WO2020080853A1 - Lrig-1 단백질에 특이적인 결합 분자 및 이의 용도 - Google Patents
Lrig-1 단백질에 특이적인 결합 분자 및 이의 용도 Download PDFInfo
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- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/0005—Vertebrate antigens
- A61K39/0011—Cancer antigens
- A61K39/001102—Receptors, cell surface antigens or cell surface determinants
- A61K39/001111—Immunoglobulin superfamily
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6801—Drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/31—Immunoglobulins specific features characterized by aspects of specificity or valency multispecific
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/75—Agonist effect on antigen
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
Definitions
- the present invention relates to a binding molecule capable of specifically binding to Lrig-1 (leucine-rich and immunoglobulin-like domains 1) protein, which is a protein present on the surface of a regulatory T cell (Treg cell), and uses thereof It is about.
- Lrig-1 leucine-rich and immunoglobulin-like domains 1
- autoimmune disease occurs by removing lymphocytes that may have specific receptors for their antigen, or by inactivating the ability to respond to themselves after contact with the self antigen. If there is a problem in inducing or continuing self-tolerance, an immune response occurs against the self-antigen, and the resulting disease is called autoimmune disease.
- Gershon introduced the concept of suppressing T cells with the possibility of the presence of T cells capable of controlling and suppressing the effector function of conventional T cells. Introduced, since the first presentation (RK Gershon and K. Kondo, Immunology, 1970, 18: 723-37), research has been conducted in many fields of immunology to characterize the biological properties and functions of regulatory T cells.
- the regulatory T cell plays an important role in naturally preventing the occurrence of excessive inflammation and immune response, but when autoimmune diseases and chronic inflammatory diseases occur, the function and number of regulatory T cells are significantly reduced. It was reported. Therefore, in patients with immune and inflammatory diseases, it is important that regulatory T cells are produced at normal levels, which may be one of the treatments for the diseases.
- CDRs complementarity determining regions
- the CDR mainly serves to bind to the antigenic epitope of the antigen.
- the CDRs of each chain are typically referred to as CDR1, CDR2 and CDR3, starting from the N-terminus, and also identified by the chain in which the particular CDR is located.
- One object of the present invention is to provide a binding molecule specific for the Lrig-1 protein present on the surface of a regulatory T cell (Treg).
- Another object of the present invention is to provide a nucleic acid molecule encoding the binding molecule according to the present invention.
- Another object of the present invention is to provide an expression vector in which the nucleic acid molecule according to the present invention is inserted.
- Another object of the present invention is to provide a host cell line transfected with the expression vector according to the present invention.
- Another object of the present invention is to provide an antibody-drug conjugate according to the present invention.
- Another object of the present invention is to provide a pharmaceutical composition for the prevention or treatment of immune-related diseases comprising the binding molecule according to the present invention.
- Another object of the present invention is a binding molecule provided in the present invention. Or to provide a method for the prevention or treatment of immune-related diseases comprising the step of administering an antibody-drug conjugate (Antibody-Drug Conjugate, ADC) to a subject in a pharmaceutically effective amount.
- ADC Antibody-Drug Conjugate
- the present inventors discovered Lrig-1 protein specifically present on the surface of regulatory T cells, and selected a monoclonal antibody capable of specifically binding to the Lrig-1 protein by selecting the epitope of the protein.
- the present invention was completed by making.
- a binding molecule specifically binding to Lrig-1 (leucine-rich and immunoglobulin-like domains 1) protein is provided.
- binding molecule is an intact immunoglobulin comprising a monoclonal antibody such as a chimeric, humanized or human monoclonal antibody, or an immunoglobulin that binds an antigen, such as Refers to a variable domain comprising an immunoglobulin fragment that competes with an intact immunoglobulin for binding of influenza A virus with monomeric HA or trimer HA. Regardless of the structure, the antigen-binding fragment binds the same antigen recognized by the intact immunoglobulin.
- Antigen-binding fragments include two or more consecutive groups of the amino acid sequence of a binding molecule, 20 or more consecutive amino acid residues, 25 or more consecutive amino acid residues, 30 or more consecutive amino acid residues, 35 or more consecutive amino acid residues, 40 or more consecutive amino acid residues , 50 or more consecutive amino acid residues, 60 or more consecutive amino acid residues, 70 or more consecutive amino acid residues, 80 or more consecutive amino acid residues, 90 or more consecutive amino acid residues, 100 or more consecutive amino acid residues, 125 or more consecutive amino acid residues, Peptides or polypeptides comprising the amino acid sequence of at least 150 contiguous amino acid residues, at least 175 contiguous amino acid residues, at least 200 contiguous amino acid residues, or at least 250 contiguous amino acid residues.
- Antigen-binding fragments are in particular Fab, F (ab '), F (ab') 2, Fv, dAb, Fd, complementarity determining region (CDR) fragments, single-chain antibodies (scFv), bivalent Single-chain antibodies, single-chain phage antibodies, containing one or more fragments of immunoglobulins sufficient to bind a specific antigen to a polypeptide, unibody, diabody, tribody, tetrabody, polypeptide Polypeptides, and the like.
- the fragments can be produced synthetically or by enzymatic or chemical degradation of complete immunoglobulins, or can be genetically engineered by recombinant DNA technology. Methods of production are well known in the art.
- the Lrig-1 protein is a transmembrane protein composed of 1091 amino acids present on the surface of regulatory T cells, extracellular or lumen-side leucine-rich repeat (LRR) and three immune bodies. It consists of immunoglobulin-like domains, transmembrane sequence and cytoplasmic tail.
- the LRIG gene family includes LRIG1, LRIG2 and LRIG3, and the amino acids between them are very conservative.
- the LRIG1 gene is highly expressed in normal skin and can be expressed in basal and hair follicle cells to control the proliferation of epithelial stem cells. Therefore, it plays an important role in maintaining the homeostasis of the epidermis and can develop into psoriasis or skin cancer when absent.
- the chromosome 3p14.3 region where LRIG1 is located When the chromosome 3p14.3 region where LRIG1 is located is cut, it has been reported that it may develop into cancer cells. In fact, the expression of LRIG1 is greatly reduced in renal cell carcinoma and cutaneous squamous cell carcinoma. Confirmed. However, recently, it has been found that the cancer expressing the Lrig-1 is only 20-30%. On the other hand, for the purposes of the present invention, the Lrig-1 protein may be a protein present in humans or mice, but is not limited thereto.
- the Lrig-1 protein may be a polypeptide represented by SEQ ID NO: 1 derived from human or a polypeptide represented by SEQ ID NO: 3 derived from mouse, but is not limited thereto.
- the Lrig-1 protein represented by SEQ ID NO: 1 may be encoded by the polynucleotide represented by SEQ ID NO: 2, but is not limited thereto.
- the Lrig-1 protein represented by SEQ ID NO: 3 may be encoded by the polynucleotide represented by SEQ ID NO: 4, but is not limited thereto.
- the binding molecule In the present invention, the binding molecule,
- Heavy chain CDR1 consisting of an amino acid sequence selected from the group represented by SEQ ID NOs: 5, 13, 21 and 29
- Heavy chain CDR2 consisting of the amino acid sequence selected from the group represented by SEQ ID NOs: 6, 14, 22 and 30
- a heavy chain variable region comprising a heavy chain CDR3 consisting of an amino acid sequence selected from the group represented by SEQ ID NOs: 7, 15, 23 and 31;
- a light chain CDR1 consisting of an amino acid sequence selected from the group represented by SEQ ID NOs: 8, 16, 24 and 32;
- a light chain CDR2 represented by amino acid sequence selected from the group represented by SEQ ID NOs: 9, 17, 25 and 33;
- Light chain CDR3 consisting of an amino acid sequence selected from the group represented by SEQ ID NO: 10, 18, 26 and 34; may be a binding molecule comprising a light chain variable region comprising.
- the binding molecule In the present invention, the binding molecule,
- a heavy chain variable region selected from the group consisting of a heavy chain variable region comprising a heavy chain CDR1 represented by SEQ ID NO: 29, a heavy chain CDR2 represented by SEQ ID NO: 30, and a heavy chain CDR3 represented by SEQ ID NO: 31;
- a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 16, a light chain CDR2 represented by SEQ ID NO: 17, and a light chain CDR3 represented by SEQ ID NO: 18;
- a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 24, a light chain CDR2 represented by SEQ ID NO: 25, and a light chain CDR3 represented by SEQ ID NO: 26;
- a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 32, a light chain CDR2 represented by SEQ ID NO: 33, and a light chain CDR3 represented by SEQ ID NO: 34; a light chain variable region selected from the group consisting of It can be a binding molecule.
