4.5 Article

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

Journal

MOLECULAR MICROBIOLOGY
Volume 62, Issue 2, Pages 356-366

Publisher

WILEY
DOI: 10.1111/j.1365-2958.2006.05375.x

Keywords

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Funding

  1. Medical Research Council [G0400926] Funding Source: researchfish
  2. MRC [G0400926] Funding Source: UKRI
  3. Medical Research Council [G0400926] Funding Source: Medline
  4. Wellcome Trust [079819] Funding Source: Medline

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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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