A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union

Rajesh K. Grover, Xueyong Zhu, Travis Nieusma, Teresa Jones, Isabel Boero, Amanda S. MacLeod, Adam Mark, Sherry Niessen, Helen J. Kim, Leopold Kong, Nacyra Assad-Garcia, Keehwan Kwon, Marta Chesi, Vaughn V. Smider, Daniel R. Salomon, Diane F. Jelinek, Robert A. Kyle, Richard B. Pyles, John I. Glass, Andrew B. WardIan A. Wilson, Richard A. Lerner

Research output: Contribution to journalArticlepeer-review

74 Scopus citations


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 k and l 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.

Original languageEnglish (US)
Pages (from-to)656-661
Number of pages6
Issue number6171
StatePublished - 2014
Externally publishedYes

ASJC Scopus subject areas

  • General


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