Journal
JOURNAL OF VIROLOGY
Volume 83, Issue 11, Pages 5321-5328Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02502-08
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Funding
- National Institutes of Health [2R01 NS046478, R01 NS055875, T32 AI007519, R01 NS049173]
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In this study, we tested the hypothesis that the glycosylation of the pathogenic isoform of the prion protein (PrPSc) might encode the selective neurotropism of prion strains. We prepared unglycosylated cellular prion protein (PrPC) 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 PrPSc molecules. Both RML- and 301C-derived prions containing unglycosylated PrPSc molecules were infectious to wild-type mice, and neuropathological analysis showed that mice inoculated with these samples maintained strain-specific patterns of PrPSc deposition and neuronal vacuolation. These results show that PrPSc glycosylation is not necessary for strain-dependent prion neurotropism.
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