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

E H Burns; A M Marciel; J M Musser

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

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

E H Burns·A M Marciel·J M Musser

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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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Bacterial Proteins Binding Sites Cells, Cultured Collagenases Cysteine Endopeptidases Enzyme Activation Enzyme Precursors Exotoxins Humans Matrix Metalloproteinase 9 Membrane Proteins Mutagenesis, Site-Directed Streptococcus pyogenes Structure-Activity Relationship Virulence Journal Article

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E H Burns, A M Marciel, J M Musser. 1997. Structure-function and pathogenesis studies of Streptococcus pyogenes extracellular cysteine protease.. https://doi.org/10.1007/978-1-4899-1825-3_136

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