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5. Escherichia coli producing CNF1 toxin hijacks Tollip to trigger Rac1-dependent cell invasion.

Author

Visvikis O, Boyer L, Torrino S, Doye A, Lemonnier M, Lorès P, Rolando M, Flatau G, Mettouchi A, Bouvard D, Veiga E, Gacon G, Cossart P, and Lemichez E

Subjects
Animals, Cell Line, Endocytosis physiology, Humans, Intracellular Signaling Peptides and Proteins genetics, Mice, Proteins metabolism, Uropathogenic Escherichia coli cytology, rac1 GTP-Binding Protein genetics, Bacterial Infections metabolism, Bacterial Toxins metabolism, Escherichia coli Proteins metabolism, Intracellular Signaling Peptides and Proteins metabolism, Uropathogenic Escherichia coli metabolism, Uropathogenic Escherichia coli pathogenicity, rac1 GTP-Binding Protein metabolism
Abstract

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., (© 2011 John Wiley & Sons A/S.)

Published
2011
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