Molecular Characterization of a Novel Staphylococcus aureus Serine Protease Operon

Samantha B Reed; Carla A Wesson; Linda E Liou; William R Trumble; Patrick M Schlievert; Gregory A Bohach; Kenneth W Bayles

doi:10.1128/IAI.69.3.1521-1527.2001

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Molecular Characterization of a Novel Staphylococcus aureus Serine Protease Operon

Journal article

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Molecular Characterization of a Novel Staphylococcus aureus Serine Protease Operon

Samantha B Reed, Carla A Wesson, Linda E Liou, William R Trumble, Patrick M Schlievert, Gregory A Bohach and Kenneth W Bayles

Infection and immunity, Vol.69(3), pp.1521-1527

03/2001

DOI: 10.1128/IAI.69.3.1521-1527.2001

PMCID: PMC98051

PMID: 11179322

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Abstract

The present study identified and characterized a unique operon ( spl ) encoding six serine protease-like proteins. In addition, native Spl proteins were isolated and characterized. Typical of most exoproteins, the spl gene products contain putative 35- or 36-amino-acid signal peptides. The Spl proteins share 44 to 95% amino acid sequence identity with each other and 33 to 36% sequence identity with V8 protease. They also contain amino acids found in catalytic triads of enzymes in the trypsin-like serine protease family, and SplB and SplC were shown to degrade casein. The spl operon is transcribed on a 5.5-kb transcript, but several nonrandom degradation products of this transcript were also identified. Similar to other S. aureus exoprotein genes, the spl operon is maximally expressed during the transition into stationary phase and is positively controlled by the Agr virulence factor regulator. The Sar regulatory system did not affect spl operon expression. PCR analysis revealed the presence of the spl operon in 64% of the S. aureus isolates tested, although one spl operon-negative isolate was shown to contain at least two of the spl genes. Finally, intraperitoneal injection of an spl operon deletion mutant revealed no major differences in virulence compared to the parental strain.

Molecular Pathogenesis

Details

Title: Subtitle: Molecular Characterization of a Novel Staphylococcus aureus Serine Protease Operon
Creators: Samantha B Reed - and Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455
Carla A Wesson - and Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455
Linda E Liou - and Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455
William R Trumble - and Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455
Patrick M Schlievert - and Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455
Gregory A Bohach - and Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455
Kenneth W Bayles - and Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455
Resource Type: Journal article
Publication Details: Infection and immunity, Vol.69(3), pp.1521-1527
DOI: 10.1128/IAI.69.3.1521-1527.2001
PMID: 11179322
PMCID: PMC98051
NLM abbreviation: Infect Immun
ISSN: 0019-9567
eISSN: 1098-5522
Publisher: American Society for Microbiology
Language: English
Date published: 03/2001
Academic Unit: Microbiology and Immunology; Internal Medicine
Record Identifier: 9984001205402771

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