- the binding molecule In the present invention, the binding molecule,
- a heavy chain variable region comprising a heavy chain CDR1 represented by SEQ ID NO: 5, a heavy chain CDR2 represented by SEQ ID NO: 6, and a heavy chain CDR3 represented by SEQ ID NO: 7; And a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 8, a light chain CDR2 represented by SEQ ID NO: 9, and a light chain CDR3 represented by SEQ ID NO: 10;
- a heavy chain variable region comprising a heavy chain CDR1 represented by SEQ ID NO: 21, a heavy chain CDR2 represented by SEQ ID NO: 22, and a heavy chain CDR3 represented by SEQ ID NO: 23;
- a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 24, a light chain CDR2 represented by SEQ ID NO: 25, and a light chain CDR3 represented by SEQ ID NO: 26;
- a heavy chain variable region comprising a heavy chain CDR1 represented by SEQ ID NO: 29, a heavy chain CDR2 represented by SEQ ID NO: 30, and a heavy chain CDR3 represented by SEQ ID NO: 31;
- a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 32, a light chain CDR2 represented by SEQ ID NO: 33, and a light chain CDR3 represented by SEQ ID NO: 34; may be a binding molecule selected from the group consisting of have.
- the binding molecule In the present invention, the binding molecule,
- a heavy chain variable region consisting of any one amino acid sequence selected from the group represented by SEQ ID Nos: 11, 19, 27 and 35;
- It may be a binding molecule comprising a; light chain variable region consisting of any one amino acid sequence selected from the group represented by SEQ ID NO: 12, 20, 28 and 36.
- the binding molecule In the present invention, the binding molecule,
- binding molecule comprising a heavy chain variable region represented by SEQ ID NO: 11 and a light chain variable region represented by SEQ ID NO: 12;
- binding molecule comprising a heavy chain variable region represented by SEQ ID NO: 19 and a light chain variable region represented by SEQ ID NO: 20;
- a binding molecule comprising a heavy chain variable region represented by SEQ ID NO: 35, and a light chain variable region represented by SEQ ID NO: 36; may be a binding molecule selected from the group consisting of.
- the binding molecule may further include an Fc region (Fragment crystallization region) or a constant region (constant region).
- the Fc region may be an Fc region of an IgG1, IgG2, IgG3 or IgG4 antibody, or may be derived therefrom, or may be a hybrid Fc region.
- the Fc region may be an Fc region of a mammalian-derived IgG1, IgG2, IgG3 or IgG4 antibody, preferably a human-derived IgG1, IgG2, IgG3 or IgG4 antibody Fc region, but is not limited thereto. .
- the constant region may be a mouse-derived IgG2a constant region represented by SEQ ID NO: 37, but is not limited thereto.
- the constant region may be a mouse derived immunoglobulin kappa constant region represented by SEQ ID NO: 38, but is not limited thereto.
- the constant region may be a human-derived IgG1 constant region represented by SEQ ID NO: 39 or SEQ ID NO: 53, but is not limited thereto.
- the constant region may be a human-derived immunoglobulin kappa constant region represented by SEQ ID NO: 40, but is not limited thereto.
- the constant region may be a human-derived IgG2 constant region represented by SEQ ID NO: 41, but is not limited thereto.
- the constant region may be a human-derived IgG3 constant region represented by SEQ ID NO: 42, but is not limited thereto.
- the constant region may be a human-derived IgG4 constant region represented by SEQ ID NO: 43, but is not limited thereto.
- the Fc region may be a human-derived immunoglobulin lambda constant region, but is not limited thereto.
- the "hybrid Fc" may be derived from a combination of human IgG subclasses or a combination of human IgD and IgG.
- the hybrid Fc has an effect of increasing the serum half-life of the biologically active molecule when binding to the biologically active molecule, polypeptide, etc., as well as increasing the expression level of the polypeptide when the nucleotide encoding the Fc-polypeptide fusion protein is expressed.
- the hybrid Fc region may be a hybrid Fc represented by SEQ ID NO: 44, but is not limited thereto.
- the Fc or constant region may be linked to the variable region by a linker.
- a linker is linked to the C-terminus of the Fc or constant region, and the N-terminus of the binding molecule of the present invention may be linked to the linker, but is not limited thereto.
- the "linker (linker)” may include a sequence that can be cleaved by an enzyme that is overexpressed in the tissue or cell of the desired disease. When it can be cleaved by an enzyme that is overexpressed as described above, it is possible to effectively prevent the activity of the polypeptide from being reduced due to the Fc or constant region.
- the peptide linker consisting of 33 amino acids located at positions 282 to 314 of human albumin most present in the blood, more preferably composed of 13 amino acids located at parts 292 to 304 It may be a peptide linker, and this part is a part exposed to the outside most of the three-dimensional structure, and is a part that minimizes the possibility of inducing an immune response in the body. However, it is not limited thereto.
- the binding molecule of the present invention may further include a heavy chain constant region consisting of an amino acid sequence selected from the group represented by SEQ ID NOs: 37, 39, 41, 42, 43, 44 and 53.
- the binding molecule of the present invention may further include a light chain constant region consisting of the amino acid sequence represented by SEQ ID NO: 38 or 40.
- binding molecule of the present invention is a binding molecule of the present invention.
- a heavy chain constant region consisting of the amino acid sequence represented by SEQ ID NO: 37;
- the light chain constant region consisting of the amino acid sequence represented by SEQ ID NO: 38 may be further included.
- binding molecule of the present invention is a binding molecule of the present invention.
- a heavy chain constant region consisting of an amino acid sequence selected from the group represented by SEQ ID Nos: 39, 41, 42, 43 and 53;
- the light chain constant region consisting of the amino acid sequence represented by SEQ ID NO: 40 may be further included.
- binding molecule of the present invention is a binding molecule of the present invention.
- the heavy chain constant region consisting of the amino acid sequence represented by SEQ ID NO: 44 may be further included.
- binding molecule of the present invention is a binding molecule of the present invention.
- a binding molecule comprising a heavy chain represented by SEQ ID NO: 45 and a light chain represented by SEQ ID NO: 46;
- a binding molecule comprising a heavy chain represented by SEQ ID NO: 47 and a light chain represented by SEQ ID NO: 48;
- a binding molecule comprising a heavy chain represented by SEQ ID NO: 49 and a light chain represented by SEQ ID NO: 50;
- a binding molecule comprising a heavy chain represented by SEQ ID NO: 51, and a light chain represented by SEQ ID NO: 52; may be a binding molecule selected from the group consisting of.
- the binding molecule of the present invention is characterized by being an antibody, but is not limited thereto no.
- the antibody has the ability to bind to the Lrig-1 protein as part of a monoclonal antibody, full-length antibody, or antibody, and competes with the binding molecule of the present invention to bind to the Lrig-1 antigen-determining site. Includes all antibody fragments that can.
- the "antibody” refers to a protein molecule that serves as a receptor specifically recognizing an antigen, including an immunoglobulin molecule that is immunologically reactive with a specific antigen.
- the antigen may be a Lrig-1 protein present on the surface of a regulatory T cell.
- the Lrig-1 protein may specifically recognize a Leucine Rich Region or an immunoglobulin-like domain, but is not limited thereto.
- the "immunoglobulin” has a heavy chain and a light chain, and each heavy chain and light chain includes a constant region and a variable region.
- the variable regions of the light and heavy chains include three variable regions and four framework regions called complementarity determining regions (hereinafter referred to as "CDRs").
- the CDR mainly serves to bind to the antigenic determinant (Epitope) of the antigen.
- the CDRs of each chain are typically referred to as CDR1, CDR2 and CDR3, starting from the N-terminus, and also identified by the chain in which the particular CDR is located.
- the "monoclonal antibody” refers to an antibody molecule having a single molecular composition obtained from a population of substantially identical antibodies, and exhibits single binding specificity and affinity for a specific antigenic determinant (Epitope).
- the "full-length antibody” is a structure having two full-length light chains and two full-length heavy chains, and each light chain is connected by a heavy chain and a disulfide bond, IgA, IgD, IgE, IgM, and IgG.
- the IgG is a subtype, and includes IgG1, IgG2, IgG3 and IgG4.
- the "fragment of the antibody” means a fragment having an antigen-binding function, and includes Fab, Fab ', F (ab') 2 and Fv, and the like.
- the Fab has a structure having a variable region of a light chain and a heavy chain, a constant region of a light chain, and a first constant region (CH1 domain) of a heavy chain, and has one antigen binding site.
- the F (ab ') 2 antibody is produced by cysteine residues in the hinge region of Fab' forming disulfide bonds.
