金黄色葡萄球菌表面蛋白SasG有助于金黄色葡萄球菌的细胞间自聚集。
Staphylococcus aureus surface protein SasG contributes to intercellular autoaggregation of Staphylococcus aureus.
作者信息
Kuroda Makoto, Ito Ryuta, Tanaka Yoshikazu, Yao Min, Matoba Kimio, Saito Shinji, Tanaka Isao, Ohta Toshiko
机构信息
Laboratory of Bacterial Genomics, Center for Pathogen Genomics, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan.
出版信息
Biochem Biophys Res Commun. 2008 Dec 26;377(4):1102-6. doi: 10.1016/j.bbrc.2008.10.134. Epub 2008 Nov 5.
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.
金黄色葡萄球菌表面蛋白G（SasG）是一种具有细胞壁分选基序的细胞表面蛋白。sasG突变体显示细胞聚集和生物膜形成显著减少。SasG由可变的A结构域和多个B结构域串联重复序列组成，非变性聚丙烯酰胺凝胶电泳（native-PAGE）和体外甲醛交联实验表明，A结构域的重组蛋白以八聚体形式呈现同源寡聚化，而B结构域则不会。本研究表明，SasG-A结构域通过同源寡聚化促进细胞间自聚集，这可能有助于金黄色葡萄球菌感染过程中对宿主组织的黏附。
Zotero 插件