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The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus

Maria B. Redpath , Timothy J. Foster , Christopher J. Bailey
DOI: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04738.x 151-155 First published online: 1 June 1991

Summary

The sequences of the epidermolytic toxins and V8 serine proteinase share about 25% identity, including the catalytic triad at the proteinase active centre. Here we have altered the putative ETA active-site serine-195 to glycine by site-directed mutagenesis. No epidermolytic activity was detected when up to 100-fold greater amounts of the homogeneous mutant ETA were injected subcutaneously into neonatal mice showing that serine-195 is required for toxicogenesis.

Key words
  • Staphylococcus aureus
  • Epidermolytic toxin
  • Serine proteinase
  • Site-directed mutagenesis

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