The NH2‐Terminal Region ofStreptococcus pyogenesM5 Protein Confers Protection against Degradation by Proteases and Enhances Mucosal Colonization of Mice
Author(s) -
Thomas A. Penfound,
Itzhak Ofek,
Harry S. Courtney,
David L. Hasty,
James B. Dale
Publication year - 2010
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/652005
Subject(s) - proteases , lipoteichoic acid , microbiology and biotechnology , streptococcus pyogenes , biology , virulence , protease , mutant , cysteine protease , myeloma protein , peptide sequence , antibody , biochemistry , staphylococcus aureus , bacteria , enzyme , immunology , genetics , gene
The NH(2)-terminal sequence of the M protein from group A streptococci defines the serotype of the organism and contains epitopes that evoke bactericidal antibodies.
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