A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli

Abstract Metal limitation is a common situation during infection and can have profound effects on the pathogen’s success. In this report, we examine the role of zinc limitation in the expression of a virulence factor in uropathogenic Escherichia coli. The pyelonephritis isolate J96 carries two hlyCA...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Elsa Velasco, Suning Wang, Marianna Sanet, Jorge Fernández-Vázquez, Daniel Jové, Estibaliz Glaría, Annabel F. Valledor, Thomas V. O’Halloran, Carlos Balsalobre
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
Materias:
R
Q
Acceso en línea:https://doaj.org/article/a174d76b47b34380a2431c2c2639eec8
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:a174d76b47b34380a2431c2c2639eec8
record_format dspace
spelling oai:doaj.org-article:a174d76b47b34380a2431c2c2639eec82021-12-02T15:08:39ZA new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli10.1038/s41598-018-24964-12045-2322https://doaj.org/article/a174d76b47b34380a2431c2c2639eec82018-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-24964-1https://doaj.org/toc/2045-2322Abstract Metal limitation is a common situation during infection and can have profound effects on the pathogen’s success. In this report, we examine the role of zinc limitation in the expression of a virulence factor in uropathogenic Escherichia coli. The pyelonephritis isolate J96 carries two hlyCABD operons that encode the RTX toxin α-hemolysin. While the coding regions of both operons are largely conserved, the upstream sequences, including the promoters, are unrelated. We show here that the two hlyCABD operons are differently regulated. The hly II operon is efficiently silenced in the presence of zinc and highly expressed when zinc is limited. In contrast, the hly I operon does not respond to zinc limitation. Genetic studies reveal that zinc-responsive regulation of the hly II operon is controlled by the Zur metalloregulatory protein. A Zur binding site was identified in the promoter sequence of the hly II operon, and we observe direct binding of Zur to this promoter region. Moreover, we find that Zur regulation of the hly II operon modulates the ability of E. coli J96 to induce a cytotoxic response in host cell lines in culture. Our report constitutes the first description of the involvement of the zinc-sensing protein Zur in directly modulating the expression of a virulence factor in bacteria.Elsa VelascoSuning WangMarianna SanetJorge Fernández-VázquezDaniel JovéEstibaliz GlaríaAnnabel F. ValledorThomas V. O’HalloranCarlos BalsalobreNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Elsa Velasco
Suning Wang
Marianna Sanet
Jorge Fernández-Vázquez
Daniel Jové
Estibaliz Glaría
Annabel F. Valledor
Thomas V. O’Halloran
Carlos Balsalobre
A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli
description Abstract Metal limitation is a common situation during infection and can have profound effects on the pathogen’s success. In this report, we examine the role of zinc limitation in the expression of a virulence factor in uropathogenic Escherichia coli. The pyelonephritis isolate J96 carries two hlyCABD operons that encode the RTX toxin α-hemolysin. While the coding regions of both operons are largely conserved, the upstream sequences, including the promoters, are unrelated. We show here that the two hlyCABD operons are differently regulated. The hly II operon is efficiently silenced in the presence of zinc and highly expressed when zinc is limited. In contrast, the hly I operon does not respond to zinc limitation. Genetic studies reveal that zinc-responsive regulation of the hly II operon is controlled by the Zur metalloregulatory protein. A Zur binding site was identified in the promoter sequence of the hly II operon, and we observe direct binding of Zur to this promoter region. Moreover, we find that Zur regulation of the hly II operon modulates the ability of E. coli J96 to induce a cytotoxic response in host cell lines in culture. Our report constitutes the first description of the involvement of the zinc-sensing protein Zur in directly modulating the expression of a virulence factor in bacteria.
format article
author Elsa Velasco
Suning Wang
Marianna Sanet
Jorge Fernández-Vázquez
Daniel Jové
Estibaliz Glaría
Annabel F. Valledor
Thomas V. O’Halloran
Carlos Balsalobre
author_facet Elsa Velasco
Suning Wang
Marianna Sanet
Jorge Fernández-Vázquez
Daniel Jové
Estibaliz Glaría
Annabel F. Valledor
Thomas V. O’Halloran
Carlos Balsalobre
author_sort Elsa Velasco
title A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli
title_short A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli
title_full A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli
title_fullStr A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli
title_full_unstemmed A new role for Zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic Escherichia coli
title_sort new role for zinc limitation in bacterial pathogenicity: modulation of α-hemolysin from uropathogenic escherichia coli
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/a174d76b47b34380a2431c2c2639eec8
work_keys_str_mv AT elsavelasco anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT suningwang anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT mariannasanet anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT jorgefernandezvazquez anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT danieljove anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT estibalizglaria anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT annabelfvalledor anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT thomasvohalloran anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT carlosbalsalobre anewroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT elsavelasco newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT suningwang newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT mariannasanet newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT jorgefernandezvazquez newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT danieljove newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT estibalizglaria newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT annabelfvalledor newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT thomasvohalloran newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
AT carlosbalsalobre newroleforzinclimitationinbacterialpathogenicitymodulationofahemolysinfromuropathogenicescherichiacoli
_version_ 1718388077468057600