An atomic resolution model for assembly, architecture, and function of the Dr adhesins.
Anderson KL., Billington J., Pettigrew D., Cota E., Simpson P., Roversi P., Chen HA., Urvil P., du Merle L., Barlow PN., Medof ME., Smith RAG., Nowicki B., Le Bouguénec C., Lea SM., Matthews S.
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.