Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding

Most Campylobacter jejuni isolates carry the fucose utilization cluster (Cj0480c-Cj0489) that supports the metabolism of L-fucose and D-arabinose. In this study we quantified L-fucose and D-arabinose metabolism and metabolite production, and the impact on Caco-2 cell interaction and binding to fibronectin, using C. jejuni NCTC11168 and the closely related human isolate C. jejuni strain 286. When cultured with L-fucose and D-arabinose, both isolates showed increased survival and production of acetate, pyruvate and succinate, and the respective signature metabolites lactate and glycolic acid, in line with an overall upregulation of L-fucose cluster proteins. In vitro Caco-2 cell studies and fibronectin-binding experiments showed a trend towards higher invasion and a significantly higher fibronectin binding efficacy of C. jejuni NCTC11168 cells grown with L-fucose and D-arabinose, while no significant differences were found with C. jejuni 286. Both fibronectin binding proteins, CadF and FlpA, were detected in the two isolates, but were not significantly differentially expressed in L-fucose or D-arabinose grown cells. Comparative proteomics analysis linked the C. jejuni NCTC11168 phenotypes uniquely to the more than 135-fold upregulated protein Cj0608, putative TolC-like component MacC, which, together with the detected Cj0606 and Cj0607 proteins, forms the tripartite secretion system MacABC with putative functions in antibiotic resistance, cell envelope stress response and virulence in Gram negative pathogenic bacteria. Further studies are required to elucidate the role of the MacABC system in C. jejuni cell surface structure modulation and virulence.

Saved in:
Bibliographic Details
Main Authors: Middendorf, Pjotr S., Wijnands, Lucas M., Boeren, Sjef, Zomer, Aldert L., Jacobs-Reitsma, Wilma F., den Besten, Heidy M.W., Abee, Tjakko
Format: Article/Letter to editor biblioteca
Language:English
Subjects:Food safety, Lipooligosaccharides, Pathogen, Secretion system, Survival,
Online Access:https://research.wur.nl/en/publications/activation-of-the-l-fucose-utilization-cluster-in-campylobacter-j
Tags: Add Tag
No Tags, Be the first to tag this record!
id dig-wur-nl-wurpubs-633254
record_format koha
spelling dig-wur-nl-wurpubs-6332542024-12-04 Middendorf, Pjotr S. Wijnands, Lucas M. Boeren, Sjef Zomer, Aldert L. Jacobs-Reitsma, Wilma F. den Besten, Heidy M.W. Abee, Tjakko Article/Letter to editor Heliyon 10 (2024) 16 ISSN: 2405-8440 Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding 2024 Most Campylobacter jejuni isolates carry the fucose utilization cluster (Cj0480c-Cj0489) that supports the metabolism of L-fucose and D-arabinose. In this study we quantified L-fucose and D-arabinose metabolism and metabolite production, and the impact on Caco-2 cell interaction and binding to fibronectin, using C. jejuni NCTC11168 and the closely related human isolate C. jejuni strain 286. When cultured with L-fucose and D-arabinose, both isolates showed increased survival and production of acetate, pyruvate and succinate, and the respective signature metabolites lactate and glycolic acid, in line with an overall upregulation of L-fucose cluster proteins. In vitro Caco-2 cell studies and fibronectin-binding experiments showed a trend towards higher invasion and a significantly higher fibronectin binding efficacy of C. jejuni NCTC11168 cells grown with L-fucose and D-arabinose, while no significant differences were found with C. jejuni 286. Both fibronectin binding proteins, CadF and FlpA, were detected in the two isolates, but were not significantly differentially expressed in L-fucose or D-arabinose grown cells. Comparative proteomics analysis linked the C. jejuni NCTC11168 phenotypes uniquely to the more than 135-fold upregulated protein Cj0608, putative TolC-like component MacC, which, together with the detected Cj0606 and Cj0607 proteins, forms the tripartite secretion system MacABC with putative functions in antibiotic resistance, cell envelope stress response and virulence in Gram negative pathogenic bacteria. Further studies are required to elucidate the role of the MacABC system in C. jejuni cell surface structure modulation and virulence. en application/pdf https://research.wur.nl/en/publications/activation-of-the-l-fucose-utilization-cluster-in-campylobacter-j 10.1016/j.heliyon.2024.e34996 https://edepot.wur.nl/671371 Food safety Lipooligosaccharides Pathogen Secretion system Survival https://creativecommons.org/licenses/by-nc-nd/4.0/ https://creativecommons.org/licenses/by-nc-nd/4.0/ Wageningen University & Research
institution WUR NL
collection DSpace
country Países bajos
countrycode NL
component Bibliográfico
access En linea
databasecode dig-wur-nl
tag biblioteca
region Europa del Oeste
libraryname WUR Library Netherlands
language English
topic Food safety
Lipooligosaccharides
Pathogen
Secretion system
Survival
Food safety
Lipooligosaccharides
Pathogen
Secretion system
Survival
spellingShingle Food safety
Lipooligosaccharides
Pathogen
Secretion system
Survival
Food safety
Lipooligosaccharides
Pathogen
Secretion system
Survival
Middendorf, Pjotr S.
