UpaH is a newly identified autotransporter protein that contributes to biofilm formation and bladder colonization by uropathogenic Escherichia coli CFT073

Allsopp, Luke P., Totsika, Makrina, Tree, Jai J., Ulett, Glen C., Mabbett, Amanda N., Wells, Timothy J., Kobe, Bostjan, Beatson, Scott A. and Schembri, Mark A. (2010) UpaH is a newly identified autotransporter protein that contributes to biofilm formation and bladder colonization by uropathogenic Escherichia coli CFT073. Infection and Immunity, 78 4: 1659-1669. doi:10.1128/IAI.01010-09

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ201640_OA.pdf Full text (open access) application/pdf 2.59MB 0

Author Allsopp, Luke P.
Totsika, Makrina
Tree, Jai J.
Ulett, Glen C.
Mabbett, Amanda N.
Wells, Timothy J.
Kobe, Bostjan
Beatson, Scott A.
Schembri, Mark A.
Title UpaH is a newly identified autotransporter protein that contributes to biofilm formation and bladder colonization by uropathogenic Escherichia coli CFT073
Formatted title
UpaH is a newly identified autotransporter protein that contributes to biofilm formation and bladder colonization by uropathogenic Escherichia coli CFT073
Journal name Infection and Immunity   Check publisher's open access policy
ISSN 1098-5522
1070-6313
Publication date 2010-04-01
Sub-type Article (original research)
DOI 10.1128/IAI.01010-09
Open Access Status File (Publisher version)
Volume 78
Issue 4
Start page 1659
End page 1669
Total pages 11
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2011
Language eng
Formatted abstract
Escherichia coli is the primary cause of urinary tract infection (UTI) in the developed world. The major factors associated with virulence of uropathogenic E. coli (UPEC) are fimbrial adhesins, which mediate specific attachment to host receptors and trigger innate host responses. Another group of adhesins is represented by the autotransporter (AT) subgroup of proteins. In this study, we identified a new AT-encoding gene, termed upaH, present in a 6.5-kb unannotated intergenic region in the genome of the prototypic UPEC strain CFT073. Cloning and sequencing of the upaH gene from CFT073 revealed an intact 8.535-kb coding region, contrary to the published genome sequence. The upaH gene was widely distributed among a large collection of UPEC isolates as well as the E. coli Reference (ECOR) strain collection. Bioinformatic analyses suggest β-helix as the predominant structure in the large N-terminal passenger (α) domain and a 12-strand β-barrel for the C-terminal β-domain of UpaH. We demonstrated that UpaH is expressed at the cell surface of CFT073 and promotes biofilm formation. In the mouse UTI model, deletion of the upaH gene in CFT073 and in two other UPEC strains did not significantly affect colonization of the bladder in single-challenge experiments. However, in competitive colonization experiments, CFT073 significantly outcompeted its upaH isogenic mutant strain in urine and the bladder.
Copyright © 2010, American Society for Microbiology. All Rights Reserved.
Keyword Urinary-tract-infections
Antigen-43-mediated autoaggregation
Bacterial adhesins
Crystal-structures
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Chemistry and Molecular Biosciences
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 48 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 51 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sun, 04 Apr 2010, 10:04:47 EST