Molecular analysis of ovine prion protein identifies similarities between BSE and an experimental isolate of natural scrapie, CH1641

J Hope, S C Wood, C R Birkett, A Chong, M E Bruce, D Cairns, W Goldmann, N Hunter, C J Bostock

Research output: Contribution to journalArticlepeer-review

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 (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 (CH 1641) with a very similar, but not identical, PrPsc profile to BSE but which differs from BSE in its transmission characteristics to mice.
Original languageEnglish
Pages (from-to)1-4
Number of pages4
JournalJournal of General Virology
Volume80 ( Pt 1)
Publication statusPublished - Jan 1999

Keywords

  • Animals
  • Cattle
  • Double-Blind Method
  • Encephalopathy, Bovine Spongiform
  • Glycosylation
  • Mice
  • Prions
  • Scrapie
  • Sheep

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