肠道致病性大肠杆菌的EspF与分选连接蛋白9结合。
EspF of enteropathogenic Escherichia coli binds sorting nexin 9.
作者信息
Marchès Oliver, Batchelor Miranda, Shaw Robert K, Patel Amit, Cummings Nicola, Nagai Takeshi, Sasakawa Chihiro, Carlsson Sven R, Lundmark Richard, Cougoule Celine, Caron Emmanuelle, Knutton Stuart, Connerton Ian, Frankel Gad
机构信息
Flowers Building, Imperial College London, London SW7 2AZ, United Kingdom.
出版信息
J Bacteriol. 2006 Apr;188(8):3110-5. doi: 10.1128/JB.188.8.3110-3115.2006.
Abstract
EspF of enteropathogenic Escherichia coli targets mitochondria and subverts a number of cellular functions. EspF consists of six putative Src homology 3 (SH3) domain binding motifs. In this study we identified sorting nexin 9 (SNX9) as a host cell EspF binding partner protein, which binds EspF via its amino-terminal SH3 region. Coimmunoprecipitation and confocal microscopy showed specific EspF-SNX9 interaction and non-mitochondrial protein colocalization in infected epithelial cells.
摘要
肠致病性大肠杆菌的EspF靶向线粒体并破坏多种细胞功能。EspF由六个假定的Src同源3（SH3）结构域结合基序组成。在本研究中，我们鉴定了分选连接蛋白9（SNX9）作为宿主细胞EspF结合伴侣蛋白，其通过氨基末端SH3区域与EspF结合。免疫共沉淀和共聚焦显微镜显示在感染的上皮细胞中存在特异性的EspF-SNX9相互作用和非线粒体蛋白共定位。
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