来自Afa/Dr菌毛侵袭性尖端复合体的溶液结构
The solution structure of the invasive tip complex from Afa/Dr fibrils.
作者信息
Cota Ernesto, Jones Celine, Simpson Peter, Altroff Harri, Anderson Kirstine L, du Merle Laurence, Guignot Julie, Servin Alain, Le Bouguénec Chantal, Mardon Helen, Matthews Stephen
机构信息
Division of Molecular Biosciences, Biochemistry Building, Imperial College London, South Kensington, London SW7 2AZ, UK.
出版信息
Mol Microbiol. 2006 Oct;62(2):356-66. doi: 10.1111/j.1365-2958.2006.05375.x. Epub 2006 Sep 8.
Abstract
Afa/Dr family of adhesins are produced by pathogenic Escherichia coli strains that are especially prevalent in chronic diarrhoeal and recurrent urinary tract infections. Most notably, they are found in up to 50% of cystitis cases in children and 30% of pyelonephritis in pregnant women. Afa/Dr adhesins are capped surface fibrils that mediate recognition of the host and subsequent bacterial internalization. Using the newly solved three-dimensional structure of the minimal invasive complex (AfaDE) combined with biochemical and cellular assays, we reveal the architecture of the fibrillar cap and identify a novel mode of synergistic integrin recognition.
摘要
Afa/Dr黏附素家族由致病性大肠杆菌菌株产生，这些菌株在慢性腹泻和复发性尿路感染中尤为常见。最值得注意的是，在高达50%的儿童膀胱炎病例和30%的孕妇肾盂肾炎病例中都发现了它们。Afa/Dr黏附素是覆盖在表面的纤丝，介导对宿主的识别以及随后的细菌内化。利用新解析出的最小侵袭复合物（AfaDE）的三维结构，结合生化和细胞分析，我们揭示了纤丝状帽的结构，并确定了一种协同整合素识别的新模式。
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