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Differential glycosylation of the protein (PrP) forming scrapie-associated fibrils

AFRC and MRC Neuropathogenesis Unit, Institute for Animal Health, West Mains Road, Edinburgh EH9 3JF, U.K.

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 34 000 and 29 000) of PrP can be reduced in apparent M_r to a lower M_r form (M_r 25 000) 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.

Received 5 October 1989; accepted 13 December 1989.

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