Molecular analysis of ovine prion protein identifies similarities between BSE and an experimental isolate of natural scrapie, CH1641. [Erratum: Mar 2000, v. 81 (pt.3), p. 851.]

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 t...

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Published inJournal of general virology Vol. 80; no. 1999; pp. 1 - 4
Main Authors Hope, J, Wood, S.C.E.R, Birkett, C.R, Chong, A, Bruce, M.E, Cairns, D, Goldmann, W, Hunter, N, Bostock, C.J
Format Journal Article
LanguageEnglish
Published 1999
Subjects
animal diseases
animal health
noninfectious diseases
viral diseases of animals and humans
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Summary: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 (PrPSc) 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 (CH1641) with a very similar, but not identical, PrPSc profile to BSE but which differs from BSE in its transmission characteristics to mice.
ISSN:0022-1317
1465-2099