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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Structure-function and pathogenesis studies of Streptococcus pyogenes extracellular cysteine protease. Burns, E.H., Marciel, A.M., Musser, J.M. Adv. Exp. Med. Biol. (1997) [Pubmed]
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