Titre
Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence.
Type
article
Institution
Externe
Auteur(s)
Schwan, C.
Auteure/Auteur
Kruppke, A.S.
Auteure/Auteur
Nölke, T.
Auteure/Auteur
Schumacher, L.
Auteure/Auteur
Koch-Nolte, F.
Auteure/Auteur
Kudryashev, M.
Auteure/Auteur
Stahlberg, H.
Auteure/Auteur
Aktories, K.
Auteure/Auteur
Liens vers les personnes
ISSN
1091-6490
Statut éditorial
Publié
Date de publication
2014-02-11
Volume
111
Numéro
6
Première page
2313
Dernière page/numéro d’article
2318
Peer-reviewed
Oui
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
Résumé
Clostridium difficile causes antibiotic-associated diarrhea and pseudomembranous colitis by the actions of Rho-glucosylating toxins A and B. Recently identified hypervirulent strains, which are associated with increased morbidity and mortality, additionally produce the actin-ADP-ribosylating toxin C. difficile transferase (CDT). CDT depolymerizes actin, causes formation of microtubule-based protrusions, and increases pathogen adherence. Here we show that CDT-induced protrusions allow vesicle traffic and contain endoplasmic reticulum tubules, connected to microtubules via the calcium sensor Stim1. The toxin reroutes Rab11-positive vesicles containing fibronectin, which is involved in bacterial adherence, from basolateral to the apical membrane sides in a microtubule- and Stim1-dependent manner. The data yield a model of C. difficile adherence regulated by actin depolymerization, microtubule restructuring, subsequent Stim1-dependent Ca(2+) signaling, vesicle rerouting, and secretion of ECM proteins to increase bacterial adherence.
PID Serval
serval:BIB_35E082E739F3
PMID
Open Access
Oui
Date de création
2023-06-09T14:03:10.435Z
Date de création dans IRIS
2025-05-20T20:38:26Z