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. Ward
  • Ian A. Wilson, Richard A. Lerner

Research output: Contribution to journalArticlepeer-review

87 Scopus citations

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 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
JournalScience
Volume343
Issue number6171
DOIs
StatePublished - 2014

ASJC Scopus subject areas

  • General

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