Biochemical typing of scrapie strains

Differences in the molecular heterogeneity of the abnormal isoforms of the prion protein, PrP super(Sc), due to differential glycosylation and partial endogenous or exogenous proteolysis have found in different scrapie strains, sources of Creutzfeldt-Jakob disease (CJD) and fatal familial insomnia (...

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Bibliographic Details
Published in:Nature (London) 1997-04, Vol.386 (6625), p.564-564
Main Authors: Somerville, Robert A, Chong, Angela, Mulqueen, Orla U, Birkett, Christopher R, Wood, Sophie C. E. R, Hope, James
Format: Article
Language:English
Subjects:
Animals
Encephalopathy, Bovine Spongiform - etiology
Glycosylation
Goats
Humanities and Social Sciences
Mice
Mice, Inbred C3H
multidisciplinary
PrPSc Proteins - chemistry
PrPSc Proteins - classification
Science
Science (multidisciplinary)
scientific-correspondence
Sheep
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Summary:Differences in the molecular heterogeneity of the abnormal isoforms of the prion protein, PrP super(Sc), due to differential glycosylation and partial endogenous or exogenous proteolysis have found in different scrapie strains, sources of Creutzfeldt-Jakob disease (CJD) and fatal familial insomnia (FFI). Recently Collinge et al. extended this analysis to include sporadic CJD and the new variant of Creutzfeldt-Jakob disease (vCJD) and found that the vCJD "type 4" pattern of PrP super(Sc) was common to mice, cats and monkeys infected with bovine spongiform encephalopathy (BSE). We have extended this analysis to include scrapie strains passaged in mice and originally derived from sheep or goats.
ISSN:0028-0836
1476-4687
DOI:10.1038/386564a0