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

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Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence. / Schwan, Carsten; Kruppke, Anna S; Nölke, Thilo; Schumacher, Lucas; Nolte, Friedrich; Kudryashev, Mikhail; Stahlberg, Henning; Aktories, Klaus.

in: P NATL ACAD SCI USA, Jahrgang 111, Nr. 6, 11.02.2014, S. 2313-8.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Schwan, C, Kruppke, AS, Nölke, T, Schumacher, L, Nolte, F, Kudryashev, M, Stahlberg, H & Aktories, K 2014, 'Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence', P NATL ACAD SCI USA, Jg. 111, Nr. 6, S. 2313-8. https://doi.org/10.1073/pnas.1311589111

APA

Schwan, C., Kruppke, A. S., Nölke, T., Schumacher, L., Nolte, F., Kudryashev, M., Stahlberg, H., & Aktories, K. (2014). Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence. P NATL ACAD SCI USA, 111(6), 2313-8. https://doi.org/10.1073/pnas.1311589111

Vancouver

Schwan C, Kruppke AS, Nölke T, Schumacher L, Nolte F, Kudryashev M et al. Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence. P NATL ACAD SCI USA. 2014 Feb 11;111(6):2313-8. https://doi.org/10.1073/pnas.1311589111

Bibtex

@article{330a4bae406f4134aa221654489d4c3f,
title = "Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence",
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 Ca(2+) signaling, vesicle rerouting, and secretion of ECM proteins to increase bacterial adherence.",
keywords = "Bacterial Adhesion, Bacterial Toxins, Biological Transport, Caco-2 Cells, Calcium Signaling, Clostridium difficile, Endoplasmic Reticulum, Enterotoxins, Fibronectins, Humans, Microtubules",
author = "Carsten Schwan and Kruppke, {Anna S} and Thilo N{\"o}lke and Lucas Schumacher and Friedrich Nolte and Mikhail Kudryashev and Henning Stahlberg and Klaus Aktories",
year = "2014",
month = feb,
day = "11",
doi = "10.1073/pnas.1311589111",
language = "English",
volume = "111",
pages = "2313--8",
journal = "P NATL ACAD SCI USA",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "6",

}

RIS

TY - JOUR

T1 - Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence

AU - Schwan, Carsten

AU - Kruppke, Anna S

AU - Nölke, Thilo

AU - Schumacher, Lucas

AU - Nolte, Friedrich

AU - Kudryashev, Mikhail

AU - Stahlberg, Henning

AU - Aktories, Klaus

PY - 2014/2/11

Y1 - 2014/2/11

N2 - 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.

AB - 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.

KW - Bacterial Adhesion

KW - Bacterial Toxins

KW - Biological Transport

KW - Caco-2 Cells

KW - Calcium Signaling

KW - Clostridium difficile

KW - Endoplasmic Reticulum

KW - Enterotoxins

KW - Fibronectins

KW - Humans

KW - Microtubules

U2 - 10.1073/pnas.1311589111

DO - 10.1073/pnas.1311589111

M3 - SCORING: Journal article

C2 - 24469807

VL - 111

SP - 2313

EP - 2318

JO - P NATL ACAD SCI USA

JF - P NATL ACAD SCI USA

SN - 0027-8424

IS - 6

ER -