Oxygen and contact with human intestinal epithelium independently stimulate virulence gene expression in enteroaggregative Escherichia coli.


Journal

Cellular microbiology
ISSN: 1462-5822
Titre abrégé: Cell Microbiol
Pays: India
ID NLM: 100883691

Informations de publication

Date de publication:
06 2019
Historique:
received: 15 06 2018
revised: 14 12 2018
accepted: 14 01 2019
pubmed: 24 1 2019
medline: 12 8 2020
entrez: 24 1 2019
Statut: ppublish

Résumé

Enteroaggregative Escherichia coli (EAEC) are important intestinal pathogens causing acute and persistent diarrhoeal illness worldwide. Although many putative EAEC virulence factors have been identified, their association with pathogenesis remains unclear. As environmental cues can modulate bacterial virulence, we investigated the effect of oxygen and human intestinal epithelium on EAEC virulence gene expression to determine the involvement of respective gene products in intestinal colonisation and pathogenesis. Using in vitro organ culture of human intestinal biopsies, we established the colonic epithelium as the major colonisation site of EAEC strains 042 and 17-2. We subsequently optimised a vertical diffusion chamber system with polarised T84 colon carcinoma cells for EAEC infection and showed that oxygen induced expression of the global regulator AggR, aggregative adherence fimbriae, E. coli common pilus, EAST-1 toxin, and dispersin in EAEC strain 042 but not in 17-2. Furthermore, the presence of T84 epithelia stimulated additional expression of the mucinase Pic and the toxins HlyE and Pet. This induction was dependent on physical host cell contact and did not require AggR. Overall, these findings suggest that EAEC virulence in the human gut is modulated by environmental signals including oxygen and the intestinal epithelium.

Identifiants

pubmed: 30673154
doi: 10.1111/cmi.13012
pmc: PMC6563437
doi:

Substances chimiques

AAP protein, E coli 0
Adhesins, Escherichia coli 0
AggR protein, E coli 0
Bacterial Toxins 0
Enterotoxins 0
Escherichia coli Proteins 0
Hemolysin Proteins 0
Trans-Activators 0
Virulence Factors 0
heat stable toxin (E coli) 0
hlyE protein, E coli 0
Pet protein, E coli EC 3.4.21.-
Serine Endopeptidases EC 3.4.21.-
Polysaccharide-Lyases EC 4.2.2.-
hyaluronate lyase EC 4.2.2.1
Oxygen S88TT14065

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e13012

Subventions

Organisme : Medical Research Council
ID : MR/J002062/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M018261/1
Pays : United Kingdom

Informations de copyright

© 2019 The Authors Cellular Microbiology Published by John Wiley & Sons Ltd.

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Auteurs

Samuel J Ellis (SJ)

Norwich Medical School, University of East Anglia, Norwich, UK.
Quadram Institute Bioscience, Norwich, UK.

Muhammad Yasir (M)

Quadram Institute Bioscience, Norwich, UK.
Institute of Microbiology and Infection, University of Birmingham, Birmingham, UK.

Douglas F Browning (DF)

Institute of Microbiology and Infection, University of Birmingham, Birmingham, UK.

Stephen J W Busby (SJW)

Institute of Microbiology and Infection, University of Birmingham, Birmingham, UK.

Stephanie Schüller (S)

Norwich Medical School, University of East Anglia, Norwich, UK.
Quadram Institute Bioscience, Norwich, UK.

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Classifications MeSH