Journal of Virology
Geisel School of Medicine
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 PrPScdeposition and neuronal vacuolation. These results show that PrPSc glycosylation is not necessary for strain-dependent prion neurotropism.
Piro JR, Harris BT, Nishina K, Soto C, Morales R, Rees JR, Supattapone S. Prion protein glycosylation is not required for strain-specific neurotropism. J Virol. 2009 Jun;83(11):5321-8. doi: 10.1128/JVI.02502-08. Epub 2009 Mar 18. PMID: 19297485; PMCID: PMC2681931.
Dartmouth Digital Commons Citation
Piro, Justin R.; Harris, Brent T.; Nishina, Koren; Soto, Claudio; Morales, Rodrigo; Rees, Judy R.; and Supattapone, Surachai, "Prion Protein Glycosylation Is Not Required for Strain-Specific Neurotropism" (2009). Dartmouth Scholarship. 1187.