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Kim, Helen J.

https://orcid.org/0000-0003-0096-7740

Mayo Clinic

Scripps Research Institute

Citations 1

A Structurally Distinct Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union
Grover, Rajesh K., Nieusma, Travis, Jones, Teresa M., Boero, Isabel, MacLeod, Amanda S. , Mark, A, 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. , Wilson, Ian A. , Lerner, Richard A. , Zhu, Xueyong , Ward, Andrew B.

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

10.1126/science.1246135 Get It

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.