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The solution structure of the invasive tip complex from Afa/Dr fibrils
Authors: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
Institution:Division of Molecular Biosciences, Biochemistry Building, Imperial College London, South Kensington, London SW7 2AZ, UK.
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.
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