OUP user menu

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


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

Sign in

Log in through your institution

Sign in as a personal subscriber

Log in through your institution

Purchase a personal subscription