- Fv Variable fragment refers to the smallest antibody fragment having only the heavy chain variable region and the light chain variable region.
- double-chain Fv the heavy chain variable region and the light chain variable region are connected by disulfide bonds
- scFv single-chain Fv
- the variable region of the heavy chain and the variable region of the light chain are commonly linked through a peptide linker.
- a protein hydrolase for example, papain or pepsin
- a fragment of Fab or F (ab ') 2 can be obtained, and the antibody fragment can be produced through genetic recombination technology.
- the antibody is a chimeric antibody, a humanized antibody, a bivalent, a bispecific molecule, a minibody, a domain antibody, a bispecific antibody, an antibody mimetic, a uni
- the body may be a diabody, a tribody, a tetrabody, or a fragment thereof, but is not limited thereto.
- the "chimeric antibody” is an antibody that recombines the variable region of a mouse antibody and the constant region of a human antibody, and is an antibody with a greatly improved immune response compared to a mouse antibody.
- the "humanized antibody” means an antibody in which the protein sequence of an antibody derived from a non-human species is modified to be similar to an antibody variant naturally produced in humans.
- the humanized antibody may be prepared by recombining a mouse-derived CDR with a FR derived from a human antibody to prepare a humanized variable region, and recombining it with a constant region of a preferred human antibody to produce a humanized antibody.
- the binding molecule can also be provided as a bispecific antibody or bispecific antigen binding fragment capable of binding to Lrig-1 protein and other proteins.
- the bispecific antibody and the bispecific antigen binding fragment may include a binding molecule according to the present invention.
- the bispecific antibody and the bispecific antigen binding fragment includes an antigen binding domain capable of binding to the Lrig-1 protein, wherein the antigen binding domain capable of binding to the Lrig-1 protein is It may comprise or consist of a binding molecule according to the invention.
- the bispecific antibodies and bispecific antigen-binding fragments provided by the present invention include an antigen-binding domain that is a binding molecule capable of binding the Lrig-1 protein according to the present invention, and an antigen-binding domain capable of binding to other target proteins.
- the antigen-binding domain capable of binding to another target protein is a protein other than the Lrig-1 protein, but is not limited thereto, and may be, for example, an antigen-binding domain capable of binding PD-1 or a cell surface receptor. However, it is not limited thereto.
- Bispecific antibodies and bispecific antigen binding fragments according to the invention may be of any suitable format, e.g., Kontermann MAbs 2012, 4 (2): 182-197, incorporated herein by reference in its entirety. It can be provided in the format described in.
- a bispecific antibody or bispecific antigen binding fragment can be a bispecific antibody conjugate (e.g., IgG2, F (ab ') 2 or CovX-body), a bispecific IgG or IgG-type molecule (e.g.
- the method for producing the bispecific antibody in the present invention is, for example, Segal and Bast, 2001. Production of Bispecific Antibodies.Current Protocols in Immunology. 14: IV: incorporated herein by reference in its entirety. 2.13: 2.13.1-2.13.16), including reducing disulfide or non-reducing thioether linkages and chemical crosslinking of antibodies or antibody fragments.
- SPDP N-succinimidyl-3-(-2-pyridyldithio) -propionate
- SPDP N-succinimidyl-3-(-2-pyridyldithio) -propionate
- SPDP N-succinimidyl-3-(-2-pyridyldithio) -propionate
- SPDP N-succinimidyl-3-(-2-pyridyldithio) -propionate
- ab disulfide linked bispecific F
- It can be used to chemically crosslink
- bispecific antibody in the present invention see, for example, DM and Bast, BJ 2001. Production of Bispecific Antibodies.Current Protocols in Immunology. 14: IV: 2.13: 2.13 .1-2.13.16), comprising fusing antibody-producing hybridomas, e.g., polyethylene glycol, to produce quadroma cells capable of secreting bispecific antibodies.
- antibody-producing hybridomas e.g., polyethylene glycol
- Bispecific antibodies and bispecific antigen binding fragments according to the invention are also described in, for example, Antibody Engineering: Methods and Protocols, Second Edition (Humana Press, 2012, both of which are incorporated herein by reference in their entirety. ), at Chapter 40: Production of Bispecific Antibodies: Diabodies and Tandem scFv (Hornig and Farber-Schwarz), or French, How to make bispecific antibodies, Methods Mol. Med. 2000; 40: 333-339), For example, it can be produced recombinantly by expression from a nucleic acid construct encoding a polypeptide for an antigen-binding molecule.
- two antigen binding domains i.e., light and heavy chain variable domains for antigen binding domains capable of binding PD-1, etc.
- DNA constructs comprising sequences encoding light chain and heavy chain variable domains for) and encoding suitable linkers or dimerization domains between antigen binding domains can be prepared by molecular cloning techniques.
- Recombinant bispecific antibodies can then be produced by expression of the construct (eg, in vitro) in a suitable host cell (eg, a mammalian host cell), and then the expressed recombinant bispecific antibody can be optionally purified.
- Antibodies can be produced by an affinity maturation process that results in a modified antibody with improved affinity for the antibody relative to the antigen as compared to the unmodified parent antibody.
- Affinity matured antibodies are described in the art, for example, Marks et al., Rio / Technology 10: 779-783 (1992); Barbas et al. Proc Nat. Acad. Sci. USA 91: 3809- 3813 (1994); Schier et al. Gene 169: 147-155 (1995); Yelton et al. J. Immunol. 155: 1994-2004 (1995); Jackson et al., J. Immunol. 154 (7): 3310-159 (1995); and Hawkins et al, J. Mol. Biol. 226: 889-896 (1992).
- the binding molecule provided in the present invention may include a variant of the amino acid sequence.
- the amino acid sequence of the antibody can be altered to improve the binding affinity and / or other biological properties of the antibody. Such modifications include, for example, deletion, insertion and / or substitution of amino acid sequence residues of the antibody.
- amino acid variations are made based on the relative similarity of amino acid side chain substituents, such as hydrophobicity, hydrophilicity, charge, size, and the like.
- amino acid side chain substituents such as hydrophobicity, hydrophilicity, charge, size, and the like.
- arginine, lysine and histidine are all positively charged residues; Alanine, glycine and serine have similar sizes; It can be seen that phenylalanine, tryptophan and tyrosine have similar shapes. Therefore, based on these considerations, arginine, lysine and histidine; Alanine, glycine and serine; And phenylalanine, tryptophan, and tyrosine are biologically equivalent functions.
- each amino acid is assigned a hydrophobicity index according to hydrophobicity and charge: isoleucine (+4.5); Valine (+4.2); Leucine (+3.8); Phenylalanine (+2.8); Cysteine / cysteine (+2.5); Methionine (+1.9); Alanine (+1.8); Glycine (-0.4); Threonine (-0.7); Serine (-0.8); Tryptophan (-0.9); Tyrosine (-1.3); Proline (-1.6); Histidine (-3.2); Glutamate (-3.5); Glutamine (-3.5); Aspartate (-3.5); Asparagine (-3.5); Lysine (-3.9); And arginine (-4.5).
- the hydrophobic amino acid index is very important in conferring the protein's interactive biological function. It is well known that amino acids with similar hydrophobic indices can be replaced to retain similar biological activity. When introducing a variation with reference to the hydrophobicity index, substitution is performed between amino acids showing a hydrophobicity index difference of preferably within ⁇ 2, more preferably within ⁇ 1, even more preferably within ⁇ 0.5.
- Amino acid exchange in proteins that do not entirely alter the activity of the molecule is known in the art (H. Neurath, R.L.Hill, The Proteins, Academic Press, New York (1979)).
- the most common exchanges are amino acid residues Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Gln / Glu.
- binding molecule of the present invention is interpreted to also include a sequence showing substantial identity with the sequence listed in the sequence listing.
- the term "substantially identical" means that the sequence of the present invention is parallel to any other sequence for maximum correspondence, and when the parallel sequence is analyzed using an algorithm commonly used in the art, at least 61%. Refers to a sequence that exhibits homology, more preferably 70% homology, even more preferably 80% homology, and most preferably 90% homology. Alignment methods for sequence comparison are known in the art. Various methods and algorithms for alignment can be found in Smith and Waterman, Adv. Appl. Math. 2: 482 (1981); Needleman and Wunsch, J. Mol. Bio. 48: 443 (1970); Pearson and Lipman, Methods in Mol. Biol.
- the binding molecule preferably the antibody
- the binding molecule can be produced by a conventional method for producing an antibody, but can be produced by affinity maturation.
