AustralieFrV1, Main, Exploration, bibRecord, 005314

Molecular Characterization of UpaB and UpaC, Two New Autotransporter Proteins of Uropathogenic Escherichia coli CFT073

Identifieur interne : 005314 ( Main/Exploration ); précédent : 005313; suivant : 005315

Molecular Characterization of UpaB and UpaC, Two New Autotransporter Proteins of Uropathogenic Escherichia coli CFT073

Auteurs : Luke P. Allsopp [Australie] ; Christophe Beloin [France] ; Glen C. Ulett [Australie] ; Jaione Valle [France] ; Makrina Totsika [Australie] ; Orla Sherlock [Australie] ; Jean-Marc Ghigo [France] ; Mark A. Schembri [Australie]

Source :

Infection and Immunity [ 0019-9567 ] ; 2012.

RBID : PMC:3255655

Abstract

Uropathogenic Escherichia coli (UPEC) is the primary cause of urinary tract infection (UTI) in the developed world. The major factors associated with virulence of 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. The genome-sequenced prototype UPEC strain CFT073 contains 11 putative AT-encoding genes. In this study, we have performed a detailed molecular characterization of two closely related AT adhesins from CFT073: UpaB (c0426) and UpaC (c0478). PCR screening revealed that the upaB and upaC AT-encoding genes are common in E. coli. The upaB and upaC genes were cloned and characterized in a recombinant E. coli K-12 strain background. This revealed that they encode proteins located at the cell surface but possess different functional properties: UpaB mediates adherence to several ECM proteins, while UpaC expression is associated with increased biofilm formation. In CFT073, upaB is expressed while upaC is transcriptionally repressed by the global regulator H-NS. In competitive colonization experiments employing the mouse UTI model, CFT073 significantly outcompeted its upaB (but not upaC) isogenic mutant strain in the bladder. This attenuated phenotype was also observed in single-challenge experiments, where deletion of the upaB gene in CFT073 significantly reduced early colonization of the bladder.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3255655

DOI: 10.1128/IAI.05322-11
PubMed: 21930758
PubMed Central: 3255655

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p>Uropathogenic <named-content content-type="genus-species">Escherichia coli</named-content>
 (UPEC) is the primary cause of urinary tract infection (UTI) in the developed world. The major factors associated with virulence of 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. The genome-sequenced prototype UPEC strain CFT073 contains 11 putative AT-encoding genes. In this study, we have performed a detailed molecular characterization of two closely related AT adhesins from CFT073: UpaB (c0426) and UpaC (c0478). PCR screening revealed that the <italic>upaB</italic>
 and <italic>upaC</italic>
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 K-12 strain background. This revealed that they encode proteins located at the cell surface but possess different functional properties: UpaB mediates adherence to several ECM proteins, while UpaC expression is associated with increased biofilm formation. In CFT073, <italic>upaB</italic>
 is expressed while <italic>upaC</italic>
 is transcriptionally repressed by the global regulator H-NS. In competitive colonization experiments employing the mouse UTI model, CFT073 significantly outcompeted its <italic>upaB</italic>
 (but not <italic>upaC</italic>
) isogenic mutant strain in the bladder. This attenuated phenotype was also observed in single-challenge experiments, where deletion of the <italic>upaB</italic>
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Molecular Characterization of UpaB and UpaC, Two New Autotransporter Proteins of Uropathogenic Escherichia coli CFT073

Molecular Characterization of UpaB and UpaC, Two New Autotransporter Proteins of Uropathogenic Escherichia coli CFT073

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Abstract

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