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Journal of Bacteriology, June 2008, p. 4147-4161, Vol. 190, No. 12
0021-9193/08/$08.00+0     doi:10.1128/JB.00122-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

UpaG, a New Member of the Trimeric Autotransporter Family of Adhesins in Uropathogenic Escherichia coli ^,

Institut Pasteur, Unité de Génétique des Biofilms, CNRS URA 2172, 25 Rue du Dr. Roux, F-75015 Paris, France,¹ School of Molecular and Microbial Sciences, University of Queensland, Brisbane QLD 4072, Australia,² Institut Pasteur, Unité des Interactions Bactéries-Cellules, 25 Rue du Dr. Roux, F-75015 Paris, France,³ Institut Pasteur, Unité de Résonance Magnétique Nucléaire des Biomolécules, CNRS URA 2185, 28 Rue du Dr. Roux, F-75015 Paris, France⁴

Received 24 January 2008/ Accepted 8 April 2008

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.

Published ahead of print on 18 April 2008.

Supplemental material for this article may be found at http://jb.asm.org/.

^# Present address: Laboratory of Microbial Biofilms, Instituto de Agrobiotecnologia UPNA/CSIC, Carretera Mutilva Baja sn, 31192 Multiva Baja, Spain.