EMD-5836
A Unique Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union
EMD-5836
Single-particle16.8 Å
Deposition: 13/12/2013Map released: 19/03/2014
Last modified: 19/03/2014
Sample Organism:
Mycoplasma genitalium,
Homo sapiens
Sample: Fab of human mAb b12 in complex with trypsinized MG281
Deposition Authors: Grover RK, Zhu X, Nieusma T, Jones T, Boreo I, MacLeod AS, Mark A, Niessen S, Kim HJ, Kong L
,
Assad-Garcia N,
Kwon K,
Chesi M,
Salomon DR,
Jelinek DF,
Kyle RA,
Pyles RB,
Glass JI ,
Ward AB,
Wilson IA,
Lerner RA
Sample: Fab of human mAb b12 in complex with trypsinized MG281
Deposition Authors: Grover RK, Zhu X, Nieusma T, Jones T, Boreo I, MacLeod AS, Mark A, Niessen S, Kim HJ, Kong L
,
Assad-Garcia N,
Kwon K,
Chesi M,
Salomon DR,
Jelinek DF,
Kyle RA,
Pyles RB,
Glass JI ,
Ward AB,
Wilson IA,
Lerner RA
A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union.
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
(2014) Science , 343 , 656 - 661
,
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
(2014) Science , 343 , 656 - 661
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.
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.