- affinity maturation refers to a process in which activated B cells produce antibodies with increased affinity for antigens in the course of an immune response.
- affinity maturation can generate antibodies or antibody fragments produced due to affinity maturation based on the principles of mutation and selection, similar to processes that occur in nature.
- the binding molecule provided in the present invention preferably an antibody, effectively activates the function of regulatory T immune cells among immune cells, increases the number of cells, and controls immune tolerance to effectively prevent immune-related diseases. , Can be improved or cured.
- the "immune-related disease” is a disease induced by excessive activation and expression of various immune cells and inflammatory cells, for example, autoimmune disease; Graft-versus-host disease; Organ transplant rejection; asthma; atopy; Or it may be an acute or chronic inflammatory disease, but is not limited thereto.
- the "autoimmune disease" in the present invention is rheumatoid arthritis, systemic scleroderma, systemic lupus erythematosus, atopic dermatitis, psoriasis, alopecia areata, asthma, Crohn's disease, Behcet's disease, Sjogren's syndrome, Gilia-Barre syndrome, chronic It may be one or more selected from the group consisting of thyroiditis, multiple sclerosis, multiple myositis, ankylosing spondylitis, fibrotitis and nodular multiple arteritis, but is not limited thereto.
- nucleic acid molecule encoding the binding molecule provided in the present invention.
- the nucleic acid molecule of the present invention includes all of the nucleic acid molecules translated from the amino acid sequence of the binding molecule provided in the present invention to a polynucleotide sequence as known to those skilled in the art. Therefore, various polynucleotide sequences can be prepared by an ORF (open reading frame), which is also included in the nucleic acid molecule of the present invention.
- ORF open reading frame
- an expression vector into which the isolated nucleic acid molecule provided in the present invention is inserted.
- the "vector” is a nucleic acid molecule capable of transporting another nucleic acid to which a nucleic acid molecule is linked.
- a vector is a "plasmid” that refers to a circular double-stranded DNA where additional DNA segments can be ligated.
- a phage vector is another type of vector.
- a viral vector in which additional DNA segments can be ligated to the viral genome.
- vectors eg, non-episomal mammalian vectors
- vectors can be integrated into the host cell's genome upon entry into the host cell, thereby replicating with the host genome.
- some vectors are capable of directing the expression of genes to which they are linked in the operational dimension.
- Such vectors are referred to herein as “recombinant expression vectors” or simply “expression vectors”.
- expression vectors useful in recombinant DNA techniques are often present in the form of plasmids.
- plasmid and vector can be used interchangeably, because plasmid is the most commonly used form of vector.
- the expression vector in the present invention commercially widely used pCDNA vector, F, R1, RP1, Col, pBR322, ToL, Ti vector; Cosmid; Phages such as lambda, lambdoid, M13, Mu, p1 P22, Q ⁇ , T-even, T2, T3, T7; It may be selected from the group consisting of plant viruses, but is not limited thereto, and any expression vector known as an expression vector to those skilled in the art can be used in the present invention, and when selecting an expression vector, depends on the properties of the target host cell.
- a vector When a vector is introduced into a host cell, it may be performed by calcium phosphate transfection, viral infection, DEAE-dextran regulatory transfection, lipofectamine transfection, or electroporation, but is not limited thereto.
- An introduction method suitable for the expression vector and the host cell can be selected and used.
- the vector contains one or more selection markers, but is not limited thereto, and selection is possible according to whether a product is produced using a vector not including the selection marker.
- the selection of the selection marker is selected by the desired host cell, which uses methods already known to those skilled in the art, so the present invention is not limited to this.
- a tag sequence may be inserted into an expression vector and fused.
- the tags include, but are not limited to, hexa-histidine tags, hemagglutinin tags, myc tags, or flag tags. Any tag that facilitates purification known to those skilled in the art can be used in the present invention.
- the expression vector provided in the present invention provides a host cell line transfected.
- host cell in the present invention includes individual cells or cell cultures that may or may not be the recipient of the vector (s) for incorporation of the polypeptide insert.
- Host cells include progeny of a single host cell, which progeny may not necessarily be completely identical (in morphological or genomic DNA complements) to the original parental cell due to natural, accidental or intentional mutation.
- Host cells include cells transfected with the polypeptide (s) herein.
- the host cell may include cells of mammalian, plant, insect, fungal or cellular origin, for example, bacterial cells such as E. coli, Streptomyces, Salmonella typhimurium; Fungal cells such as yeast cells and Pichia pastoris; Insect cells such as Drozophila and Spodoptera Sf9 cells; Chinese hamster ovary cells (CHO), SP2 / 0 (mouse myeloma), human lymphoblastoid, COS, NSO (mouse myeloma), 293T, Bow melanoma cells, HT-1080, BHK (Baby Hamster Kidney Cells), animal cells of HEK (Human Embryonic Kidney Cells) or PERC.6 (Human Retinal Cells); Or it may be a plant cell, but is not limited thereto, and any cell that can be used as a host cell line known to those skilled in the art can be used.
- bacterial cells such as E. coli, Strepto
- the transfection method is an arbitrary method for injecting a desired vector into the host cell, and any known method capable of injecting the vector into the host cell may be included.
- a method using CaCl 2 Electroporation, microinjection, calcium phosphate precipitation, electroporation, liposome-mediated transfection, DEAE-dextran treatment, gene bombardment and virus transfection, etc. can be used, but are not limited to this. It is not.
- an antibody-drug conjugate comprising an antibody and a drug provided by the present invention is provided.
- the "antibody-drug conjugate (ADC)" refers to a form in which a drug and an antibody are chemically linked without lowering the biological activity of the antibody and the drug.
- the antibody-drug conjugate is a form in which the drug is bound to the N-terminal amino acid residue of the heavy and / or light chain of the antibody, specifically, the N-terminal or ⁇ -amine group of the heavy and / or light chain of the antibody. Refers to this combined form.
- the "drug” may mean any substance having a specific biological activity in a cell, which is a concept including DNA, RNA, or peptide.
- the drug may be in the form of a reactor capable of crosslinking by reacting with an ⁇ -amine group, and also includes a form in which a linker including a reactor capable of crosslinking by reacting with an ⁇ -amine group is linked.
- Examples of the reactive group capable of crosslinking by reacting with the ⁇ -amine group in the present invention are not particularly limited as long as they are capable of reacting and crosslinking by reacting with the N-terminal ⁇ -amine group of the heavy or light chain of the antibody. All kinds of reactions with known amine groups are included. Examples include isothiocyanate, isocyanates, acyl azide, NHS ester, sulfonyl chloride, aldehyde, glyoxal, Epoxide, Oxirane, Carbonate, Aryl halide, Imidoester, Carbodiimide, Anhydride and Fluorophenyl Ester ester), but is not limited thereto.
- the drug is included irrespective of its type, as long as it is a drug capable of treating a disease targeted by the Lrig-1 antibody, but is preferably an immune-related disease, for example, autoimmune disease, graft-versus-host disease , Organ transplant rejection, asthma, atopy, or acute or chronic inflammatory disease.
- an immune-related disease for example, autoimmune disease, graft-versus-host disease , Organ transplant rejection, asthma, atopy, or acute or chronic inflammatory disease.
- the binding molecule provided in the present invention provides a pharmaceutical composition for the prevention or treatment of immune-related diseases comprising an antibody-drug conjugate (Antibody-Drug Conjugate, ADC) as an active ingredient.
- ADC Antibody-Drug Conjugate
- the binding molecule provided in the present invention preferably an antibody, effectively activates the function of regulatory T immune cells among immune cells, increases the number of cells, and controls immune tolerance to effectively prevent immune-related diseases. , Can be improved or cured.
- the "immune-related disease” is a disease induced by excessive activation and expression of various immune cells and inflammatory cells, for example, autoimmune disease; Graft-versus-host disease; Organ transplant rejection; asthma; atopy; Or it may be an acute or chronic inflammatory disease, but is not limited thereto.
- the "autoimmune disease" in the present invention is rheumatoid arthritis, systemic scleroderma, systemic lupus erythematosus, atopic dermatitis, psoriasis, alopecia areata, asthma, Crohn's disease, Behcet's disease, Sjogren's syndrome, Gilia-Barre syndrome, chronic It may be one or more selected from the group consisting of thyroiditis, multiple sclerosis, multiple myositis, ankylosing spondylitis, fibrotitis and nodular multiple arteritis, but is not limited thereto.
- prevention may include, without limitation, any action to block or suppress or delay the symptoms of a disease using the pharmaceutical composition of the present invention.
- treatment may include, without limitation, any action that improves or benefits symptoms of a disease using the pharmaceutical composition of the present invention.
