Atypical scrapie isolates involve a uniform prion species with a complex molecular signature

The pathobiology of atypical scrapie, a prion disease affecting sheep and goats, is still poorly understood. In a previous study, we demonstrated that atypical scrapie affecting small ruminants in Switzerland differs in the neuroanatomical distribution of the pathological prion protein (PrP(d)). To...

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Bibliographic Details
Published in:PloS one 2011-11, Vol.6 (11), p.e27510-e27510
Main Authors: Götte, Dorothea R, Benestad, Sylvie L, Laude, Hubert, Zurbriggen, Andreas, Oevermann, Anna, Seuberlich, Torsten
Format: Article
Language:English
Subjects:
Anatomy
Animal diseases
Animals
Biology
Blotting, Western
Bovine spongiform encephalopathy
BSE
Cattle
Creutzfeldt-Jakob disease
Disease transmission
Electrophoresis, Polyacrylamide Gel
Endopeptidase K
Endopeptidase K - metabolism
Gel electrophoresis
Genetic engineering
Goats
Immunohistochemistry
Laboratories
Life Sciences
Medicine
Mice
Ovis aries
Pathology
Peptides
Prion protein
Prions (Proteins)
Prions - metabolism
Proteinase
Scrapie
Scrapie - metabolism
Sheep
Sodium lauryl sulfate
Transgenic mice
Veterinary Science
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Summary:The pathobiology of atypical scrapie, a prion disease affecting sheep and goats, is still poorly understood. In a previous study, we demonstrated that atypical scrapie affecting small ruminants in Switzerland differs in the neuroanatomical distribution of the pathological prion protein (PrP(d)). To investigate whether these differences depend on host-related vs. pathogen-related factors, we transmitted atypical scrapie to transgenic mice over-expressing the ovine prion protein (tg338). The clinical, neuropathological, and molecular phenotype of tg338 mice is similar between mice carrying the Swiss atypical scrapie isolates and the Nor98, an atypical scrapie isolate from Norway. Together with published data, our results suggest that atypical scrapie is caused by a uniform type of prion, and that the observed phenotypic differences in small ruminants are likely host-dependant. Strikingly, by using a refined SDS-PAGE technique, we established that the prominent proteinase K-resistant prion protein fragment in atypical scrapie consists of two separate, unglycosylated peptides with molecular masses of roughly 5 and 8 kDa. These findings show similarities to those for other prion diseases in animals and humans, and lay the groundwork for future comparative research.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0027510