Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components
Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components
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DOI：
10.1099/mic.0.28860-0
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发表时间：
2006-08-01
期刊：
影响因子：
2.8
通讯作者：
Donnenberg, Michael S.
中科院分区：
文献类型：
--
作者：
Daniel, Anu;Singh, Aparna;Donnenberg, Michael S.
典型的肠致病性大肠杆菌菌株表达属于IV型皮利家族的已确定的毒力因子，称为肠形成菌毛（BFP）。BFP作为成束的丝状附属物存在于细胞表面上，并且通过由bfp操纵子编码的蛋白质组装和收缩。这些蛋白质组装成一个分子机器。BFP机器可以在概念上分为三个组件：细胞质膜（CM）子组件，其由CM蛋白和细胞质核苷酸结合蛋白组成;外膜（OM）子组件和菌毛本身。作者以前的特点CM子组件和菌毛。在这项研究中，一个更完整的表征OM子组件进行了生物化学，生物物理和遗传方法的组合。据报道，BfpG对OM的靶向受到分泌素BfpB的影响。BfpG和BfpU与BfpB的氨基端相互作用。BfpU具有复杂的细胞分布模式，并且与BfpB和BfpG沿着是OM子组件的一部分。
Typical enteropathogenic Escherichia coli strains express an established virulence factor belonging to the type IV pili family, called the bundle-forming pilus (BFP). BFP are present on the cell surface as bundled filamentous appendages, and are assembled and retracted by proteins encoded by the bfp operon. These proteins assemble to form a molecular machine. The BFP machine may be conceptually divided into three components: the cytoplasmic membrane (CM) subassembly, which is composed of CM proteins and cytoplasmic nucleotide-binding proteins; the outer membrane (OM) subassembly and the pilus itself. The authors have previously characterized the CM subassembly and the pilus. In this study, a more complete characterization of the OM subassembly was carried out using a combination of biochemical, biophysical and genetic approaches. It is reported that targeting of BfpG to the OM was influenced by the secretin BfpB. BfpG and BfpU interacted with the amino terminus of BfpB. BfpU had a complex cellular distribution pattern and, along with BfpB and BfpG, was part of the OM subassembly.