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A Structurally Distinct Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union

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, Ian A., Lerner, Richard A.
Science 2014 v.343 no.6171 pp. 656-661
Mycoplasma, antibodies, antigens, binding sites, crystal structure, humans, humoral immunity, immune system, industry
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.