Abstract
Five mouse scrapie strains, a mouse-passaged scrapie isolate derived from a field case in sheep in Germany, and 2 mouse-passaged bovine spongiform encephalopathy (BSE) isolates were analyzed by immunoblot in regards to banding patterns of proteinase K-digested pathologic prion proteins (PrPres). To obtain reliable results, the photo-imager technique was used for measurement of staining band intensities. Distinct and reproducible profiles were observed for the different strains or isolates. A British and a German BSE isolate were similar, suggesting the same source of infection. The German scrapie isolate resembled scrapie strain ME7, which has frequently been isolated from sheep scrapie in the past. In selected strains or isolates, no influence of the mouse lines used was observed on PrPres profiles, nor were brain region-specific differences apparent. This investigation suggests that PrPres glycotyping can be an invaluable tool for the in vitro differentiation of BSE and scrapie isolates.
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