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Papers In Press, published online ahead of print August 30, 2002
S112, Department of Microbiology, University of Toronto, Department of Laboratory Medicine and Pathobiology, Toronto, ON M4N 3M5
Corresponding Author: martin.mcgavin{at}swchsc.on.ca
The SspB cysteine protease of Staphylococcus aureus is expressed in an operon, flanked by the sspA serine protease, and sspC, encoding a 12.9 kDa protein of unknown function. SspB was expressed as a 40 kDa prepropeptide pSspB, which did not undergo autocatalytic maturation. Activity of pSspB was reduced compared to 22 kDa mature SspB, but was equivalent to mature SspB after incubation with SspA, which specifically removed the pSspB N-terminal propeptide. SspC abrogated the activity of pSspB when incubated in a 1:1 complex, but had no affect on SspA or papain. Activity of the pSspB:SspC complex was restored when incubated with SspA, and SspC was cleaved by SspA but not pSspB. Thus, SspC maintains pSspB as an inert zymogen, and SspA is required for removal of the propeptide, and inactivation of SspC. Like the papain protease family, SspB cleaved substrates with a hydrophobic amino acid at P2, but had a strong preference for arginine at P1. It did not cleave casein, serum albumin, IgG or IgA, but promoted detachment of cultured keratinocytes, and cleaved fibronectin and fibrinogen at sites recognized by urokinase plasminogen activator and plasmin respectively. It also processed high molecular weight kininogen in a manner resembling plasma kallikrein. Thus, SspB exhibits a novel maturation mechanism, and mimics the specificity of plasma serine proteases.
J. Biol. Chem, 10.1074/jbc.M207162200
Submitted on July 17, 2002
Revised on August 30, 2002
Accepted on August 30, 2002
Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus
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