title: UpaG, a new member of the trimeric autotransporter family of adhesins in uropathogenic Escherichia coli.
abstract: The ability of Escherichia coli to colonize both intestinal and extraintestinal sites is driven by the presence of specific virulence factors, among which are the autotransporter (AT) proteins. Members of the trimeric AT adhesin family are important virulence factors for several gram-negative pathogens and mediate adherence to eukaryotic cells and extracellular matrix (ECM) proteins. In this study, we characterized a new trimeric AT adhesin (UpaG) from uropathogenic E. coli (UPEC). Molecular analysis of UpaG revealed that it is translocated to the cell surface and adopts a multimeric conformation. We demonstrated that UpaG is able to promote cell aggregation and biofilm formation on abiotic surfaces in CFT073 and various UPEC strains. In addition, UpaG expression resulted in the adhesion of CFT073 to human bladder epithelial cells, with specific affinity to fibronectin and laminin. Prevalence analysis revealed that upaG is strongly associated with E. coli strains from the B2 and D phylogenetic groups, while deletion of upaG had no significant effect on the ability of CFT073 to colonize the mouse urinary tract. Thus, UpaG is a novel trimeric AT adhesin from E. coli that mediates aggregation, biofilm formation, and adhesion to various ECM proteins.
authors.affiliation: Institut Pasteur, Unité de Génétique des Biofilms, URA CNRS 2172, 25, Rue du Dr. Roux, 75724 Paris Cedex 15, France.
authors.forename: Jaione
authors.initials: J
authors.lastname: Valle
authors.forename: Amanda N
authors.initials: AN
authors.lastname: Mabbett
authors.forename: Glen C
authors.initials: GC
authors.lastname: Ulett
authors.forename: Alejandro
authors.initials: A
authors.lastname: Toledo-Arana
authors.forename: Karine
authors.initials: K
authors.lastname: Wecker
authors.forename: Makrina
authors.initials: M
authors.lastname: Totsika
authors.forename: Mark A
authors.initials: MA
authors.lastname: Schembri
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Ghigo
authors.forename: Christophe
authors.initials: C
authors.lastname: Beloin
mesh_terms: D018830:Adhesins, Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001422:Bacterial Adhesion / Q000235:genetics / Q000502:physiology; D018441:Biofilms / Q000254:growth & development; D015153:Blotting, Western; D002460:Cell Line; D019281:Dimerization; D004847:Epithelial Cells / Q000378:metabolism / Q000382:microbiology; D004926:Escherichia coli / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D004927:Escherichia coli Infections / Q000378:metabolism / Q000382:microbiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005260:Female; D005353:Fibronectins / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D007797:Laminin / Q000378:metabolism; D051379:Mice; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014551:Urinary Tract / Q000382:microbiology
chemical_list: D018830:Adhesins, Escherichia coli; D029968:Escherichia coli Proteins; D005353:Fibronectins; D007797:Laminin