A Structurally Distinct Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union
2014
Grover, Rajesh K. | Zhu, Xueyong | Nieusma, Travis | Jones, Teresa | Boero, 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, I. A. (Ian A.) | Lerner, Richard A. (Richard Alan)
Easy M Our immune systems can produce a vastly diverse repertoire of antibody molecules that each recognize and bind to a specific foreign antigen via a hypervariable region. However, there are a few bacterial antigens—such as Protein A, Protein G, and Protein L—that instead bind to the antibody's conserved regions and can bind to a large number of different antibodies. These high-affinity broad-spectrum antibody-binding properties have been widely exploited both in the laboratory and in industry for purifying, immobilizing, and detecting antibodies. Grover et al. (p. 656) have now identified Protein M found on the surface of human mycoplasma, which displays even broader antibody-binding specificity. The crystal structure of Protein M revealed how Protein-M binding blocks the antibody's antigen binding site. This mechanism may be exploited by mycoplasma to escape the humoral immune response.
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