Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7

Polynucleotide phosphorylase (PNPase) is reported to regulate virulence in Salmonella, Yersinia spp. and Campylobacter jejuni, yet its role in Escherichia coli O157:H7 has not been investigated. To gain insights into its roles in E. coli O157:H7 virulence, pnp deletion mutants were generated and the...

Full description

Bibliographic Details
Main Authors: Jia eHu, Meijun eZhu
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-08-01
Series:Frontiers in Microbiology
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00806/full
_version_ 1819142155645485056
author Jia eHu
Jia eHu
Meijun eZhu
author_facet Jia eHu
Jia eHu
Meijun eZhu
author_sort Jia eHu
collection DOAJ
description Polynucleotide phosphorylase (PNPase) is reported to regulate virulence in Salmonella, Yersinia spp. and Campylobacter jejuni, yet its role in Escherichia coli O157:H7 has not been investigated. To gain insights into its roles in E. coli O157:H7 virulence, pnp deletion mutants were generated and the major virulence factors were compared to their parental wild type strains. Deletion of pnp in E. coli O157:H7 dramatically decreased stx2 mRNA expression and Stx2 protein production, and impaired lambdoid prophage activation in E. coli O157:H7. Quantitative PCR further confirmed that the Stx2 phage lytic growth was repressed by pnp deletion. Consistent with reduced Stx2 production and Stx2 phage activation, the transcriptional levels of genes involved in phage lysis and replication were down-regulated. In addition, disruption of pnp in E. coli O157:H7 decreased its adhesion to intestinal epithelial cells as well as cattle colonic explant tissues. On the other hand, PNPase inactivation in E. coli O157:H7 enhanced Tir protein content and the transcription of type three secretion system components, including genes encoding intimin, Tir and EspB as well as LEE positive regulator, Ler. Collectively, data indicate that PNPase has pleiotropic effects on the virulence of E. coli O157:H7.
first_indexed 2024-12-22T12:05:51Z
format Article
id doaj.art-e6a8909fbd7d41d9853c70738d63fe17
institution Directory Open Access Journal
issn 1664-302X
language English
last_indexed 2024-12-22T12:05:51Z
publishDate 2015-08-01
publisher Frontiers Media S.A.
record_format Article
series Frontiers in Microbiology
spelling doaj.art-e6a8909fbd7d41d9853c70738d63fe172022-12-21T18:26:27ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2015-08-01610.3389/fmicb.2015.00806154382Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7Jia eHu0Jia eHu1Meijun eZhu2Washington State UniversityUniversity of WyomingWashington State UniversityPolynucleotide phosphorylase (PNPase) is reported to regulate virulence in Salmonella, Yersinia spp. and Campylobacter jejuni, yet its role in Escherichia coli O157:H7 has not been investigated. To gain insights into its roles in E. coli O157:H7 virulence, pnp deletion mutants were generated and the major virulence factors were compared to their parental wild type strains. Deletion of pnp in E. coli O157:H7 dramatically decreased stx2 mRNA expression and Stx2 protein production, and impaired lambdoid prophage activation in E. coli O157:H7. Quantitative PCR further confirmed that the Stx2 phage lytic growth was repressed by pnp deletion. Consistent with reduced Stx2 production and Stx2 phage activation, the transcriptional levels of genes involved in phage lysis and replication were down-regulated. In addition, disruption of pnp in E. coli O157:H7 decreased its adhesion to intestinal epithelial cells as well as cattle colonic explant tissues. On the other hand, PNPase inactivation in E. coli O157:H7 enhanced Tir protein content and the transcription of type three secretion system components, including genes encoding intimin, Tir and EspB as well as LEE positive regulator, Ler. Collectively, data indicate that PNPase has pleiotropic effects on the virulence of E. coli O157:H7.http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00806/fullEpitheliumShiga Toxin 2PNPaseAdhesionintestinetype III secretion system
spellingShingle Jia eHu
Jia eHu
Meijun eZhu
Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7
Frontiers in Microbiology
Epithelium
Shiga Toxin 2
PNPase
Adhesion
intestine
type III secretion system
title Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7
title_full Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7
title_fullStr Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7
title_full_unstemmed Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7
title_short Defects in Polynucleotide phosphorylase impairs virulence in Escherichia coli O157:H7
title_sort defects in polynucleotide phosphorylase impairs virulence in escherichia coli o157 h7
topic Epithelium
Shiga Toxin 2
PNPase
Adhesion
intestine
type III secretion system
url http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.00806/full
work_keys_str_mv AT jiaehu defectsinpolynucleotidephosphorylaseimpairsvirulenceinescherichiacolio157h7
AT jiaehu defectsinpolynucleotidephosphorylaseimpairsvirulenceinescherichiacolio157h7
AT meijunezhu defectsinpolynucleotidephosphorylaseimpairsvirulenceinescherichiacolio157h7