- the pharmaceutical composition may be characterized in that it is in the form of capsules, tablets, granules, injections, ointments, powders or beverages, and the pharmaceutical composition may be characterized for humans.
- the pharmaceutical composition is not limited to these, but may be used in the form of oral dosage forms such as powders, granules, capsules, tablets, aqueous suspensions, external preparations, suppositories, and sterile injection solutions, respectively, according to a conventional method. You can.
- the pharmaceutical composition of the present invention may include a pharmaceutically acceptable carrier.
- Pharmaceutically acceptable carriers may include binders, lubricants, disintegrants, excipients, solubilizers, dispersants, stabilizers, suspending agents, pigments, fragrances, etc. when administered orally, and in the case of injections, buffers, preservatives, painless Agents, solubilizers, isotonic agents, stabilizers, etc.
- the formulation of the pharmaceutical composition of the present invention can be variously prepared by mixing with a pharmaceutically acceptable carrier as described above.
- a pharmaceutically acceptable carrier for example, when administered orally, tablets, troches, capsules, elixirs, suspensions, syrups, wafers, etc. may be prepared, and in the case of injection, unit dosage ampoules or multiple doses may be prepared. have.
- Others can be formulated as solutions, suspensions, tablets, capsules, sustained-release preparations, and the like.
- examples of carriers, excipients and diluents suitable for formulation include lactose, dextrose, sucrose, sorbitol, mannitol, xylitol, erythritol, malditol, starch, acacia rubber, alginate, gelatin, calcium phosphate, calcium silicate, Cellulose, methyl cellulose, microcrystalline cellulose, polyvinylpyrrolidone, water, methylhydroxybenzoate, propylhydroxybenzoate, talc, magnesium stearate or mineral oil and the like can be used.
- fillers, anti-coagulants, lubricants, wetting agents, fragrances, emulsifiers, preservatives and the like may be further included.
- the route of administration of the pharmaceutical composition to the present invention is not limited to these, but oral, intravenous, intramuscular, intraarterial, intramedullary, intrathecal, intracardiac, transdermal, subcutaneous, intraperitoneal, intranasal, intestinal, topical, This includes sublingual or rectal. Oral or parenteral administration is preferred.
- the "parenteral" includes subcutaneous, intradermal, intravenous, intramuscular, intraarticular, synovial sac, intrasternal, intrathecal, intralesional and intracranial injection or infusion techniques.
- the pharmaceutical composition of the present invention may also be administered in the form of suppositories for rectal administration.
- the pharmaceutical composition of the present invention depends on a number of factors, including the activity, age, weight, general health, sex, diet, administration time, route of administration, release rate, drug combination and severity of the particular disease to be prevented or treated, of the specific compound used. It may vary, and the dosage of the pharmaceutical composition varies depending on the patient's condition, weight, disease severity, dosage form, administration route and duration, but can be appropriately selected by those skilled in the art, and 0.0001 to 50 mg / kg per day Or it can be administered at 0.001 to 50mg / kg. The administration may be administered once a day, or may be divided into several times. The above dosage does not limit the scope of the present invention in any case.
- the pharmaceutical composition according to the present invention may be formulated as pills, dragees, capsules, liquids, gels, syrups, slurries, suspensions.
- the binding molecule provided by the present invention to the subject; Or it provides a method for preventing, improving or treating an immune-related disease, comprising administering an antibody-drug conjugate (Antibody-Drug Conjugate, ADC) in a pharmaceutically effective amount.
- ADC Antibody-Drug Conjugate
- the binding molecule provided in the present invention preferably an antibody, effectively activates the function of regulatory T immune cells among immune cells, increases the number of cells, and controls immune tolerance to effectively prevent immune-related diseases. , Can be improved or cured.
- the "individual” is a subject suspected of developing an immune-related disease, and the subject suspected of developing the cancer or immune-related disease is a mammal including a mouse, livestock, etc., including humans, who may or may develop the disease.
- the method of the present invention is a binding molecule provided in the present invention; Or administering an antibody-drug conjugate in a pharmaceutically effective amount.
- a suitable total daily dosage may be determined by the treating physician within the correct medical judgment range, and may be administered once or several times.
- a specific therapeutically effective amount for a particular patient is a composition and the specific composition of the active ingredient, the age of the patient, including the type and extent of the reaction to be achieved and, in some cases, other agents being used.
- the present invention is not limited thereto, and the method for preventing or treating the immune-related disease may be a combination therapy further comprising administering a compound or a substance having therapeutic activity for one or more diseases.
- the “combination” refers to simultaneous, separate or sequential administration. If the administration is sequential or individual, the interval between the administration of the secondary components should be such that the beneficial effects of the combination are not lost.
- the dose of the antibody-drug conjugate (ADC) may be about 0.0001 ⁇ g to 500 mg per kg of patient body weight, but is not limited thereto.
- a binding molecule preferably an antibody, specific for the Lrig-1 protein according to the present invention activates the function of regulatory T cells, increases the number of cells, and modulates immune tolerance to various immune cells and inflammatory cells As a disease induced by the excessive activation and expression of, effective immune diseases such as autoimmune disease, graft-versus-host disease, organ transplant rejection, asthma, atopy, or acute or chronic inflammatory disease It can be prevented, improved or treated.
- effective immune diseases such as autoimmune disease, graft-versus-host disease, organ transplant rejection, asthma, atopy, or acute or chronic inflammatory disease It can be prevented, improved or treated.
- a binding molecule specific to the Lrig-1 protein according to the present invention preferably an antibody
- Figure 1 shows the structure of the Lrig-1 protein according to an embodiment of the present invention.
- FIG. 2 shows the structure of the Lrig-1 protein according to an embodiment of the present invention.
- Figure 3 shows the results of predicting the antigenic determinant (epitope) of the Lrig-1 protein according to an embodiment of the present invention.
- Figure 4 shows the results of predicting the antigenic determinant (epitope) of the Lrig-1 protein according to an embodiment of the present invention.
- FIG. 5 shows the expression level of Lrig-1 mRNA according to an embodiment of the present invention.
- Figure 6 shows the expression level of Lrig-1 mRNA according to an embodiment of the present invention.
- FIG. 7 shows the expression level of Lrig-1 mRNA according to an embodiment of the present invention.
- Figure 8 shows the expression level of Lrig-1, Lrig-2 and Lrig-3 mRNA according to an embodiment of the present invention.
- Figure 9 shows the result of comparing the expression level of Lrig-1 protein in regulatory T cells and non-regulating T cells according to an embodiment of the present invention.
- FIG 10 shows the expression of Lrig-1 protein on the surface of regulatory T cells according to an embodiment of the present invention.
- Figure 11 shows the results of analyzing the binding force of Lrig-1 protein of Lrig-1 protein specific monoclonal antibodies (A7, C8, E7 and G3) according to an embodiment of the present invention.
- Lrig-1 protein-specific monoclonal antibody (A7, C8, E7, and G3) according to an embodiment of the present invention shows the results of analyzing the mechanism of regulation of Lrig-1 protein-induced Stat3 phosphorylation in T cells will be.
- Figure 13 shows the results of analyzing the therapeutic effect of autoimmune diseases of Lrig-1 protein specific monoclonal antibodies (A7, C8, E7 and G3) according to an embodiment of the present invention.
- a heavy chain variable region comprising a heavy chain CDR1 represented by SEQ ID NO: 5, a heavy chain CDR2 represented by SEQ ID NO: 6, and a heavy chain CDR3 represented by SEQ ID NO: 7;
- a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 8, a light chain CDR2 represented by SEQ ID NO: 9, and a light chain CDR3 represented by SEQ ID NO: 10;
- a heavy chain variable region comprising a heavy chain CDR1 represented by SEQ ID NO: 21, a heavy chain CDR2 represented by SEQ ID NO: 22, and a heavy chain CDR3 represented by SEQ ID NO: 23;
- a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 24, a light chain CDR2 represented by SEQ ID NO: 25, and a light chain CDR3 represented by SEQ ID NO: 26;
- a heavy chain variable region comprising a heavy chain CDR1 represented by SEQ ID NO: 29, a heavy chain CDR2 represented by SEQ ID NO: 30, and a heavy chain CDR3 represented by SEQ ID NO: 31; And a light chain variable region comprising a light chain CDR1 represented by SEQ ID NO: 32, a light chain CDR2 represented by SEQ ID NO: 33, and a light chain CDR3 represented by SEQ ID NO: 34; a binding molecule selected from the group consisting of to provide.
- Th0, Th1, Th2, Th17 and iTreg a subset of T cells, were prepared.
