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

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.

MeSH terms

  • Adhesins, Escherichia coli / chemistry
  • Adhesins, Escherichia coli / genetics
  • Adhesins, Escherichia coli / metabolism*
  • Amino Acid Sequence
  • Bacterial Adhesion / genetics
  • Bacterial Adhesion / physiology
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Fimbriae, Bacterial / genetics
  • Fimbriae, Bacterial / metabolism
  • Magnetic Resonance Spectroscopy
  • Microscopy, Fluorescence
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding

Substances

  • Adhesins, Escherichia coli
  • Dr adhesin, E coli
  • Escherichia coli Proteins

Associated data

  • PDB/2FVN