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

Eugene H. Burns; Ann Marie Marciel; James M. Musser

doi:10.1007/978-1-4899-1825-3_136

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

Eugene H. Burns, Ann Marie Marciel, James M. Musser

Research output: Contribution to journal › Article

6 Scopus citations

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.

Original language	English (US)
Pages (from-to)	589-592
Number of pages	4
Journal	Advances in experimental medicine and biology
Volume	418
DOIs	https://doi.org/10.1007/978-1-4899-1825-3_136
State	Published - 1997

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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AU - Marciel, Ann Marie

AU - Musser, James M.

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AB - 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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