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首页> 外文期刊>Journal of bacteriology >Structure-Function Analysis of BfpB, a Secretin-Like Protein Encoded by the Bundle-Forming-Pilus Operon of EnteropathogenicEscherichia coli
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Structure-Function Analysis of BfpB, a Secretin-Like Protein Encoded by the Bundle-Forming-Pilus Operon of EnteropathogenicEscherichia coli

机译:BfpB的结构功能分析,这种蛋白由肠致病性大肠杆菌的束形成菌毛操纵子编码。

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Production of type IV bundle-forming pili by enteropathogenicEscherichia coli (EPEC) requires BfpB, an outer-membrane lipoprotein and member of the secretin protein superfamily. BfpB was found to compose a ring-shaped, high-molecular-weight outer-membrane complex that is stable in 4% sodium dodecyl sulfate at temperatures of ≤65°C. Chemical cross-linking and immunoprecipitation experiments disclosed that the BfpB multimeric complex interacts with BfpG, and mutational studies showed that BfpG is required for the formation and/or stability of the multimer but not for the outer-membrane localization of BfpB. Formation of the BfpB multimer also does not require BfpA, the repeating subunit of the pilus filament. Functional studies of the BfpB-BfpG complex revealed that its presence confers vancomycin sensitivity, indicating that it may form an incompletely gated channel through the outer membrane. BfpB expression is also associated with accumulation of EPEC proteins in growth medium, suggesting that it may support both pilus biogenesis and protein secretion.
机译:肠致病性大肠埃希氏菌(EPEC)产生IV型成束菌毛需要BfpB,外膜脂蛋白和促胰液素蛋白超家族成员。发现BfpB组成了一个环状的高分子量外膜复合物,该复合物在≤65°C的温度下在4%的十二烷基硫酸钠中稳定。化学交联和免疫沉淀实验表明BfpB多聚体复合物与BfpG相互作用,突变研究表明BfpG是多聚体形成和/或稳定性所必需的,而不是BfpB的外膜定位所必需的。 BfpB多聚体的形成也不需要BfpA(菌毛丝的重复亚基)。 BfpB-BfpG复合物的功能研究表明,它的存在赋予万古霉素敏感性,表明它可能形成穿过外膜的不完全封闭的通道。 BfpB的表达还与EPEC蛋白在生长培养基中的积累有关,表明它可能支持菌毛的生物发生和蛋白的分泌。

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