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© J.M. Ghigo (Institut Pasteur) and Brigite Arbeille (LBC-ME. Faculté de Médecine de Tours)
Colorized scanning electron microscopy of an E. coli biofilm developing on a glass surface
Publication : Journal of bacteriology

UpaG, a new member of the trimeric autotransporter family of adhesins in uropathogenic Escherichia coli

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of bacteriology - 18 Apr 2008

Valle J, Mabbett AN, Ulett GC, Toledo-Arana A, Wecker K, Totsika M, Schembri MA, Ghigo JM, Beloin C

Link to Pubmed [PMID] – 18424525

J. Bacteriol. 2008 Jun;190(12):4147-61

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.

http://www.ncbi.nlm.nih.gov/pubmed/18424525