Publication | Open Access
The solution structure of the invasive tip complex from Afa/Dr fibrils
46
Citations
35
References
2006
Year
Protein SecretionEngineeringInvasive Tip ComplexProtein AssemblyCell AdhesionBacteriophageMolecular BiologyCytoskeletonAfa/dr FibrilsSolution StructureBioanalysisMinimal Invasive ComplexClinical MicrobiologyBiomolecular EngineeringAfa/dr FamilyAfa/dr AdhesinsSynthetic BiologyMicrobiologyMedicine
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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