- the iTreg refers to cells artificially induced differentiation in a medium containing the following composition.
- T cells The subtype of T cells was first isolated from naive T cells obtained from rat spleens, followed by RPMI1640 (Invitrogen Gibco, Grand Island, NY) containing 10% of fetal bovine serum (FBS; hyclone, logan, UT). Differentiation was induced to each cell through cultivation for 72 hours in a 37 ° C, 5% CO 2 incubator by further including the components shown in Table 1 below in the nutrient medium.
- FBS fetal bovine serum
- Lrig-1 protein a surface protein of regulatory T cells, a three-dimensional conformation of the extracellular domain of Lrig-1 protein was predicted.
- LRR1 to LRR15 a total of 15 leucine rich regions (Lucine rich regions) of LRR1 to LRR15 existed in the Lrig-LRR domain (amino acid sequences 41 to 494) among the extracellular domains of the Lrig-1 protein.
- LRR domains were composed of 23 to 27 amino acids, and 3 to 5 leucine were present.
- three immunoglobulin-like domains exist in amino acid sequences 494 to 781 of the Lrig-1 protein among the extracellular domains of the Lrig-1 protein.
- Ellipro server http://tools.iedb.org/ellipro/
- the Ellipro search engine used the corresponding search engine known to be the most reliable among the algorithms for predicting existing antigenic determinants.
- Example 2 After inputting the extracellular domain analyzed in Example 1 into the antigenic determinant prediction software, the predicted contiguous or discontinuous amino acid sequence of the predicted antigenic determinant is shown in FIGS. 3 and 4.
- Antibodies specific to the Lrig-1 protein according to the present invention were produced. This antibody did not produce a specific antigenic determinant, but produced an antibody capable of binding to any region of the Lrig-1 protein.
- Lrig-1 protein In order to construct the antibody, cells expressing Lrig-1 protein were produced. More specifically, after cutting the DNA fragment and pcDNA (hygro) corresponding to SEQ ID NO: 2 with a cleavage enzyme, culturing at 37 ° C. to ligation to insert the DNA sequence of the Lrig-1 protein (insert). A pcDNA was prepared. The produced pcDNA having the inserted SEQ ID NO: 2 was introduced through transfection into L cells so that Lrig-1 protein could be expressed on the surface of L cells.
- pcDNA hygro
- the sequences of the light chain (heavy chain) and light chain (heavy chain) amino acids capable of binding to the Lrig-1 expressed on the cell surface were selected from the human scFv library, and a total of 8 heavy and light chains were selected.
- the selected heavy and light chain amino acid sequences were fused with the mlgG2a Fc region to produce a monoclonal antibody.
- the sequence of the monoclonal antibody is shown in Table 2 below.
- Lrig-1 protein can act as a biomarker specific for regulatory T cells.
- CD4 + T cells were isolated from the spleen of the mouse using a magnet-activated cell sorting (MACS) via CD4 beads. Subsequently, control T (CD4 + CD25 + T) cells and unregulated T (CD4 + CD25 - T) cells were isolated using a fluorescently activated cell sorter (FACS) using a CD25 antibody. Each cell and the cells differentiated in Preparation Example 1 were extracted with mRNA using Trizol, and then genomic RNA was removed using gDNA extraction kit (Qiagen) to remove gDNA by a protocol provided by the company. . mRNA with gDNA removed was synthesized with cDNA through the BDsprint cDNA synthesis kit (Clonetech).
- the real-time polymerase chain reaction was performed using SYBR Green (Molecular Probes) under the conditions of 40 cycles at 95 ° C for 3 minutes, 61 ° C for 15 seconds, and 72 ° C for 30 seconds by a protocol provided by a company. It was carried out using primers, and the relative gene expression was calculated using the ⁇ CT method, and normalized using HPRT, and the results are shown in FIGS. 5 to 8.
- the unregulated T (CD4 + CD25 - T) as compared to control cells T (CD4 + CD25 + T) 18.1 times the expression of Lrig-1 in the cell it can be seen that high.
- This expression level was about 10 times higher than that of the previously known markers of regulatory T cells, Lag3 and Ikzf4.
- Lrig-1 was highest among Lrig-1, Lrig-2 and Lrig-3 corresponding to the Lrig family.
- the Lrig-1 protein according to the present invention is specifically expressed in regulatory T cells, particularly naturally occurring regulatory T cells.
- Lrig-1 protein expressed from Lrig-1 mRNA was specifically expressed only in regulatory T cells.
- a magnetically active cell sorter (magnet-activated) from the spleen of the mouse to CD4 beads using FOXP3-RFP-infused (Knock-in) mice bound with a red fluorescence protein (RFP) to the FOXP3 promoter, a regulatory T cell-specific transcription factor.
- CD4 + T cells were isolated using cell sorting (MACS). Then, using the RFP protein, it was obtained by separating regulatory T (CD4 + RFP + T) cells and non-regulating T (CD4 + RFP - T) through a fluorescence-activated cell sorter (FACS). Each of the cells, the purchased Lrig-1 antibody and the negative control were stained through an isotype to measure the expression level of Lrig-1 with a fluorescence-activated cell sorter, and the results are shown in FIG. 9.
- the Lrig-1 protein according to the present invention is specifically expressed in regulatory T cells.
- the Lrig-1 protein In order for the Lrig-1 protein to be targeted for cell therapy, it must be expressed on the surface of regulatory T cells for more effective target treatment, so it was confirmed whether Lrig-1 protein was expressed on the surface.
- the differentiated T cell subtypes of Preparation Example 1 were stained with anti-CD4-APC and anti-Lrig-1-PE antibodies, and each cell surface using a fluorescence-activated cell sorter (FACS). The expression level of Lrig-1 was measured at, and the results are shown in FIG. 10.
- activated T cells As shown in Figure 10, activated T cells, activated T cells, Th1 cells, Th2 cells, Th17 cells, and naive (Naive) cells, the expression of Lrig-1 is expressed in an amount of 0.77 to 15.3, whereas differentiation In the induced T cells (iTreg), 83.9 was highly expressed.
- the Lrig-1 protein according to the present invention is not only specifically expressed in regulatory T cells (Treg) cells, but also more particularly expressed on the surface of Treg cells.
- each of the antibodies of Preparation Examples 1 to 8 was expressed in L cells stably expressing Lrig-1. After binding, a mouse antibody can be recognized, and eFlour 670 is put into a conjugated secondary antibody, and then FACS is used to analyze the binding capacity of the monoclonal antibody to the Lrig-1 protein. 11 is shown.
- Lrig-1 protein specific monoclonal antibodies (A7, C8, E7, and G3) according to the present invention effectively recognize and bind to Lrig-1 protein present on the surface of L cells. .
- the antibodies of Preparation Examples 1 to 8 are Treg cells. After stimulation of Lrig-1 present on the surface of the Treg cells by treatment with, the degree of tyrosine phosphorylation of the Stat3 protein present in the Treg cells stimulated by phosphotyrosine immunoblot was analyzed and , The results are shown in FIG. 12.
- Lrig-1 protein-specific monoclonal antibodies (A7, C8, E7 and G3) according to the present invention were confirmed to increase the phosphorylation (phosphorylation) of Stat3 to the same level as Th17 cells.
- Lrig-1 protein-specific monoclonal antibody (A7, C8, E7, and G3) according to the present invention significantly inhibits the effect of reducing weight in inflammatory bowel disease-induced mice.
- Lrig-1 protein-specific monoclonal antibody is an autoimmune disease induced by excessive activation and expression of various immune cells and inflammatory cells, graft versus host disease, organ transplant rejection, asthma, It can be seen that it is possible to effectively prevent, ameliorate or treat immune-related diseases such as atopy or acute or chronic inflammatory diseases.
- the present invention is a binding molecule capable of specifically binding to Lrig-1 (leucine-rich and immunoglobulin-like domains 1) protein, which is a protein present on the surface of a regulatory T cell (Treg cell), and uses thereof , Autoimmune disease, graft-versus-host disease, organ transplant rejection, asthma, atopy, or acute or chronic inflammatory disease.
