title: The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus.
abstract: 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.
authors.affiliation: Department of Biochemistry, Trinity College, Dublin, Republic of Ireland.
authors.forename: M B
authors.initials: MB
authors.lastname: Redpath
authors.forename: T J
authors.initials: TJ
authors.lastname: Foster
authors.forename: C J
authors.initials: CJ
authors.lastname: Bailey
mesh_terms: D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D005083:Exfoliatins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000633:toxicity*; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D012697:Serine Endopeptidases / Q000737:chemistry*; D012867:Skin / Q000473:pathology; D013211:Staphylococcus aureus
chemical_list: D005083:Exfoliatins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase