2) locus and/or a T cell receptor gamma constant 1 (TRGC1) locus and/or a T cell receptor gamma constant 2 (TRGC2) locus and/or a T cell receptor delta constant (TRDC) locus and/or a CD3 gamma (CD3G) locus and/or a CD3 delta (CD3D) locus and/or CD3 epsilon (CD3E) locus and/or B2M locus and/or other gene locus of the immunoresponsive cell. 5. The immunoresponsive cell of any one of claims 1-4, wherein the placement of the recombinant CATCR expression cassette disrupts the endogenous expression of a TCR- CD3 complex protein comprising a native TCR alpha chain and/or a native TCR beta chain and/or a native TCR gamma and/or a native TCR delta chain and/or a native CD3 gamma chain and/or a native CD3 delta chain and/or a native CD3 epsilon chain and/or a native B2M chain in the immunoresponsive cell. Attorney Docket No: 44807-0422WO1 6. The immunoresponsive cell of any one of claims 1-5, wherein the placement of the recombinant CATCR expression cassette prevents mispairing between the recombinant CATCR and native TCR-CD3 complex chains in the immunoresponsive cell. 7. The immunoresponsive cell of any one of claims 1-6, wherein the CATCR complex associates with a CD3ζ chain, and wherein binding of a cognate B cell receptor to the autoantigenic peptide of the CATCR activates the CD3ζ chain, wherein the activation of the CD3ζ chain activates the immunoresponsive cell. 8. The immunoresponsive cell of any one of claims 1-7, wherein the autoantigenic peptide is derived from a phospholipid-binding protein. 9. The immunoresponsive cell of claim 8, wherein the phospholipid binding protein is beta- 2 glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), or prothrombin (PT). 10. The immunoresponsive cell of any one of claims 1-9, wherein the autoantigenic peptide is expressed under a signal peptide endogenous to the autoantigen. 11. The immunoresponsive cell of any one of claims 1-9, wherein the autoantigenic peptide is expressed under a non-endogenous signal peptide. 12. The immunoresponsive cell of any one of claims 1-11, wherein the autoantigenic peptide is expressed as part of a CD3 gamma (CD3 ^) chain; a CD3 epsilon (CD3ε) chain; a CD3 delta (CD3δ) chain; a T cell receptor (TCR) alpha chain; a T cell receptor (TCR) beta chain, a T cell receptor (TCR) gamma chain, or a T cell receptor (TCR) delta chain of the recombinant CATCR. 13. The immunoresponsive cell of any one of claims 8-12, wherein the autoantigenic peptide comprises: Attorney Docket No: 44807-0422WO1 at least part of a domain of β2GPI, wherein β2GPI comprises domain I (DI), domain II (DII), domain III (DIII), domain IV (DIV), or domain V (DV); an amino acid epitope comprising a sequence of RGGMR; or any combinations thereof. 14. The immunoresponsive cell of any one of claims 8-12, wherein the autoantigenic peptide comprises at least part of the endothelial protein C receptor (EPCR); the full or part of the extracellular (EC) domains of EPCR; a modified extracellular (EC) domain of EPCR; or EPCR in complex with a phospholipid. 15. The immunoresponsive cell of any one of claims 8-12, wherein the autoantigenic peptide comprises at least part of prothrombin (PT) or posttranslationally modified prothrombin. 16. The immunoresponsive cell of any one of claims 1-15, wherein the immunoresponsive cell is a human immune cell. 17. The immunoresponsive cell of any one of claims 1-16, wherein the immunoresponsive cell is a T cell. 18. A nucleic acid sequence encoding a recombinant CATCR, wherein the recombinant CATCR comprises: (a) an extracellular binding domain comprising an autoantigenic peptide, wherein the autoantigenic peptide is recognized by a B cell receptor (BCR), and (b) a constant domain comprising a native or modified peptide of a T cell receptor-CD3 delta/ gamma/ epsilon complex protein. 19. The nucleic acid of claim 18, wherein the recombinant CATCR further comprises a linker or hinge domain. 20. The nucleic acid of claim 18 or 19, wherein the recombinant CATCR further comprises an intracellular co-stimulatory, immunomodulatory, or signaling domain. Attorney Docket No: 44807-0422WO1 21. The nucleic acid of any one of claims 18-20, wherein the recombinant CATCR comprises a recombinant T cell receptor (TCR)-CD3 protein complex. 22. The nucleic acid of any one of claims 18-21, wherein the recombinant CATCR is expressed from an expression cassette placed in an endogenous T cell receptor alpha constant (TRAC) locus and/or a T cell receptor beta constant 1 (TRBC1) locus and/or a T cell receptor beta constant 2 (TRBC2) locus and/or a T cell receptor gamma constant 1 (TRGC1) locus and/or a T cell receptor gamma constant 2 (TRGC2) locus and/or a T cell receptor delta constant (TRDC) locus and/or a CD3 gamma (CD3G) locus and/or a CD3 delta (CD3D) locus and/or CD3 epsilon (CD3E) locus and/or B2M locus and/or other gene locus of the immunoresponsive cell. 23. The nucleic acid of any one of claims 18-22, wherein the placement of the recombinant CATCR expression cassette disrupts the endogenous expression of a TCR-CD3 complex protein comprising a native TCR alpha chain and/or a native TCR beta chain and/or a native TCR gamma and/or a native TCR delta chain and/or a native CD3 gamma chain and/or a native CD3 delta chain and/or a native CD3 epsilon chain and/or a native B2M chain in the immunoresponsive cell. 24. The nucleic acid of any one of claims 18-23, wherein the placement of the recombinant CATCR expression cassette prevents mispairing between the recombinant CATCR and native TCR-CD3 complex chains in the immunoresponsive cell. 25. The nucleic acid of any one of claims 18-24, wherein the CATCR complex associates with a CD3ζ chain, and wherein binding of a cognate B cell receptor to the autoantigenic peptide of the CATCR activates the CD3ζ chain, wherein the activation of the CD3ζ chain activates the immunoresponsive cell. 26. The nucleic acid of any one of claims 18-25, wherein the autoantigenic peptide is derived from a phospholipid-binding protein. Attorney Docket No: 44807-0422WO1 27. The nucleic acid of claim 26, wherein the phospholipid binding protein is beta-2 glycoprotein I (β2GPI), endothelial protein C receptor (EPCR), or prothrombin (PT). 