Molecular characterization of a novel Staphylococcus aureus serine protease operon

S. B. Reed, C. A. Wesson, L. E. Liou, W. R. Trumble, P. M. Schlievert, G. A. Bohach, K. W. Bayles

Research output: Contribution to journalArticle

81 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1521-1527
Number of pages7
JournalInfection and immunity
Volume69
Issue number3
DOIs
StatePublished - Mar 14 2001

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Serine Proteases
Operon
Staphylococcus aureus
Genes
Amino Acids
Proteins
Virulence Factors
Protein Sorting Signals
Caseins
Intraperitoneal Injections
Virulence
Amino Acid Sequence
Polymerase Chain Reaction
Enzymes

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

Cite this

Reed, S. B., Wesson, C. A., Liou, L. E., Trumble, W. R., Schlievert, P. M., Bohach, G. A., & Bayles, K. W. (2001). Molecular characterization of a novel Staphylococcus aureus serine protease operon. Infection and immunity, 69(3), 1521-1527. https://doi.org/10.1128/IAI.69.3.1521-1527.2001

Molecular characterization of a novel Staphylococcus aureus serine protease operon. / Reed, S. B.; Wesson, C. A.; Liou, L. E.; Trumble, W. R.; Schlievert, P. M.; Bohach, G. A.; Bayles, K. W.

In: Infection and immunity, Vol. 69, No. 3, 14.03.2001, p. 1521-1527.

Research output: Contribution to journalArticle

Reed, SB, Wesson, CA, Liou, LE, Trumble, WR, Schlievert, PM, Bohach, GA & Bayles, KW 2001, 'Molecular characterization of a novel Staphylococcus aureus serine protease operon', Infection and immunity, vol. 69, no. 3, pp. 1521-1527. https://doi.org/10.1128/IAI.69.3.1521-1527.2001
Reed SB, Wesson CA, Liou LE, Trumble WR, Schlievert PM, Bohach GA et al. Molecular characterization of a novel Staphylococcus aureus serine protease operon. Infection and immunity. 2001 Mar 14;69(3):1521-1527. https://doi.org/10.1128/IAI.69.3.1521-1527.2001
Reed, S. B. ; Wesson, C. A. ; Liou, L. E. ; Trumble, W. R. ; Schlievert, P. M. ; Bohach, G. A. ; Bayles, K. W. / Molecular characterization of a novel Staphylococcus aureus serine protease operon. In: Infection and immunity. 2001 ; Vol. 69, No. 3. pp. 1521-1527.
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