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. 1997:418:589-92.
doi: 10.1007/978-1-4899-1825-3_136.

Structure-function and pathogenesis studies of Streptococcus pyogenes extracellular cysteine protease

E H Burns Jr  1 , A M Marciel, J M Musser
Affiliations

Structure-function and pathogenesis studies of Streptococcus pyogenes extracellular cysteine protease

E H Burns Jr et al. Adv Exp Med Biol. 1997.

Abstract

Replacement of the single cysteine residue (C192) with serine in the Streptococcus pyogenes extracellular cysteine protease (SCP) prevented auto-catalytic processing of the 40-kDa zymogen to the 28-kDa mature form and eliminated proteolytic activity. SCP incubated with human endothelial cells induced a time- and concentration-dependent increase in a 66-kDa gelatinase/type IV collagenase in culture supernatants. Activation of this gelatinase/collagenase may contribute to endothelial cell damage, tissue destruction, and hemodynamic derangement observed in some patients with severe, invasive S. pyogenes infection.

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