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Published 30 August 2004. doi:10.1083/jcb.200406078
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 166, Number 5, 743-753
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Article

 Role of lipid rafts in E-cadherin– and HGF-R/Met–mediated entry of Listeria monocytogenes into host cells

Stéphanie Seveau1, Hélène Bierne1, Stéphanie Giroux2, Marie-Christine Prévost2, and Pascale Cossart1

1 Unité des Interactions Bactéries-Cellules, Institut National de la Santé et de la Recherche Médicale (INSERM) U604
2 Plate-forme de microscopie électronique, Institut Pasteur, 75015 Paris, Cedex 15, France

Address correspondence to Pascale Cossart, Unité des Interactions Bactéries-Cellules, INSERM U604, Institut Pasteur, 75015 Paris Cedex 15, France. Tel.: 33-1-45-68-88-41. Fax: 33-1-45-68-87-06. email: pcossart{at}pasteur.fr

Listeria monocytogenes uptake by nonphagocytic cells is promoted by the bacterial invasion proteins internalin and InlB, which bind to their host receptors E-cadherin and hepatocyte growth factor receptor (HGF-R)/Met, respectively. Here, we present evidence that plasma membrane organization in lipid domains is critical for Listeria uptake. Cholesterol depletion by methyl-ß-cyclodextrin reversibly inhibited Listeria entry. Lipid raft markers, such as glycosylphosphatidylinositol-linked proteins, a myristoylated and palmitoylated peptide and the ganglioside GM1 were recruited at the bacterial entry site. We analyzed which molecular events require membrane cholesterol and found that the presence of E-cadherin in lipid domains was necessary for initial interaction with internalin to promote bacterial entry. In contrast, the initial interaction of InlB with HGF-R did not require membrane cholesterol, whereas downstream signaling leading to F-actin polymerization was cholesterol dependent. Our work, in addition to documenting for the first time the role of lipid rafts in Listeria entry, provides the first evidence that E-cadherin and HGF-R require lipid domain integrity for their full activity.

Key Words: Listeria; phagocytosis; rafts; E-cadherin; HGF-R/c-Met

Abbreviations used in this paper: DRM, detergent-resistant membrane; Ger Ger, geranylgeranylation; GM1, ganglioside 1; GPI, glycosylphosphatidylinositol; HGF, hepatocyte growth factor; HGF-R; HGF receptor; LLO, listeriolysin O; MßCD, methyl-ß-cyclodextrin; MyrPalm, myristoylation and palmitoylation; Prp, Prion protein.


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