The same prion strain causes vCJD and BSE

Andrew F. Hill, Melanie Desbruslais, Susan Joiner, Katie C. L. Sidle, Ian Gowland, John Collinge, Lawrence J. Doey and Peter Lantos
Additional contact information
Andrew F. Hill: Prion Disease Group, Neurogenetics Unit, Imperial College School of Medicine at St Marys
Melanie Desbruslais: Prion Disease Group, Neurogenetics Unit, Imperial College School of Medicine at St Marys
Susan Joiner: Prion Disease Group, Neurogenetics Unit, Imperial College School of Medicine at St Marys
Katie C. L. Sidle: Prion Disease Group, Neurogenetics Unit, Imperial College School of Medicine at St Marys
Ian Gowland: Prion Disease Group, Neurogenetics Unit, Imperial College School of Medicine at St Marys
John Collinge: St Mary's Hospital
Lawrence J. Doey: Institute of Psychiatry
Peter Lantos: Institute of Psychiatry

Nature, 1997, vol. 389, issue 6650, 448-450

Abstract: Abstract Epidemiological and clinicopathological studies, allied with pathological prion protein (PrPSc) analysis, strongly support the hypothesis that the human prion disease new variant Creutzfeldt-Jakob disease (vCJD) is causally related to bovine spongiform encephalopathy (BSE)1,2, but considerable controversy remains. Distinct prion strains are distinguished by their biological properties on transmission to laboratory animals and by physical and chemical differences in PrPSc strains. We now find that the biological and molecular transmission characteristics of vCJD are consistent with it being the human counterpart of BSE.

Date: 1997
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DOI: 10.1038/38925

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