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

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 ? and ? 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.

SUBMITTER: Grover RK

PROVIDER: S-EPMC3987992 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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

Grover Rajesh K RK Zhu Xueyong X Nieusma Travis T Jones Teresa T Boreo Isabel I MacLeod Amanda S AS Mark Adam A Niessen Sherry S Kim Helen J HJ Kong Leopold L Assad-Garcia Nacyra N Kwon Keehwan K Chesi Marta M Smider Vaughn V VV Salomon Daniel R DR Jelinek Diane F DF Kyle Robert A RA Pyles Richard B RB Glass John I JI Ward Andrew B AB Wilson Ian A IA Lerner Richard A RA

Science (New York, N.Y.) 20140201 6171

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, ...[more]

PMID: 24503852

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Project description:Structure comparison tools can be used to align related protein structures to identify structurally conserved and variable regions and to infer functional and evolutionary relationships. While the conserved regions often superimpose well, the variable regions appear non superimposable. Differences in homologous protein structures are thought to be due to evolutionary plasticity to accommodate diverged sequences during evolution. One of the kinds of differences between 3-D structures of homologous proteins is rigid body displacement. A glaring example is not well superimposed equivalent regions of homologous proteins corresponding to ?-helical conformation with different spatial orientations. In a rigid body superimposition, these regions would appear variable although they may contain local similarity. Also, due to high spatial deviation in the variable region, one-to-one correspondence at the residue level cannot be determined accurately. Another kind of difference is conformational variability and the most common example is topologically equivalent loops of two homologues but with different conformations. In the current study, we present a refined view of the "structurally variable" regions which may contain local similarity obscured in global alignment of homologous protein structures. As structural alphabet is able to describe local structures of proteins precisely through Protein Blocks approach, conformational similarity has been identified in a substantial number of 'variable' regions in a large data set of protein structural alignments; optimal residue-residue equivalences could be achieved on the basis of Protein Blocks which led to improved local alignments. Also, through an example, we have demonstrated how the additional information on local backbone structures through protein blocks can aid in comparative modeling of a loop region. In addition, understanding on sequence-structure relationships can be enhanced through our approach. This has been illustrated through examples where the equivalent regions in homologous protein structures share sequence similarity to varied extent but do not preserve local structure.

Dataset Information

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

Publications

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

Similar Datasets

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