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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.