Analysis of the Glycosylation Profile of Disease-Associated Water-Soluble Prion Protein Using Lectins

The disease-associated water-soluble form of hamster prion protein (ws-) has recently been found to be less stable than classical . Since the stability of PrP to degradation correlates with its glycosylation level, the aim of this study was to investigate whether there are differences between the glycosylation of ws- and classical of hamster which might account for the ws- minor stability compared with that of the classical . Thus, ws-PrP and classical PrP were captured from noninfected or scrapie-infected hamster brain homogenate [high-speed supernatant () and high-speed pellet ()] and blood plasma by anti-PrP antibodies (3F4 and 6H4) and subjected to screening for glycans by lectins under denaturing or nondenaturing procedures in a sandwich lectin-ELISA. Glycans have been found in minor quantities and differently exposed on ws- from and plasma compared with classical from . These differences have been shown to be potentially responsible for the instability of ws-. Treatment of infected blood with GdnHCl significantly (P

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