An atomic resolution model for assembly, architecture, and function of the Dr adhesins.
Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.
Department of Biological Sciences, Wolfson Laboratories, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
Kirstine L
KL
Anderson
Jason
J
Billington
David
D
Pettigrew
Ernesto
E
Cota
Peter
P
Simpson
Pietro
P
Roversi
Ho An
HA
Chen
Petri
P
Urvil
Laurence
L
du Merle
Paul N
PN
Barlow
M Edward
ME
Medof
Richard A G
RA
Smith
Bogdan
B
Nowicki
Chantal
C
Le Bouguénec
Susan M
SM
Lea
Stephen
S
Matthews
D018830:Adhesins, Escherichia coli / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D018958:CD55 Antigens / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism / Q000472:pathogenicity; D010861:Fimbriae, Bacterial; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D020349:Surface Plasmon Resonance
D018830:Adhesins, Escherichia coli; D018958:CD55 Antigens; D021122:Protein Subunits