title: Prion protein glycosylation is not required for strain-specific neurotropism.
abstract: In this study, we tested the hypothesis that the glycosylation of the pathogenic isoform of the prion protein (PrP(Sc)) might encode the selective neurotropism of prion strains. We prepared unglycosylated cellular prion protein (PrP(C)) substrate molecules from normal mouse brain by treatment with PNGase F and used reconstituted serial protein cyclic misfolding amplification reactions to produce RML and 301C mouse prions containing unglycosylated PrP(Sc) molecules. Both RML- and 301C-derived prions containing unglycosylated PrP(Sc) molecules were infectious to wild-type mice, and neuropathological analysis showed that mice inoculated with these samples maintained strain-specific patterns of PrP(Sc) deposition and neuronal vacuolation. These results show that PrP(Sc) glycosylation is not necessary for strain-dependent prion neurotropism.
authors.affiliation: Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA.
authors.forename: Justin R
authors.initials: JR
authors.lastname: Piro
authors.forename: Brent T
authors.initials: BT
authors.lastname: Harris
authors.forename: Koren
authors.initials: K
authors.lastname: Nishina
authors.forename: Claudio
authors.initials: C
authors.lastname: Soto
authors.forename: Rodrigo
authors.initials: R
authors.lastname: Morales
authors.forename: Judy R
authors.initials: JR
authors.lastname: Rees
authors.forename: Surachai
authors.initials: S
authors.lastname: Supattapone
mesh_terms: D000818:Animals; D006031:Glycosylation; D051379:Mice; D009474:Neurons / Q000378:metabolism*; D009928:Organ Specificity; D011328:Prions / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D013379:Substrate Specificity
chemical_list: D011328:Prions