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Publication : Both host prion protein 131-188 subregion and prion strain characteristics regulate glycoform of PrP Sc.

First Author  Yokoyama T Year  2007
Journal  Arch Virol Volume  152
Issue  3 Pages  603-9
PubMed ID  17106625 Mgi Jnum  J:278321
Mgi Id  MGI:6323307 Doi  10.1007/s00705-006-0858-0
Citation  Yokoyama T, et al. (2007) Both host prion protein 131-188 subregion and prion strain characteristics regulate glycoform of PrP Sc. Arch Virol 152(3):603-9
abstractText  Prion proteins (PrPs) contain 2 N-linked glycosylation sites and are present in cells in 3 different forms. An abnormal isoform of prion protein (PrP(Sc)) has different glycoform patterns for different prion strains. However, the molecular basis of the strain-specific glycoform variability in prions has remained elusive. To understand the molecular basis of these glycoform differences, we analyzed PrP(Sc) in 2 lines of transgenic mice (MHM2 and MH2M with PrP null background) that expressed a chimeric PrP. Our result indicated that PrP 131-188 (substitutions at I139M, Y155N, and S170N) contributed to both PrP(C) and PrP(Sc) glycoform ratios. Furthermore, the PrP(Sc) glycoform pattern within these transgenic mice showed a subtle difference depending on the inoculated prion. This study indicated that the PrP(Sc) glycoform ratio was influenced by both host PrP(C) and the prion strain.
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