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Streptococcal M protein: molecular design and biological behavior
Author(s) -
Vincent A. Fischetti
Publication year - 1989
Publication title -
clinical microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.177
H-Index - 282
eISSN - 1070-6305
pISSN - 0893-8512
DOI - 10.1128/cmr.2.3.285
Subject(s) - organism , biology , epitope , virulence , structural motif , bacteria , antigen , microbiology and biotechnology , biochemistry , genetics , gene
M protein is a major virulence determinant for the group A streptococcus by virtue of its ability to allow the organism to resist phagocytosis. Common in eucaryotes, the fibrillar coiled-coil design for the M molecule may prove to be a common motif for surface proteins in gram-positive organisms. This type of structure offers the organism several distinct advantages, ranging from antigenic variation to multiple functional domains. The close resemblance of this molecular design to that of certain mammalian proteins could help explain on a molecular level the formation of epitopes responsible for serological cross-reactions between microbial and mammalian proteins. Many of the approaches described in the elucidation of the M-protein structure may be applied for characterizing similar molecules in other microbial systems.

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