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Retrovirus infection strongly enhances scrapie infectivity release in cell culture
Author(s) -
Leblanc Pascal,
Alais Sandrine,
PortoCarreiro Isabel,
Lehmann Sylvain,
Grassi Jacques,
Raposo Graça,
Darlix Jean Luc
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601162
Subject(s) - biology , infectivity , virology , scrapie , endosome , retrovirus , murine leukemia virus , virus , intracellular , cell culture , microvesicles , microbiology and biotechnology , prion protein , genetics , gene , microrna , medicine , disease , pathology
Prion diseases are neurodegenerative disorders associated in most cases with the accumulation in the central nervous system of PrP Sc (conformationally altered isoform of cellular prion protein (PrP C ); Sc for scrapie), a partially protease‐resistant isoform of the PrP C . PrP Sc is thought to be the causative agent of transmissible spongiform encephalopathies. The mechanisms involved in the intercellular transfer of PrP Sc are still enigmatic. Recently, small cellular vesicles of endosomal origin called exosomes have been proposed to contribute to the spread of prions in cell culture models. Retroviruses such as murine leukemia virus (MuLV) or human immunodeficiency virus type 1 (HIV‐1) have been shown to assemble and bud into detergent‐resistant microdomains and into intracellular compartments such as late endosomes/multivesicular bodies. Here we report that moloney murine leukemia virus (MoMuLV) infection strongly enhances the release of scrapie infectivity in the supernatant of coinfected cells. Under these conditions, we found that PrP C , PrP Sc and scrapie infectivity are recruited by both MuLV virions and exosomes. We propose that retroviruses can be important cofactors involved in the spread of the pathological prion agent.