Journal article

Mutated but Not Deleted Ovine PrP(C) N-Terminal Polybasic Region Strongly Interferes with Prion Propagation in Transgenic Mice.

Manal Khalifé, Fabienne Reine, Sophie Paquet-Fifield, Johan Castille, Laetitia Herzog, Marthe Vilotte, Mohammed Moudjou, Katayoun Moazami-Goudarzi, Samira Makhzami, Bruno Passet, Olivier Andréoletti, Didier Vilette, Hubert Laude, Vincent Béringue, Jean-Luc Vilotte

Journal of Virology | Published : 2016

Abstract

UNLABELLED: Mammalian prions are proteinaceous infectious agents composed of misfolded assemblies of the host-encoded, cellular prion protein (PrP). Physiologically, the N-terminal polybasic region of residues 23 to 31 of PrP has been shown to be involved in its endocytic trafficking and interactions with glycosaminoglycans or putative ectodomains of membrane-associated proteins. Several recent reports also describe this PrP region as important for the toxicity of mutant prion proteins and the efficiency of prion propagation, both in vitro and in vivo. The question remains as to whether the latter observations made with mouse PrP and mouse prions would be relevant to other PrP species/prion ..

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