- Lrig-1 leucine-rich and immunoglobulin-like domains 1
- Reg cell regulatory T cell
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Abstract
Description
분화 세포 | 조성 |
Th0 | anti-CD3, anti-CD28 |
Th1 | IL-12, anti-IL-4 항체 |
Th2 | IL-4, anti-IFNβ |
Th17 | IL-6, TGFβ, anti-IFNβ, anti-IL-4 |
iTreg | IL-2, TGFβ |
구분 | 클론 | 위치 | 아미노산 서열 | 서열정보 |
제조예 1 | A7 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSGYDMSWVRQAPGKGLEWVSLIYPDSGNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDAGLSWAGAFDYWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | 서열번호 45 |
경쇄 | QSVLTQPPSASGTPGQRVTISCSGSSSNIGSNYVTWYQQLPGTAPKLLIYSDSHRPSGVPDRFSGSKSGTSASLAISGLQSEDEADYYCGSWDYSLSAYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | 서열번호 46 | ||
제조예 2 | C8 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSNYYMSWVRQAPGKGLEWVSGISPGDSSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKGLYSNPNEPFDYWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | 서열번호 47 |
경쇄 | QSVLTQPPSASGTPGQRVTISCTGSSSNIGSNYVSWYQQLPGTAPKLLIYDDSQRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCGTWDYSLNGYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | 서열번호 48 | ||
제조예 3 | E7 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYDMSWVRQAPGKGLEWVSGISPDGSNIYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKVGLRCRYEACSYAYGMDVWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | 서열번호 49 |
경쇄 | QSVLTQPPSASGTPGQRVTISCSGSSSNIGSNYVSWYQQLPGTAPKLLIYSDSHRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCATWDSSLNGYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | 서열번호 50 | ||
제조예 4 | G3 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSNYDMSWVRQAPGKGLEWVSSISPSSGSIYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKDLDAFWRPSFDYWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | 서열번호 51 |
경쇄 | QSVLTQPPSASGTPGQRVTISCTGSSSNIGNNNVNWYQQLPGTAPKLLIYSDSHRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCGSWDDSLSAYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | 서열번호 52 | ||
제조예 5 | A8 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSDYDMSWVRQVPGKGLEWVSWISHGGGSIYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARGLGLCKTGLCYYYDAMDVWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | - |
경쇄 | QSVLTQPPSASGTPGQRVTISCTGSSSNIGNNSVTWYQQLPGTAPKLLIYADNNRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCAAWDSSLSAYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | - | ||
제조예 6 | B8 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSDYYMSWVRQAPGKGLEWVSGISHDSGSKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARHWTTFDYWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | - |
경쇄 | QSVLTQPPSASGTPGQRVTISCSGSSSNIGSNNVTWYQQLPGTAPKLLIYANSNRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCGAWDYSLSAYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | - | ||
제조예 7 | D9 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSNYAMSWVRQAPGKGLEWVSAIYPGGGSIYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDILPCPWGRCYYDYAMDVWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | - |
경쇄 | QSVLTQPPSASGTPGQRVTISCSDSSSNIGSNTVSWYQQLPGTAPKLLIYADNNRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCGTWDYSLSGYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | - | ||
제조예 8 | H6 clone | 중쇄 | EVQLLESGGGLVQPGGSLRLSCAASGFTFSNYAMSWVRQAPGKGLEWVSVISHGGGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARVISNCHLGVCYYSNGMDVWGQGTLVTVSSTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEEEMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK | - |
경쇄 | QSVLTQPPSASGTPGQRVTISCSGSSSNIGNNDVYWYQQLPGTAPKLLIYSDSQRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCGTWDYSLSGYVFGGGTKLTVLRTVAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC | - |
프라이머 | 서열 |
쥐 Lrig-1 | Forward 5' - GAC GGA ATT CAG TGA GGA GAA CCT - 3' |
Reverse 5' - CAA CTG GTA GTG GCA GCT TGT AGG - 3' | |
쥐 Lrig-2 | forward 5' - TCA CAA GGA ACA TTG TCT GAA CCA- 3' |
reverse 5' - GCC TGA TCT AAC ACA TCC TCC TCA- 3' | |
쥐 Lrig-3 | forward 5' - CAG CAC CTT GAG CTG AAC AGA AAC - 3' |
reverse 5' - CCA GCC TTT GGT AAT CTC GGT TAG - 3' | |
쥐 FOXP3 | forward 5' - CTT TCA CCT ATC CCA CCC TTA TCC - 3' |
reverse 5' - ATT CAT CTA CGG TCC ACA CTG CTC - 3' | |
ACTG1 | forward 5' - GGC GTC ATG GTG GGC ATG GG - 3' |
reverse 5' - ATG GCG TGG GGA AGG GCG TA - 3' |
Claims (25)
- Lrig-1(leucine-rich and immunoglobulin-like domains 1) 단백질에 특이적으로 결합하는 결합 분자로서,상기 결합 분자는, 서열번호 5, 13, 21 및 29로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 중쇄 CDR1; 서열번호 6, 14, 22 및 30으로 표시되는 군에서 선택된 아미노산 서열로 이루어지는 중쇄 CDR2; 서열번호 7, 15, 23 및 31로 표시되는 군에서 선택된 아미노산 서열로 이루어지는 중쇄 CDR3;을 포함하는 중쇄 가변 영역; 및서열번호 8, 16, 24 및 32로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 경쇄 CDR1; 서열번호 9, 17, 25 및 33으로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 경쇄 CDR2; 서열번호 10, 18, 26 및 34로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 경쇄 CDR3;를 포함하는 경쇄 가변 영역을 포함하는 것인, 결합 분자.
- 제1항에 있어서,상기 Lrig-1 단백질은 서열번호 1 또는 3으로 표시되는 아미노산 서열로 이루어지는 것인, 결합 분자.
- 제1항에 있어서,상기 Lrig-1 단백질은 서열번호 2 또는 4로 표시되는 폴리뉴클레오티드에 의해 코딩되는 것인, 결합 분자.
- 제1항에 있어서,상기 결합 분자는,(a) 서열번호 5로 표시되는 중쇄 CDR1, 서열번호 6으로 표시되는 중쇄 CDR2, 및 서열번호 7로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역;(b) 서열번호 13으로 표시되는 중쇄 CDR1, 서열번호 14로 표시되는 중쇄 CDR2, 및 서열번호 15로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역;(c) 서열번호 21로 표시되는 중쇄 CDR1, 서열번호 22로 표시되는 중쇄 CDR2, 및 서열번호 23으로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역; 및(d) 서열번호 29로 표시되는 중쇄 CDR1, 서열번호 30으로 표시되는 중쇄 CDR2, 및 서열번호 31로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역;으로 이루어진 군에서 선택되는 중쇄 가변 영역; 및(e) 서열번호 8로 표시되는 경쇄 CDR1, 서열번호 9로 표시되는 경쇄 CDR2, 및 서열번호 10으로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역;(f) 서열번호 16으로 표시되는 경쇄 CDR1, 서열번호 17로 표시되는 경쇄 CDR2, 및 서열번호 18로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역;(g) 서열번호 24로 표시되는 경쇄 CDR1, 서열번호 25로 표시되는 경쇄 CDR2, 및 서열번호 26으로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역;(h) 서열번호 32로 표시되는 경쇄 CDR1, 서열번호 33으로 표시되는 경쇄 CDR2, 및 서열번호 34로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역;으로 이루어진 군에서 선택되는 경쇄 가변 영역;을 포함하는 것인, 결합 분자.
- 제1항에 있어서,상기 결합 분자는,(1) 서열번호 5로 표시되는 중쇄 CDR1, 서열번호 6으로 표시되는 중쇄 CDR2, 및 서열번호 7로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역; 및 서열번호 8로 표시되는 경쇄 CDR1, 서열번호 9로 표시되는 경쇄 CDR2, 및 서열번호 10으로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역을 포함하는 결합 분자;(2) 서열번호 13으로 표시되는 중쇄 CDR1, 서열번호 14로 표시되는 중쇄 CDR2, 및 서열번호 15로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역; 및 서열번호 16으로 표시되는 경쇄 CDR1, 서열번호 17로 표시되는 경쇄 CDR2, 및 서열번호 18로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역을 포함하는 결합 분자;(3) 서열번호 21로 표시되는 중쇄 CDR1, 서열번호 22로 표시되는 중쇄 CDR2, 및 서열번호 23으로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역; 및 서열번호 24로 표시되는 경쇄 CDR1, 서열번호 25로 표시되는 경쇄 CDR2, 및 서열번호 26으로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역을 포함하는 결합 분자;(4) 서열번호 29로 표시되는 중쇄 CDR1, 서열번호 30으로 표시되는 중쇄 CDR2, 및 서열번호 31로 표시되는 중쇄 CDR3를 포함하는 중쇄 가변 영역; 및 서열번호 32로 표시되는 경쇄 CDR1, 서열번호 33으로 표시되는 경쇄 CDR2, 및 서열번호 34로 표시되는 경쇄 CDR3를 포함하는 경쇄 가변 영역을 포함하는 결합 분자;로 이루어진 군에서 선택되는, 결합 분자.
