Prion Protein Glycosylation Is Not Required for Strain-Specific Neurotropism

Authors

Justin R. Piro, Dartmouth College
Brent T. Harris, Dartmouth College
Koren Nishina, Dartmouth College
Claudio Soto, University of Texas at Austin
Rodrigo Morales, University of Texas at Austin
Judy R. Rees, Dartmouth College
Surachai Supattapone, Dartmouth College

Document Type

Article

Publication Date

6-2009

Publication Title

Journal of Virology

Department

Geisel School of Medicine

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^Scdeposition and neuronal vacuolation. These results show that PrP^Sc glycosylation is not necessary for strain-dependent prion neurotropism.

DOI

10.1128/JVI.02502-08

Original Citation

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.
https://digitalcommons.dartmouth.edu/facoa/1187