The bile salt sodium taurocholate induces Campylobacter jejuni outer membrane vesicle production and increases OMV‐associated proteolytic activity. (28th December 2017)
- Record Type:
- Journal Article
- Title:
- The bile salt sodium taurocholate induces Campylobacter jejuni outer membrane vesicle production and increases OMV‐associated proteolytic activity. (28th December 2017)
- Main Title:
- The bile salt sodium taurocholate induces Campylobacter jejuni outer membrane vesicle production and increases OMV‐associated proteolytic activity
- Authors:
- Elmi, Abdi
Dorey, Amber
Watson, Eleanor
Jagatia, Heena
Inglis, Neil F.
Gundogdu, Ozan
Bajaj‐Elliott, Mona
Wren, Brendan W.
Smith, David G.E.
Dorrell, Nick - Abstract:
- Abstract: Campylobacter jejuni, the leading cause of bacterial acute gastroenteritis worldwide, secretes an arsenal of virulence‐associated proteins within outer membrane vesicles (OMVs). C . jejuni OMVs contain three serine proteases (HtrA, Cj0511, and Cj1365c) that cleave the intestinal epithelial cell (IEC) tight and adherens junction proteins occludin and E‐cadherin, promoting enhanced C . jejuni adhesion to and invasion of IECs. C . jejuni OMVs also induce IECs innate immune responses. The bile salt sodium taurocholate (ST) is sensed as a host signal to coordinate the activation of virulence‐associated genes in the enteric pathogen Vibrio cholerae. In this study, the effect of ST on C . jejuni OMVs was investigated. Physiological concentrations of ST do not have an inhibitory effect on C . jejuni growth until the early stationary phase. Coculture of C . jejuni with 0.1% or 0.2% ( w / v ) ST stimulates OMV production, increasing both lipid and protein concentrations. C . jejuni ST‐OMVs possess increased proteolytic activity and exhibit a different protein profile compared to OMVs isolated in the absence of ST. ST‐OMVs exhibit enhanced cytotoxicity and immunogenicity to T84 IECs and enhanced killing of Galleria mellonella larvae. ST increases the level of mRNA transcripts of the OMVs‐associated serine protease genes and the cdtABC operon that encodes the cytolethal distending toxin. Coculture with ST significantly enhances the OMVs‐induced cleavage of E‐cadherinAbstract: Campylobacter jejuni, the leading cause of bacterial acute gastroenteritis worldwide, secretes an arsenal of virulence‐associated proteins within outer membrane vesicles (OMVs). C . jejuni OMVs contain three serine proteases (HtrA, Cj0511, and Cj1365c) that cleave the intestinal epithelial cell (IEC) tight and adherens junction proteins occludin and E‐cadherin, promoting enhanced C . jejuni adhesion to and invasion of IECs. C . jejuni OMVs also induce IECs innate immune responses. The bile salt sodium taurocholate (ST) is sensed as a host signal to coordinate the activation of virulence‐associated genes in the enteric pathogen Vibrio cholerae. In this study, the effect of ST on C . jejuni OMVs was investigated. Physiological concentrations of ST do not have an inhibitory effect on C . jejuni growth until the early stationary phase. Coculture of C . jejuni with 0.1% or 0.2% ( w / v ) ST stimulates OMV production, increasing both lipid and protein concentrations. C . jejuni ST‐OMVs possess increased proteolytic activity and exhibit a different protein profile compared to OMVs isolated in the absence of ST. ST‐OMVs exhibit enhanced cytotoxicity and immunogenicity to T84 IECs and enhanced killing of Galleria mellonella larvae. ST increases the level of mRNA transcripts of the OMVs‐associated serine protease genes and the cdtABC operon that encodes the cytolethal distending toxin. Coculture with ST significantly enhances the OMVs‐induced cleavage of E‐cadherin and occludin. C . jejuni OMVs also cleave the major endoplasmic reticulum chaperone protein BiP/GRP78 and this activity is associated with the Cj1365c protease. These data suggest that C . jejuni responds to the presence of physiological concentrations of the bile salt ST that increases OMV production and the synthesis of virulence‐associated factors that are secreted within the OMVs. We propose that these events contribute to pathogenesis. … (more)
- Is Part Of:
- Cellular microbiology. Volume 20:Number 3(2018)
- Journal:
- Cellular microbiology
- Issue:
- Volume 20:Number 3(2018)
- Issue Display:
- Volume 20, Issue 3 (2018)
- Year:
- 2018
- Volume:
- 20
- Issue:
- 3
- Issue Sort Value:
- 2018-0020-0003-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2017-12-28
- Subjects:
- bile salts -- Campylobacter -- outer membrane vesicles -- proteolytic activity
Microbiology -- Periodicals
Cytology -- Periodicals
Host-parasite relationships -- Periodicals
Microbiology -- Periodicals
Cells -- Periodicals
Microbiologie -- Périodiques
Microbiologie
Relation hôte-parasite
Cytologie
Cellule
Réponse cellulaire
Ressource Internet (Descripteur de forme)
Périodique électronique (Descripteur de forme)
579.05 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1462-5814;screen=info;ECOIP ↗
http://www.blackwell-synergy.com/issuelist.asp?journal=cmi ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-5822 ↗
https://www.hindawi.com/journals/cmi/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/cmi.12814 ↗
- Languages:
- English
- ISSNs:
- 1462-5814
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3097.933400
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 5821.xml