Anderson Kirstine L, Billington Jason, Pettigrew David, Cota Ernesto, Simpson Peter, Roversi Pietro, Chen Ho An, Urvil Petri, du Merle Laurence, Barlow Paul N, Medof M Edward, Smith Richard A G, Nowicki Bogdan, Le Bouguénec Chantal, Lea Susan M, Matthews Stephen
Department of Biological Sciences, Wolfson Laboratories, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
Mol Cell. 2004 Aug 27;15(4):647-57. doi: 10.1016/j.molcel.2004.08.003.
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.
致病细菌拥有粘附蛋白复合物，这些复合物在靶向宿主细胞和传播感染方面发挥着重要作用。虽然每个粘附蛋白家族通常与特定的人类疾病相关，但来自大肠杆菌的Dr家族是一个显著的例外，因为其成员与腹泻和尿路感染都有关联。据报道，这些蛋白在细菌细胞表面形成菌毛和无附属物结构，并靶向共同的宿主细胞受体——衰变加速因子（DAF或CD55）。利用新解析出的AfaE三维结构，我们构建了一个可靠的原子分辨率模型，该模型揭示了通过供体链互补进行组装的结构基础以及帽状表面纤维的结构。
