RT Journal Article SR Electronic(1) A1 Somerville, Robert A. A1 Ritchie, Lyndsay A.YR 1990 T1 Differential glycosylation of the protein (PrP) forming scrapie-associated fibrils JF Journal of General Virology, VO 71 IS 4 SP 833 OP 839 DO https://doi.org/10.1099/0022-1317-71-4-833 PB Microbiology Society, SN 1465-2099, AB PrP is a glycoprotein found in normal brain. In brain affected by scrapie it forms scrapie-associated fibrils (SAF). PrP from SAF shows considerable heterogeneity of size and charge on two-dimensional gels. It separates into six major regions, the three more acidic regions arising as a result of partial proteolytic degradation. The two more basic higher M r forms (M r 34000 and 29000) of PrP can be reduced in apparent M r to a lower M r form (M r 25000) with Peptide-N- glycosidase F. In addition, a series of lectins has been found to bind to PrP. Some bind preferentially to the higher M r forms whereas others bind more strongly to the lower M r form. Some of the heterogeneity of PrP is therefore due to differential N-glycosylation. We suggest that one or two N-linked carbohydrate chains are bound to the protein causing some of the differences in M r The major cause of heterogeneity of PrP is therefore proteolytic cleavage combined with differential glycosylation at the two potential N-glycosylation sites. The glycolipid moiety attached to PrP may be responsible for some lectin binding to all three bands. Using lectins as a probe to study potential differences in N-glycosylation we have looked at their binding to PrP isolated from SAF, from different strains of scrapie and from different regions of the same brain. No major differences in the N-glycan moieties were found., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-71-4-833