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Niessen, Sherry

A5074409054 | I123431417

Mayo Clinic

Scripps Research Institute

Citations 1

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

Science | February 6, 2014 | Volume: 343 | Issue: 6171 | Pages: 656-661

10.1126/science.1246135 | PMID 24503852

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.