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Short Communication |
1 Veterinary Laboratories Agency (VLA), Woodham Lane, Addlestone, Surrey, UK
2 VLA, Pentlands Science Park, Bush Loan, Penicuik, Midlothian, Scotland, UK
3 Moredun Research Institute, Pentlands Science Park, Bush Loan, Penicuik, Midlothian, Scotland, UK
Correspondence
Michael Stack
m.j.stack{at}vla.defra.gsi.gov.uk
During the 1980s, bovine spongiform encephalopathy (BSE)-contaminated meat and bonemeal were probably fed to sheep, raising concerns that BSE may have been transmitted to sheep in the UK. The human disease, variant Creutzfeldt–Jakob disease, arose during the BSE epidemic, and oral exposure of humans to BSE-infected tissues has been implicated in its aetiology. The concern is that sheep BSE could provide another source of BSE exposure to humans via sheep products. Two immunological techniques, Western immunoblotting (WB) and immunohistochemistry (IHC), have been developed to distinguish scrapie from cases of experimental sheep BSE by the characteristics of their respective abnormal, disease-associated prion proteins (PrPd). This study compares the WB and IHC characteristics of PrPd from brains of primary, secondary and tertiary experimental ovine BSE cases with those of cattle BSE and natural sheep scrapie. Discrimination between experimental sheep BSE and scrapie remained possible by both methods, regardless of the route of challenge.
Supplementary methods, references and figures are available with the online version of this paper.
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