An atomic resolution model for assembly, architecture, and function of the Dr adhesins
An atomic resolution model for assembly, architecture, and function of the Dr adhesins
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DOI：
10.1016/j.molcel.2004.08.003
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发表时间：
2004-08-27
期刊：
影响因子：
16
通讯作者：
Matthews, S
中科院分区：
文献类型：
--
作者：
Anderson, KL;Billington, J;Matthews, S
病原菌具有粘附蛋白复合物，其在靶向宿主细胞和传播感染中发挥重要作用。虽然每个粘附蛋白家族通常与特定的人类疾病有关，但来自大肠杆菌的Dr家族是一个值得注意的例外，因为其成员与尿道和尿道感染都有关。据报道，这些蛋白质在细菌细胞表面形成菌毛和无菌毛结构，并靶向共同的宿主细胞受体，即衰变加速因子（CD55）。使用新解决的三维结构的AfaE，我们已经构建了一个强大的原子分辨率模型，揭示了由供体链互补组装的结构基础和加盖表面纤维的架构。
Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.