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Journal Article

Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence

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Citation

Schwan, C., Kruppke, A. S., Nölke, A., Schumacher, L., Koch-Nolte, F., Kudryashev, M., et al. (2014). Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence. Proceedings of the National Academy of Sciences of the United States of America, 111(6), 2313-2318. doi:10.1073/pnas.1311589111.


Cite as: https://hdl.handle.net/21.11116/0000-0008-1143-9
Abstract
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 Ca2+ signaling, vesicle rerouting, and secretion of ECM proteins to increase bacterial adherence.