AustralieFrV1, Main, Exploration, bibRecord, 005C37

Functional Heterogeneity of the UpaH Autotransporter Protein from Uropathogenic Escherichia coli

Identifieur interne : 005C37 ( Main/Exploration ); précédent : 005C36; suivant : 005C38

Functional Heterogeneity of the UpaH Autotransporter Protein from Uropathogenic Escherichia coli

Auteurs : Luke P. Allsopp [Australie] ; Christophe Beloin [France] ; Danilo Gomes Moriel [Australie] ; Makrina Totsika [Australie] ; Jean-Marc Ghigo [France] ; Mark A. Schembri [Australie]

Source :

Journal of bacteriology [ 0021-9193 ] ; 2012.

RBID : Pascal:12-0407315

Descripteurs français

Pascal (Inist)
- Escherichia coli, Protéine, Souche uropathogène, Système sécrétion type V.

English descriptors

KwdEn :
- Escherichia coli, Protein, Type V secretion system.

Abstract

Uropathogenic Escherichia coli (UPEC) is responsible for the majority of urinary tract infections (UTI). To cause a UTI, UPEC must adhere to the epithelial cells of the urinary tract and overcome the shear flow forces of urine. This function is mediated primarily by fimbrial adhesins, which mediate specific attachment to host cell receptors. Another group of adhesins that contributes to UPEC-mediated UTI is 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 adhesininvolved-in-diffuse-adherence (AIDA-I)-type AT protein that contributes to biofilm formation and bladder colonization. In this study we 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 (UpaH^CR) and a hydrophobic region (UpaH^HR). Deletion of these domains reduced biofilm formation but not the binding to ECM proteins. Despite variation in the 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 functions of the UpaH AT protein.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3486098

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">Uropathogenic Escherichia coli (UPEC) is responsible for the majority of urinary tract infections (UTI). To cause a UTI, UPEC must adhere to the epithelial cells of the urinary tract and overcome the shear flow forces of urine. This function is mediated primarily by fimbrial adhesins, which mediate specific attachment to host cell receptors. Another group of adhesins that contributes to UPEC-mediated UTI is 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 adhesininvolved-in-diffuse-adherence (AIDA-I)-type AT protein that contributes to biofilm formation and bladder colonization. In this study we 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 (UpaH<sup>CR</sup>
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). Deletion of these domains reduced biofilm formation but not the binding to ECM proteins. Despite variation in the 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 functions of the UpaH AT protein.</div>
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Functional Heterogeneity of the UpaH Autotransporter Protein from Uropathogenic Escherichia coli

Functional Heterogeneity of the UpaH Autotransporter Protein from Uropathogenic Escherichia coli

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

	Serveur d'exploration sur les relations entre la France et l'Australie
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