A Unique Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union
We report the discovery and crystal structure of a human mycoplasma protein, Protein M, which binds with high affinity to antibodies, predominantly through attachment to the variable region of the κ and λ light chains. Protein M broadly blocks antibody-antigen union and its mechanism of inhibition i...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 2014-02, Vol.343 (6171), p.656-661 |
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creator | Grover, Rajesh K. Zhu, Xueyong Nieusma, Travis Jones, Teresa Boreo, Isabel MacLeod, Amanda S. Mark, Adam Niessen, Sherry Kim, Helen J. Kong, Leopold Assad-Garcia, Nacyra Kwon, Keehwan Chesi, Marta Smider, Vaughn V. Salomon, Daniel R. Jelinek, Diane F. Kyle, Robert A. Pyles, Richard B. Glass, John I. Ward, Andrew B. Wilson, Ian A. Lerner, Richard A. |
description | We report the discovery and crystal structure of a human mycoplasma protein, Protein M, which binds with high affinity to antibodies, predominantly through attachment to the variable region of the κ and λ light chains. Protein M broadly blocks antibody-antigen union and its mechanism of inhibition is of considerable interest because, as a diversity system, the binding mode of each antibody is different. Protein M thus appears to function by a mechanism that is independent of the sequences of members of the extensive antibody repertoire. By anchoring to conserved regions of the antibody light chains, Protein M is in a position to extend its large C-terminal domain over the antibody combining site and block entrance to macromolecular antigens. |
doi_str_mv | 10.1126/science.1246135 |
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title | A Unique Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union |
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