Both host prion protein 131-188 subregion and prion strain characteristics regulate glycoform of PrP Sc.
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.
Yokoyama
T
T
Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki, Japan. tyoko@affrc.go.jp
Shimada
K
K
Masujin
K
K
Iwamaru
Y
Y
Imamura
M
M
Ushiki
Y K
YK
Kimura
K M
KM
Itohara
S
S
Shinagawa
M
M
D000818:Animals; D006224:Cricetinae; D017931:DNA Primers; D006023:Glycoproteins / Q000737:chemistry; D006031:Glycosylation; D051379:Mice; D010446:Peptide Fragments / Q000737:chemistry*; D011328:Prions / Q000737:chemistry*
D017931:DNA Primers; D006023:Glycoproteins; D010446:Peptide Fragments; D011328:Prions; C522835:prion protein (131-188)