Summary.
Prion proteins (PrPs) contain 2 N-linked glycosylation sites and are present in cells in 3 different forms. An abnormal isoform of prion protein (PrPSc) 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 PrPSc 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 PrPC and PrPSc glycoform ratios. Furthermore, the PrPSc glycoform pattern within these transgenic mice showed a subtle difference depending on the inoculated prion. This study indicated that the PrPSc glycoform ratio was influenced by both host PrPC and the prion strain.
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Yokoyama, T., Shimada, K., Masujin, K. et al. Both host prion protein 131–188 subregion and prion strain characteristics regulate glycoform of PrPSc . Arch Virol 152, 603–609 (2007). https://doi.org/10.1007/s00705-006-0858-0
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DOI: https://doi.org/10.1007/s00705-006-0858-0