Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1934086 | Biochemical and Biophysical Research Communications | 2008 | 5 Pages |
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.
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Authors
Makoto Kuroda, Ryuta Ito, Yoshikazu Tanaka, Min Yao, Kimio Matoba, Shinji Saito, Isao Tanaka, Toshiko Ohta,