NR AWVF
AU Yokoyama,T.; Shimada,K.; Masujin,K.; Iwamaru,Y.; Imamura,M.; Ushiki,Y.K.; Kimura,K.M.; Itohara,S.; Shinagawa,M.
TI Both host prion protein 131-188 subregion and prion strain characteristics regulate glycoform of PrPsc
QU Archives of Virology 2007 Mar; 152(3): 603-9
PT journal article; research support, non-u.s. gov't
AB 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.
MH Animals; Cricetinae; DNA Primers; Glycoproteins/chemistry; Glycosylation; Mice; Peptide Fragments/*chemistry; Prions/*chemistry
AD Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki, Japan. tyoko@affrc.go.jp
SP englisch
PO Österreich