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Updated: Jul 18, 2026

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
Published on: October 3, 2012
Both host prion protein 131-188 subregion and prion strain characteristics regulate glycoform of PrP Sc
T Yokoyama1, K Shimada, K Masujin
1Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki, Japan. tyoko@affrc.go.jp
Abstract:
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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