Wijnands, Lucas M.
Boeren, Sjef
Zomer, Aldert L.
Jacobs-Reitsma, Wilma F.
den Besten, Heidy M.W.
Abee, Tjakko
Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding
description Most Campylobacter jejuni isolates carry the fucose utilization cluster (Cj0480c-Cj0489) that supports the metabolism of L-fucose and D-arabinose. In this study we quantified L-fucose and D-arabinose metabolism and metabolite production, and the impact on Caco-2 cell interaction and binding to fibronectin, using C. jejuni NCTC11168 and the closely related human isolate C. jejuni strain 286. When cultured with L-fucose and D-arabinose, both isolates showed increased survival and production of acetate, pyruvate and succinate, and the respective signature metabolites lactate and glycolic acid, in line with an overall upregulation of L-fucose cluster proteins. In vitro Caco-2 cell studies and fibronectin-binding experiments showed a trend towards higher invasion and a significantly higher fibronectin binding efficacy of C. jejuni NCTC11168 cells grown with L-fucose and D-arabinose, while no significant differences were found with C. jejuni 286. Both fibronectin binding proteins, CadF and FlpA, were detected in the two isolates, but were not significantly differentially expressed in L-fucose or D-arabinose grown cells. Comparative proteomics analysis linked the C. jejuni NCTC11168 phenotypes uniquely to the more than 135-fold upregulated protein Cj0608, putative TolC-like component MacC, which, together with the detected Cj0606 and Cj0607 proteins, forms the tripartite secretion system MacABC with putative functions in antibiotic resistance, cell envelope stress response and virulence in Gram negative pathogenic bacteria. Further studies are required to elucidate the role of the MacABC system in C. jejuni cell surface structure modulation and virulence.
format Article/Letter to editor
topic_facet Food safety
Lipooligosaccharides
Pathogen
Secretion system
Survival
author Middendorf, Pjotr S.
Wijnands, Lucas M.
Boeren, Sjef
Zomer, Aldert L.
Jacobs-Reitsma, Wilma F.
den Besten, Heidy M.W.
Abee, Tjakko
author_facet Middendorf, Pjotr S.
Wijnands, Lucas M.
Boeren, Sjef
Zomer, Aldert L.
Jacobs-Reitsma, Wilma F.
den Besten, Heidy M.W.
Abee, Tjakko
author_sort Middendorf, Pjotr S.
title Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding
title_short Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding
title_full Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding
title_fullStr Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding
title_full_unstemmed Activation of the L-fucose utilization cluster in Campylobacter jejuni induces proteomic changes and enhances Caco-2 cell invasion and fibronectin binding
title_sort activation of the l-fucose utilization cluster in campylobacter jejuni induces proteomic changes and enhances caco-2 cell invasion and fibronectin binding
url https://research.wur.nl/en/publications/activation-of-the-l-fucose-utilization-cluster-in-campylobacter-j
work_keys_str_mv AT middendorfpjotrs activationofthelfucoseutilizationclusterincampylobacterjejuniinducesproteomicchangesandenhancescaco2cellinvasionandfibronectinbinding
AT wijnandslucasm activationofthelfucoseutilizationclusterincampylobacterjejuniinducesproteomicchangesandenhancescaco2cellinvasionandfibronectinbinding
AT boerensjef activationofthelfucoseutilizationclusterincampylobacterjejuniinducesproteomicchangesandenhancescaco2cellinvasionandfibronectinbinding
AT zomeraldertl activationofthelfucoseutilizationclusterincampylobacterjejuniinducesproteomicchangesandenhancescaco2cellinvasionandfibronectinbinding
AT jacobsreitsmawilmaf activationofthelfucoseutilizationclusterincampylobacterjejuniinducesproteomicchangesandenhancescaco2cellinvasionandfibronectinbinding
AT denbestenheidymw activationofthelfucoseutilizationclusterincampylobacterjejuniinducesproteomicchangesandenhancescaco2cellinvasionandfibronectinbinding
AT abeetjakko activationofthelfucoseutilizationclusterincampylobacterjejuniinducesproteomicchangesandenhancescaco2cellinvasionandfibronectinbinding
_version_ 1819140397937459200