A Structurally Distinct Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union.

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Bibliographic Details
Title:	A Structurally Distinct Human Mycoplasma Protein that Generically Blocks Antigen-Antibody Union.
Authors:	Grover, Rajesh K., Xueyong Zhu, Nieusma, Travis, Jones, Teresa, Boero, Isabel, MacLeod, Amanda S., Mark, Adam, Niessen, Sherry, Kim, Helen J., Kong, Leopold, Assad-Garcia, Nacyra, Kwon, Keehwan, Chesi, Marta, Smider, Vaughn V., Salomon, Daniel R., Jelinek, Diane F., Kyle, Robert A., Pyles, Richard B., Glass, John I., Ward, Andrew B.
Source:	Science (pre-March 2025). 2/7/2014, Vol. 343 Issue 6171, p656-661. 6p.
Subjects:	Mycoplasma, Antigen-antibody reactions, Crystal structure, Membrane proteins, Protein structure, Immunoglobulin G, Antigens
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. [ABSTRACT FROM AUTHOR]
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Database:	Psychology and Behavioral Sciences Collection

Description
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. [ABSTRACT FROM AUTHOR]
ISSN:	00368075
DOI:	10.1126/science.1246135