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Infection and Immunity, January 2001, p. 159-169, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.159-169.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Description of Staphylococcus Serine Protease (ssp) Operon in Staphylococcus aureus and Nonpolar Inactivation of sspA-Encoded Serine Protease

Kelly Rice,1 Robert Peralta,1 Darrin Bast,2 Joyce de Azavedo,2 and Martin J. McGavin1,*

University of Toronto Department of Laboratory Medicine and Pathobiology, and Sunnybrook and Womens' College Health Science Centre, Department of Microbiology, North York, Ontario, Canada M4N 3M5,1 and Mt. Sinai Hospital and Toronto Medical Laboratories, University of Toronto, Toronto, Ontario, Canada M5G 1X52

Received 3 July 2000/Returned for modification 28 August 2000/Accepted 2 October 2000

Signature tagged mutagenesis has recently revealed that the Ssp serine protease (V8 protease) contributes to in vivo growth and survival of Staphylococcus aureus in different infection models, and our previous work indicated that Ssp could play a role in controlling microbial adhesion. In this study, we describe an operon structure within the ssp locus of S. aureus RN6390. The ssp gene encoding V8 protease is designated as sspA, and is followed by sspB, which encodes a 40.6-kDa cysteine protease, and sspC, which encodes a 12.9-kDa protein of unknown function. S. aureus SP6391 is an isogenic derivative of RN6390, in which specific loss of SspA function was achieved through a nonpolar allelic replacement mutation. In addition to losing SspA, the culture supernatant of SP6391 showed a loss of 22- to 23-kDa proteins and the appearance of a 40-kDa protein corresponding to SspB. Although the 40-kDa SspB protein could degrade denatured collagen, our data establish that this is a precursor form which is normally processed by SspA to form a mature cysteine protease. Culture supernatant of SP6391 also showed a new 42-kDa glucosaminidase and enhanced glucosaminidase activity in the 29 to 32 kDa range. Although nonpolar inactivation of sspA exerted a pleiotropic effect, S. aureus SP6391 exhibited enhanced virulence in a tissue abscess infection model relative to RN6390. Therefore, we conclude that SspA is required for maturation of SspB and plays a role in controlling autolytic activity but does not by itself exert a significant contribution to the development of tissue abscess infections.

* Corresponding author. Mailing address: S-112 Department of Microbiology, Sunnybrook and Women's College Health Science Centre, North York, Ontario, Canada M4N 3M5. Phone: (416) 480-5831. Fax: (416) 480-5737. E-mail: martin.mcgavin{at}swchsc.on.ca.

Infection and Immunity, January 2001, p. 159-169, Vol. 69, No. 1
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.1.159-169.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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