期刊
SCIENCE
卷 343, 期 6171, 页码 656-661出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1246135
关键词
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资金
- Scripps Research Institute
- NIH through the National Center for Research Resources' P41 program [RR017573]
- NIH [RO1 AI042266, 5 R21 AI098057-02, R01 AG020686, U19 AI06360, K08 AR063729-01]
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 kappa and lambda 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.
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