28. The nucleic acid of any one of claims 18-27, wherein the autoantigenic peptide is expressed as part of a CD3 gamma (CD3 ^) chain; a CD3 epsilon (CD3ε) chain; a CD3 delta (CD3δ) chain; a T cell receptor (TCR) alpha chain; a T cell receptor (TCR) beta chain; a T cell receptor (TCR) gamma chain, or a T cell receptor (TCR) delta chain of the CATCR. 29. The nucleic acid of any one of claims 26-28, wherein the autoantigenic peptide comprises: at least part of a domain of β2GPI, wherein the β2GPI comprises domain I (DI), domain II (DII), domain III (DIII), domain IV (DIV), or domain V (DV); an amino acid epitope comprising a sequence of RGGMR; or any combinations thereof. 30. The nucleic acid of any one of claims 26-28, wherein the autoantigenic peptide comprises at least part of the endothelial protein C receptor (EPCR); the full or part of the extracellular (EC) domains of EPCR; a modified extracellular (EC) domain of EPCR; or EPCR in complex with a phospholipid. 31. The nucleic acid of any one of claims 26-28, wherein the autoantigenic peptide comprises at least part of prothrombin (PT) or posttranslationally modified prothrombin. 32. A vector comprising the nucleic acid of any one of claims 18-31. 33. The vector of claim 32, further comprising a promoter. 34. The vector of claim 33, wherein the promoter is a TRAC promoter or EF1-alpha promoter. Attorney Docket No: 44807-0422WO1 35. The vector of claim 34, wherein the promoter is an EF1-alpha promoter, CMV promoter, hPGK promoter, RPBSA promoter, or human gene promoter. 36. The vector of any one of claim 32-35, wherein the vector is a viral vector. 37. A method of producing an engineered immune cell, the method comprising: introducing into an immune cell a nucleic acid of any one of claims 18-31 or a vector of any one of claims 32-36, thereby producing the engineered immune cell. 38. The method of claim 37, wherein the nucleic acid is introduced into the immunoresponsive cell by using a gene-editing agent. 39. The method of claim 38, wherein the gene-editing agent comprises CRISPR/Cas components. 40. The method of claim 39, wherein the nucleic acid is introduced into a gene locus of the immunoresponsive cell, wherein expression of the nucleic acid is under control of the endogenous promoter of the gene locus. 41. The method of claim 39, wherein the nucleic acid is introduced into a gene locus of the immunoresponsive cell, wherein the expression of the nucleic acid is under control of an exogenous promoter. 42. The method of claim 41, wherein the exogenous promoter is an EF1-alpha promoter, CMV promoter, hPGK promoter, RPBSA promoter, TRAC promoter, or human gene promoter. 43. An engineered immune cell produced by any one of the methods of claims 37-42. 44. A pharmaceutical composition comprising an engineered immune cell of claim 43 and a pharmaceutically acceptable carrier. Attorney Docket No: 44807-0422WO1 45. A method of treating an autoimmune disease in a subject, the method comprising administering to the subject the engineered immune cell of claim 43 or a pharmaceutical composition of claim 44. 46. The method of claim 45, wherein the autoimmune disease is an autoimmune rheumatic disease, systemic autoimmune disease, or an organ-specific autoimmune disease. 47. The method of claim 46, wherein the systemic autoimmune disease is rheumatoid arthritis (RA), spondyloarthropathies, ankylosing spondylitis and psoriatic arthritis, juvenile idiopathic arthritis, systemic lupus erythematosus, lupus nephritis, Sjögren’s disease, scleroderma/ systemic sclerosis, an idiopathic inflammatory myopathy, myositis, dermatomyositis, antisynthetase syndrome, an immune-mediated necrotizing myopathy, IgG4-related disease, vasculitis, granulomatosis with polyangiitis, microscopic polyangiitis, eosinophilic granulomatosis with polyangiitis, anti-glomerular basement membrane disease, Henoch-Schönlein purpura, Kawasaki disease, polyarteritis nodosa, Takayasu's arteritis, or giant cell arteritis. 48. The method of claim 46, wherein the organ-specific autoimmune disease is acquired haemophilia, autoimmune encephalitis, autoimmune hemolytic anemia, autoimmune hepatitis, autoimmune and paraneoplastic encephalitis, Addison’s disease, celiac disease, Graves’ disease, Hashimoto thyroiditis, immune thrombocytopenia purpura, multiple sclerosis, myelin oligodendrocyte glycoprotein (MOG) antibody-related diseases, neuromyelitis optica (NMO) spectrum disorders, myasthenia gravis, Lambert-Eaton myasthenia syndrome, pemphigus vulgaris, pemphigus foliaceous, bullous pemphigoid, other autoimmune blistering diseases, autoimmune membranous nephropathy, primary membranous nephropathy, primary biliary cirrhosis, thrombotic thrombocytopenic purpura, or type I diabetes mellitus. 49. The method of claim 46, wherein the autoimmune disease is antiphospholipid antibody syndrome (APS) or its preclinical state.