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J. Virol. doi:10.1128/JVI.01137-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

PrP^c does not mediate internalization of PrP^Sc but is required at an early stage for de novo prion infection of Rov cells

Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas; France

^* To whom correspondence should be addressed. Email: hubert.laude{at}jouy.inra.fr. d.vilette{at}envt.fr.

	Abstract

We have studied the interactions of exogenous prions with an epithelial cell line expressing PrP^c protein inducibly and permissive to infection by sheep scrapie agent. We demonstrate that abnormal PrP (PrP^Sc) and infectivity are efficiently internalized in Rov cells, whether PrP^c is expressed or not. At difference with earlier studies implicating cellular heparan sulfates in PrP^Sc internalization, we failed to evidence any involvement of such molecules in Rov cells, indicating that prions can enter target cells by several routes. We further show that PrP^Sc taken up in the absence of PrP^c was unable to promote efficient prion multiplication once PrP^c expression was restored in the cells. This observation argues that interaction of PrP^Sc with PrP^c has to occur early, in specific subcellular compartment(s) and is consistent with the view that the first prion multiplication events may occur at the cell surface.

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