Abstract
We report the discovery of a broadly reactive antibody-binding protein (Protein M) from human mycoplasma. The crystal structure of the ectodomain of transmembrane Protein M differs from other known protein structures, as does its mechanism of antibody binding. Protein M binds with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the κ and λ light chains. Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens. Similar to the other immunoglobulin-binding proteins such as Protein A, Protein M as well as its orthologs in other Mycoplasma species could become invaluable reagents in the antibody field.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigen-Antibody Reactions / genetics
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Antigen-Antibody Reactions / immunology*
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Antigens / immunology*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / immunology*
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Crystallography, X-Ray
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Humans
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Immunoglobulin G / immunology*
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Immunoglobulin Variable Region / immunology*
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Immunoglobulin kappa-Chains / immunology
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Immunoglobulin lambda-Chains / immunology
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Lymphokines / chemistry
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Lymphokines / genetics
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Lymphokines / immunology*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / immunology*
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Mycoplasma / immunology*
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology
Substances
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Antigens
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Bacterial Proteins
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Immunoglobulin G
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Immunoglobulin Variable Region
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Immunoglobulin kappa-Chains
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Immunoglobulin lambda-Chains
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Lymphokines
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Membrane Proteins
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Recombinant Proteins
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immunoglobulin-binding factors
Associated data
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PDB/4NZR
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PDB/4NZT
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PDB/4NZU