Molecular analysis of ovine prion protein identifies similarities between BSE and an experimental isolate of natural scrapie, CH 1641

Hope, J., Wood, S. C.E.R., Birkett, C. R., Chong, A., Bruce, M. E., Cairns, D., Goldmann, W., Hunter, N. and Bostock, C. J. (1999) Molecular analysis of ovine prion protein identifies similarities between BSE and an experimental isolate of natural scrapie, CH 1641. Journal of General Virology, 80 (1). pp. 1-4. ISSN 0022-1317

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Abstract

New variant Creutzfeldt-Jakob disease (vCJD) and bovine spongiform encephalopathy (BSE) are caused by the same strain of pathogen and, as sheep can develop experimental BSE, this has raised concern that humans may be at risk from eating mutton if BSE has naturally transmitted to sheep. Biochemical typing of abnormal prion proteins (PrP(Sc)) has been suggested to detect BSE in sheep. Although this approach is ingenuous, we can now report biochemical evidence of strain variation in contemporary and archival brain tissue from cases of experimental BSE or experimental and natural scrapie in sheep. Interestingly, we found at least one isolate of natural scrapie (CH 1641)with a very similar, but not identical, PrP(Sc) profile to BSE but which differs from BSE in its transmission characteristics to mice.

Item Type:	Article
Uncontrolled Keywords:	virology ,/dk/atira/pure/subjectarea/asjc/2400/2406
Faculty \ School:	Faculty of Science > School of Biological Sciences
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	05 Dec 2025 13:30
Last Modified:	05 Dec 2025 13:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/101284
DOI:	10.1099/0022-1317-80-1-1

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