Published 2011
| Version v1
Journal article
Escherichia coli Producing CNF1 Toxin Hijacks Tollip to Trigger Rac1-Dependent Cell Invasion
Contributors
Others:
- Centre méditérannéen de médecine moléculaire (C3M) ; Université Nice Sophia Antipolis (1965 - 2019) (UNS) ; COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)
- Université Paris Descartes - Paris 5 (UPD5)
- Université de Nice Sophia-Antipolis (UNSA)
- Université Joseph Fourier - Grenoble 1 (UJF)
- Interactions Bactéries-Cellules (UIBC) ; Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)
- conseil regional PACA; Conseil general des Alpes-Maritimes; INSERM; Agence Nationale de la Recherche [ANR A05135AS, R07120AA, R07113AS]; Association pour la Recherche sur le Cancer [ARC 4906]; Ligue Nationale contre le Cancer
Description
Rho GTPases, which are master regulators of both the actin cytoskeleton and membrane trafficking, are often hijacked by pathogens to enable their invasion of host cells. Here we report that the cytotoxic necrotizing factor-1 (CNF1) toxin of uropathogenic Escherichia coli (UPEC) promotes Rac1-dependent entry of bacteria into host cells. Our screen for proteins involved in Rac1-dependent UPEC entry identifies the Toll-interacting protein (Tollip) as a new interacting protein of Rac1 and its ubiquitinated forms. We show that knockdown of Tollip reduces CNF1-induced Rac1-dependent UPEC entry. Tollip depletion also reduces the Rac1-dependent entry of Listeria monocytogenes expressing InlB invasion protein. Moreover, knockdown of Tollip, Tom1 and clathrin, decreases CNF1 and Rac1-dependent internalization of UPEC. Finally, we show that Tollip, Tom1 and clathrin associate with Rac1 and localize at the site of bacterial entry. Collectively, these findings reveal a new link between Rac1 and Tollip, Tom1 and clathrin membrane trafficking components hijacked by pathogenic bacteria to allow their efficient invasion of host cells.
Abstract
International audienceAdditional details
Identifiers
- URL
- https://hal.inrae.fr/hal-02651745
- URN
- urn:oai:HAL:hal-02651745v1