- 제1항에 있어서,상기 결합 분자는,서열번호 11, 19, 27 및 35로 표시되는 군에서 선택되는 어느 하나의 아미노산 서열로 이루어지는 중쇄 가변 영역; 및서열번호 12, 20, 28 및 36으로 표시되는 군에서 선택되는 어느 하나의 아미노산 서열로 이루어지는 경쇄 가변 영역;을 포함하는 결합 분자.
- 제1항에 있어서,상기 결합 분자는,(i) 서열번호 11로 표시되는 중쇄 가변 영역, 및 서열번호 12로 표시되는 경쇄 가변 영역을 포함하는 결합 분자;(ii) 서열번호 19로 표시되는 중쇄 가변 영역, 및 서열번호 20으로 표시되는 경쇄 가변 영역을 포함하는 결합 분자;(iii) 서열번호 27로 표시되는 중쇄 가변 영역, 및 서열번호 28로 표시되는 경쇄 가변 영역을 포함하는 결합 분자; 및(iv) 서열번호 35로 표시되는 중쇄 가변 영역, 및 서열번호 36으로 표시되는 경쇄 가변 영역을 포함하는 결합 분자;로 이루어진 군에서 선택되는 결합 분자.
- 제1항에 있어서,상기 결합 분자는 Fc 영역 또는 불변 영역(constant region)을 더 포함하는, 결합 분자.
- 제9항에 있어서,상기 Fc 영역은 IgG1, IgG2, IgG3 또는 IgG4 항체의 Fc 영역, 또는 하이브리드 Fc(hybrid Fc) 영역인, 결합 분자.
- 제1항에 있어서,상기 결합 분자는, 서열번호 37, 39, 41, 42, 43, 44 및 53으로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 중쇄 불변 영역을 더 포함하는, 결합 분자.
- 제1항에 있어서,상기 결합 분자는, 서열번호 38 또는 40으로 표시되는 아미노산 서열로 이루어지는 경쇄 불변 영역을 더 포함하는, 결합 분자.
- 제1항에 있어서,상기 결합 분자는,서열번호 37로 표시되는 아미노산 서열로 이루어지는 중쇄 불변 영역; 및서열번호 38로 표시되는 아미노산 서열로 이루어지는 경쇄 불변 영역을 더 포함하는, 결합 분자.
- 제1항에 있어서,상기 결합 분자는,서열번호 39, 41, 42, 43 및 53으로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 중쇄 불변 영역; 및서열번호 40으로 표시되는 아미노산 서열로 이루어지는 경쇄 불변 영역을 더 포함하는, 결합 분자.
- 제1항에 있어서,상기 결합 분자는, 서열번호 44로 표시되는 아미노산 서열로 이루어지는 중쇄 불변 영역을 더 포함하는, 결합 분자.
- 제1항에 있어서,상기 결합 분자는,서열번호 45로 표시되는 중쇄, 및 서열번호 46으로 표시되는 경쇄를 포함하는 결합 분자;서열번호 47로 표시되는 중쇄, 및 서열번호 48로 표시되는 경쇄를 포함하는 결합 분자;서열번호 49로 표시되는 중쇄, 및 서열번호 50으로 표시되는 경쇄를 포함하는 결합 분자; 및서열번호 51로 표시되는 중쇄, 및 서열번호 52로 표시되는 경쇄를 포함하는 결합 분자;로 이루어진 군에서 선택되는 것인, 결합 분자.
- 제1항에 있어서,상기 결합 분자는 항체 또는 그 단편인, 결합 분자.
- 제16항에 있어서,상기 항체는 키메라 항체, 인간화 항체(humanized antibody), 이가(bivalent), 양특이성 분자, 미니바디(minibody), 도메인 항체, 이중특이적 항체(bispecific antibody), 항체 모방체, 유니바디(unibody), 디아바디(diabody), 트리아바디(triabody), 테트라바디(tetrabody) 또는 이의 단편인, 결합 분자.
- 제1항 내지 제17항 중 어느 한 항의 결합 분자를 코딩하는 핵산 분자.
- 제18항의 핵산 분자가 삽입된 발현 벡터.
- 제19항의 발현 벡터가 형질 감염된 숙주 세포주.
- 서열번호 5, 13, 21 및 29로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 중쇄 CDR1; 서열번호 6, 14, 22 및 30으로 표시되는 군에서 선택된 아미노산 서열로 이루어지는 중쇄 CDR2; 서열번호 7, 15, 23 및 31로 표시되는 군에서 선택된 아미노산 서열로 이루어지는 중쇄 CDR3;을 포함하는 중쇄 가변 영역; 및서열번호 8, 16, 24 및 32로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 경쇄 CDR1; 서열번호 9, 17, 25 및 33으로 표시되는 군에서 선택되는 아미노산 서열로 표시되는 경쇄 CDR2; 서열번호 10, 18, 26 및 34로 표시되는 군에서 선택되는 아미노산 서열로 이루어지는 경쇄 CDR3;를 포함하는 경쇄 가변 영역을 포함하는 항체; 및 약물을 포함하는 항체-약물 결합체.
- 제1항 내지 제17항 중 어느 한 항의 결합 분자를 유효 성분으로 포함하는 면역 관련 질환의 예방 또는 치료용 약학 조성물.
- 제22항에 있어서,상기 면역 관련 질환은 자가면역질환, 이식편대숙주 질환, 장기이식거부반응, 천식, 아토피, 또는 급성 또는 만성의 염증 질환인, 약학 조성물.
- 개체에게 제1항 내지 제17항 중 어느 한 항의 결합 분자를 약학적 유효량으로 투여하는 단계를 포함하는 면역 관련 질환의 예방 또는 치료 방법.
- 개체에게 제21항의 항체-약물 결합체를 약학적 유효량으로 투여하는 단계를 포함하는 면역 관련 질환의 예방 또는 치료 방법.
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AU2019362131A AU2019362131A1 (en) | 2018-10-17 | 2019-10-17 | Binding molecule specific to Lrig-1 protein, and use thereof |
US17/286,424 US20220275080A1 (en) | 2018-10-17 | 2019-10-17 | Binding molecule specific to lrig-1 protein, and use thereof |
CA3116573A CA3116573A1 (en) | 2018-10-17 | 2019-10-17 | Binding molecule specific for lrig-1 protein and use thereof |
JP2021521249A JP2022512749A (ja) | 2018-10-17 | 2019-10-17 | Lrig-1タンパク質に特異的な結合分子及びその用途 |
EP19872549.1A EP3882266A4 (en) | 2018-10-17 | 2019-10-17 | LRIG-1 PROTEIN SPECIFIC BINDING MOLECULE AND USE THEREOF |
CN201980069021.XA CN112912402A (zh) | 2018-10-17 | 2019-10-17 | Lrig-1蛋白的特异性结合分子及其用途 |
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PCT/KR2019/013666 WO2020080853A1 (ko) | 2018-10-17 | 2019-10-17 | Lrig-1 단백질에 특이적인 결합 분자 및 이의 용도 |
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EP (2) | EP3868782A1 (ko) |
JP (2) | JP7526493B2 (ko) |
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KR102694121B1 (ko) * | 2020-10-22 | 2024-08-13 | 주식회사 굳티셀 | 활성화된 면역 세포의 세포 표면 항원 및 이의 다양한 용도 |
US20240301050A1 (en) * | 2021-01-27 | 2024-09-12 | Good T Cells, Inc. | Novel binding molecule and use thereof |
CN113480646B (zh) * | 2021-07-01 | 2022-03-15 | 中国科学院生物物理研究所 | 特异性结合h1.4移码突变蛋白的单克隆抗体制备及其应用 |
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US20220213186A1 (en) * | 2019-03-20 | 2022-07-07 | Good T Cells, Inc. | Composition for preventing or treating brain and nervous system disease |
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KR102306346B1 (ko) | 2021-09-30 |
WO2020080854A1 (ko) | 2020-04-23 |
CA3116573A1 (en) | 2020-04-23 |
EP3882266A4 (en) | 2022-07-27 |
JP7526493B2 (ja) | 2024-08-01 |
KR102302393B1 (ko) | 2021-09-16 |
EP3868782A1 (en) | 2021-08-25 |
US20220275080A1 (en) | 2022-09-01 |
KR20200043301A (ko) | 2020-04-27 |
JP2022512749A (ja) | 2022-02-07 |
US20220275081A1 (en) | 2022-09-01 |
AU2019362131A1 (en) | 2021-05-27 |
EP3882266A1 (en) | 2021-09-22 |
CN113056485A (zh) | 2021-06-29 |
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