The solution structure of the invasive tip complex from Afa/Dr fibrils

被引:38
作者
Cota, Ernesto
Jones, Celine
Simpson, Peter
Altroff, Harri
Anderson, Kirstine L.
du Merle, Laurence
Guignot, Julie
Servin, Alain
Le Bouguenec, Chantal
Mardon, Helen
Matthews, Stephen
机构
[1] Imperial Coll London, Div Mol Biosci, London SW7 2AZ, England
[2] Univ Oxford, Womens Ctr, John Radcliffe Hosp, Nuffield Dept Obstet & Gynaecol,Div Med Sci, Oxford OX3 9DU, England
[3] Inst Pasteur, Unite Pathogenie Bacterienne Muqueuses, F-75724 Paris 15, France
[4] Fac Pharm Paris 11, INSERM, Unite 510, Chatenay Malabry, France
基金
英国医学研究理事会; 英国惠康基金;
关键词
D O I
10.1111/j.1365-2958.2006.05375.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:356 / 366
页数:11
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