The solution structure of the invasive tip complex from Afa/Dr fibrils.
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.
Cota
Ernesto
E
Division of Molecular Biosciences, Biochemistry Building, Imperial College London, South Kensington, London SW7 2AZ, UK.
Jones
Celine
C
Simpson
Peter
P
Altroff
Harri
H
Anderson
Kirstine L
KL
du Merle
Laurence
L
Guignot
Julie
J
Servin
Alain
A
Le Bouguénec
Chantal
C
Mardon
Helen
H
Matthews
Stephen
S
D018830:Adhesins, Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion / Q000235:genetics / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding
D018830:Adhesins, Escherichia coli; C465564:Dr adhesin, E coli; D029968:Escherichia coli Proteins