Abstract
The M proteins of Streptococcus pyogenes play an important role in pathogenesis by enabling these pathogens to resist phagocytosis. However, M proteins are sensitive to cleavage by trypsin from the animal host, as well as by a cysteine protease (SCP) from the Streptococci. Now it appears that Streptococci regulate the cleavage of M proteins, and perhaps other cell-surface proteins, by grabbing the host protease inhibitor α2-macroglobulin with a protein designated GRAB (protein G-related α2-macroglobulin-binding protein) 1 Rasmussen M. Muller H-P. Bjorck L. Protein GRAB of Streptococcus pyogenes regulates proteolysis at the bacterial cell surface by binding α2-macroglobulin. J. Biol. Chem. 1999; 274: 15336-15344 Crossref PubMed Scopus (108) Google Scholar . When bound at the streptococcal cell surface, α2-macroglobulin retains its broad spectrum anti-protease activity. GRAB appears to play a role in the virulence of S. pyogenes as the virulence of grab-expressing bacteria is attenuated.
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