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First published online April 16, 2004
doi: 10.1242/10.1242/jcs.01066

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Unconventional myosin VIIa and vezatin, two proteins crucial for Listeria entry into epithelial cells

¹ Unité des Interactions Bactéries-Cellules, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris CEDEX 15, France
² Unité de Génétique des Déficits Sensoriels, Institut Pasteur, 25-28 rue du Dr Roux, 75724 Paris CEDEX 15, France

^* Authors for correspondence (e-mails: pcossart{at}pasteur.fr; mlecuit{at}pasteur.fr)

Accepted 17 December 2003

Listeria monocytogenes is a bacterial pathogen with the capacity to invade non-phagocytic cells. This dynamic process involves coordinated membrane remodelling and actin cytoskeleton rearrangements. Although some of the molecular factors promoting these events have been identified, the driving force allowing internalization is unknown. One of the receptors for L. monocytogenes on epithelial cells is E-cadherin, a transmembrane protein normally involved in homophilic interactions that allow cell-cell contacts at the adherens junctions. E-cadherin has to be connected to the actin cytoskeleton to mediate strong cell-cell adhesion and to trigger Listeria entry; - and ß-catenins play key roles in these processes. We have recently identified an unconventional myosin, myosin VIIa and its ligand vezatin, at the adherens junctions of polarized epithelial cells. Here, we demonstrate by pharmacological and genetic approaches that both myosin VIIa and vezatin are crucial for Listeria internalization. These results provide the first evidence for the role of an unconventional myosin in bacterial internalization and a novel example of the exploitation of mammalian proteins, by a pathogen, to establish a successful infection.

Key words: E-cadherin, Listeria, Myosin, Vezatin, Phagocytosis

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