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J. Biol. Chem., Vol. 277, Issue 44, 41770-41777, November 1, 2002
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From the 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 with 22-kDa mature SspB, but it
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 effect
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 it 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.
Identification of a Novel Maturation Mechanism and Restricted
Substrate Specificity for the SspB Cysteine Protease of
Staphylococcus aureus*
,,§,
**, and§§¶¶
Department of Laboratory Medicine and
Pathobiology and the Department of Medicine, University of
Toronto, Toronto, Ontario M5G 1L5, Canada, the Departments of
** Dermatology and §§ Microbiology,
Sunnybrook and Womens College Health Science Center, Toronto, Ontario
M4N 3M5, Canada, and the ¶ Institute for Biochemistry II,
University of Frankfurt Medical School, Frankfurt D-60590, Germany
*
This work was supported in part by Operating Grant MOP12669
from the Canadian Institutes for Health Research (to M. J. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Dermatology, Johns Hopkins
University, Baltimore, MD 21287-0900.
¶¶
To whom correspondence should be addressed: S112 Dept.
of Microbiology, Sunnybrook and Womens College Health Science Centre, 2075 Bayview Ave., Toronto, ON M4N 3M5, Canada. Tel.:
416-480-5831; Fax: 416-480-5737; E-mail:
martin.mcgavin@swchsc.on.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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