Functional heterogeneity of the UpaH autotransporter protein from uropathogenic Escherichia coli

Allsopp, Luke P., Beloin, Christophe, Gomes Moriel, Danilo, Totsika, Makrina, Ghigo, Jean-Marc and Schembri, Mark A. (2012) Functional heterogeneity of the UpaH autotransporter protein from uropathogenic Escherichia coli. Journal of Bacteriology, 194 21: 5769-5782. doi:10.1128/JB.01264-12

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Author Allsopp, Luke P.
Beloin, Christophe
Gomes Moriel, Danilo
Totsika, Makrina
Ghigo, Jean-Marc
Schembri, Mark A.
Title Functional heterogeneity of the UpaH autotransporter protein from uropathogenic Escherichia coli
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1098-5530
Publication date 2012-08-17
Sub-type Article (original research)
DOI 10.1128/JB.01264-12
Open Access Status File (Publisher version)
Volume 194
Issue 21
Start page 5769
End page 5782
Total pages 37
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2013
Language eng
Abstract Uropathogenic Escherichia coli (UPEC) are responsible for the majority of urinary tract infections(UTI). To cause UTI, UPEC must adhere to epithelial cells of the urinary tract and overcome the shear flow forces of urine. This function is primarily mediated by fimbrial adhesins, which mediate specific attachment to host cell receptors. Another group of adhesins that contribute to UPEC mediated UTI are autotransporter (AT) proteins. AT proteins possess a range of virulence properties such as adherence, aggregation, invasion and biofilm formation. One recently characterized AT protein of UPEC is UpaH, a large AIDA-I type AT protein that contributes to biofilm formation and bladder colonization. In this study, we have characterized a series of naturally occurring variants of UpaH. We demonstrate that extensive sequence variation exists within the passenger-encoding domain of UpaH variants from different UPEC strains. This sequence variation is associated with functional heterogeneity with respect to the ability of UpaH to mediate biofilm formation. In contrast, all of the UpaH variants examined retained a conserved ability to mediate binding to extracellular matrix (ECM) proteins. Bioinformatic analysis of the UpaH passenger domain identified a conserved region (UpaHCR) and hydrophobic region (UpaHHR). Deletion of these domains reduced biofilm formation but not binding to ECM proteins. Despite variation in upaH sequence, the transcription of upaH was repressed by a conserved mechanism involving the global regulator H-NS, and mutation of the hns gene relieved this repression. Overall, our findings shed new light on the regulation and function of the UpaH AT protein.
Keyword Biofilm
Autotransporter
Uropathogenic Escherichia coli
Adhesin
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Published ahead of print: 17 August 2012.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Tue, 02 Oct 2012, 09:46:30 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences