Staphylococcal exfoliative toxins cleave α-and β-melanocyte-stimulating hormones
JV Rago, GM Vath, TJ Tripp, GA Bohach… - Infection and …, 2000 - Am Soc Microbiol
Infection and immunity, 2000•Am Soc Microbiol
The staphylococcal exfoliative toxins (ETs) A and B (ETA and ETB) are 27-kDa exotoxins
produced by certain strains of Staphylococcus aureus and are the causative agents of
staphylococcal scalded-skin syndrome. The crystal structures of the ETs strongly indicate
that the proteins are members of the serine protease family of enzymes, although protease
activity until now has not yet been conclusively demonstrated. Here, we show that the
peptide β-melanocyte-stimulating hormone (β-MSH) is cleaved by ETA and that both ETA …
produced by certain strains of Staphylococcus aureus and are the causative agents of
staphylococcal scalded-skin syndrome. The crystal structures of the ETs strongly indicate
that the proteins are members of the serine protease family of enzymes, although protease
activity until now has not yet been conclusively demonstrated. Here, we show that the
peptide β-melanocyte-stimulating hormone (β-MSH) is cleaved by ETA and that both ETA …
Abstract
The staphylococcal exfoliative toxins (ETs) A and B (ETA and ETB) are 27-kDa exotoxins produced by certain strains ofStaphylococcus aureus and are the causative agents of staphylococcal scalded-skin syndrome. The crystal structures of the ETs strongly indicate that the proteins are members of the serine protease family of enzymes, although protease activity until now has not yet been conclusively demonstrated. Here, we show that the peptide β-melanocyte-stimulating hormone (β-MSH) is cleaved by ETA and that both ETA and ETB are capable of cleaving α-MSH. Both toxins exhibit cleavage at specific glutamic acid residues in MSH peptides. Moreover, biologically inactive mutants of ETA were incapable of cleaving β-MSH.
American Society for Microbiology