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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Grover, RK; Zhu, X; Nieusma, T; Jones, T; Boero, I; MacLeod, AS; Mark, A; Niessen, S; Kim, HJ; Kong, L; Assad-Garcia, N; Kwon, K; Chesi, M; Smider, VV; Salomon, DR; Jelinek, DF; Kyle, RA; Pyles, RB; Glass, JI; Ward, AB; Wilson, IA; Lerner, RA

Published Date

  • January 1, 2014

Published In

Volume / Issue

  • 343 / 6171

Start / End Page

  • 656 - 661

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1246135

Citation Source

  • Scopus