Staphylococcus aureus surface protein SasG contributes to intercellular autoaggregation of Staphylococcus aureus

Makoto Kuroda, Ryuta Ito, Yoshikazu Tanaka, Min Yao, Kimio Matoba, Shinji Saito, Isao Tanaka, Toshiko Ohta

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

Staphylococcus aureus surface protein G (SasG) is one of cell surface proteins with cell-wall sorting motif. The sasG mutant showed significantly reduced cell aggregation and biofilm formation. SasG is comprised of variable A domain and multiple tandem repeats of B domain, native-PAGE and in vitro formaldehyde cross-linking experiments revealed that the recombinant protein of the A domain showed homo-oligomerization as an octamer, but B domain did not. This study shows that SasG-A domain contributes to intercellular autoaggregation by homo-oligomerization, and that may facilitate the adherence to host-tissues in the infection of S. aureus.

Original languageEnglish
Pages (from-to)1102-1106
Number of pages5
JournalBiochemical and biophysical research communications
Volume377
Issue number4
DOIs
Publication statusPublished - 2008 Dec 26
Externally publishedYes

Keywords

  • Autoaggregation
  • Cell-wall anchored protein
  • Homo-oligomerization

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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