• Media type: E-Article
  • Title: Characterization of the Accessory Sec System of Staphylococcus aureus
  • Contributor: Siboo, Ian R.; Chaffin, Donald O.; Rubens, Craig E.; Sullam, Paul M.
  • imprint: American Society for Microbiology, 2008
  • Published in: Journal of Bacteriology
  • Language: English
  • DOI: 10.1128/jb.00300-08
  • ISSN: 0021-9193; 1098-5530
  • Keywords: Molecular Biology ; Microbiology
  • Origination:
  • Footnote:
  • Description: <jats:title>ABSTRACT</jats:title> <jats:p> The SraP adhesin of <jats:italic>Staphylococcus aureus</jats:italic> is a member of a highly conserved family of serine-rich surface glycoproteins of gram-positive bacteria. For streptococci, export of the SraP homologs requires a specialized transport pathway (the accessory Sec system). Compared to streptococci, however, SraP is predicted to differ in its signal peptide and glycosylation, which may affect its dependence on a specialized system for transport. In addition, two genes ( <jats:italic>asp4</jats:italic> and <jats:italic>asp5</jats:italic> ) essential for export in <jats:italic>Streptococcus gordonii</jats:italic> are missing in <jats:italic>S. aureus</jats:italic> . Thus, the selectivity of the accessory Sec system in <jats:italic>S. aureus</jats:italic> may also differ compared to streptococci. To address these issues, the five genes encoding the putative accessory Sec system ( <jats:italic>secY2</jats:italic> , <jats:italic>secA2</jats:italic> , and <jats:italic>asp1-3</jats:italic> ) were disrupted individually in <jats:italic>S. aureus</jats:italic> ISP479C, and the resultant mutants were examined for SraP export. Disruption of <jats:italic>secA2</jats:italic> resulted in the near complete loss of SraP surface expression. Similar results were seen with disruption of <jats:italic>secY2</jats:italic> and <jats:italic>asp1</jats:italic> , <jats:italic>asp2</jats:italic> , or <jats:italic>asp3</jats:italic> . To assess whether the accessory Sec system transported other substrates, we compared secreted proteomes of ISP479C and a <jats:italic>secA2</jats:italic> isogenic mutant, by two-dimensional fluorescence difference gel electrophoresis. Although two consistent differences in proteome content were noted between the strains, neither protein appeared to be a likely substrate for accessory Sec export. Thus, the accessory Sec system of <jats:italic>S. aureus</jats:italic> is required for the export of SraP, and it appears to be dedicated to the transport of this substrate exclusively. </jats:p>
  • Access State: Open Access