| Literature DB >> 18983982 |
Makoto Kuroda1, Ryuta Ito, Yoshikazu Tanaka, Min Yao, Kimio Matoba, Shinji Saito, Isao Tanaka, Toshiko Ohta.
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.Entities:
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Year: 2008 PMID： 18983982 DOI： 10.1016/j.bbrc.2008.10.134
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575