| Literature DB >> 24503852 |
Rajesh K Grover1,2, Xueyong Zhu3, Travis Nieusma3, Teresa Jones1, Isabel Boreo1, Amanda S MacLeod4, Adam Mark5, Sherry Niessen6, Helen J Kim3, Leopold Kong3, Nacyra Assad-Garcia7, Keehwan Kwon7, Marta Chesi8, Vaughn V Smider1, Daniel R Salomon5, Diane F Jelinek9, Robert A Kyle9, Richard B Pyles10, John I Glass7, Andrew B Ward3, Ian A Wilson3,11, Richard A Lerner1,2.
Abstract
We report the discovery of a broadly reactive antibody-binding protein (Protein M) from human mycoplasma. The crystal structure of the ectodomain of transmembrane Protein M differs from other known protein structures, as does its mechanism of antibody binding. Protein M binds with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the κ and λ light chains. Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens. Similar to the other immunoglobulin-binding proteins such as Protein A, Protein M as well as its orthologs in other Mycoplasma species could become invaluable reagents in the antibody field.Entities:
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Year: 2014 PMID: 24503852 PMCID: PMC3987992 DOI: 10.1126/science.1246135
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728