The role of the serine protease active site in the mode of action of epidermolytic toxin of Staphylococcus aureus.
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.
Redpath
M B
MB
Department of Biochemistry, Trinity College, Dublin, Republic of Ireland.
Foster
T J
TJ
Bailey
C J
CJ
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
D005083:Exfoliatins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase