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

• Published in: Molecular microbiology Vol. 62; no. 2; pp. 356 - 366
• Main 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
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.10.2006; Blackwell Science; Wiley
• Subjects: Adhesins, Escherichia coli; Adhesins, Escherichia coli - chemistry; Adhesins, Escherichia coli - genetics; Adhesins, Escherichia coli - metabolism; Amino Acid Sequence; Bacterial Adhesion; Bacterial Adhesion - genetics; Bacterial Adhesion - physiology; Biological and medical sciences; E coli; Escherichia coli; Escherichia coli Proteins; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Fimbriae, Bacterial; Fimbriae, Bacterial - genetics; Fimbriae, Bacterial - metabolism; Fundamental and applied biological sciences. Psychology; Human health and pathology; Infections; Infectious diseases; Life Sciences; Magnetic Resonance Spectroscopy; Microbiology; Microbiology and Parasitology; Microscopy, Fluorescence; Models, Molecular; Molecular Sequence Data; Pathogens; Protein Binding; Studies; Microbiology
• ISSN: 0950-382X; 1365-2958
• DOI: 10.1111/j.1365-2958.2006.05375.x

Summary 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.