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Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD

J Collinge1, K C Sidle, J Meads

  • 1Neurogenetics Unit, Department of Biochemistry and Molecular Genetics, Imperial College School of Medicine at St. Mary's, London, UK. j.collinge@ic.ac.uk

Nature
|October 24, 1996
PubMed

Insights

Different strains of transmissible spongiform encephalopathies, like new variant Creutzfeldt-Jakob disease (vCJD), show distinct prion protein (PrPSc) properties. These characteristics suggest the prion protein itself may encode the disease, with BSE linked to vCJD.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are characterized by the accumulation of abnormal prion protein (PrPSc).
  • Different TSE strains exhibit distinct physicochemical properties of PrPSc.
  • These strain properties can be maintained upon transmission to transgenic mice.

Purpose of the Study:

  • To investigate the strain characteristics of PrPSc in new variant Creutzfeldt-Jakob disease (vCJD).
  • To compare vCJD strain properties with those of Bovine Spongiform Encephalopathy (BSE) and other CJD strains.
  • To explore the role of the prion protein in encoding disease phenotype.

Main Methods:

  • Physicochemical analysis of PrPSc properties.
  • Transmission studies to transgenic mice.
  • Comparative analysis of strain characteristics across different TSEs.

Main Results:

  • New variant CJD (vCJD) exhibits distinct PrPSc strain characteristics.
  • These vCJD strain characteristics resemble those of BSE transmitted to various species (mice, cats, macaques).
  • The findings are consistent with BSE being the source of vCJD.

Conclusions:

  • The prion protein (PrPSc) may directly encode the disease phenotype.
  • Strain typing of PrPSc is crucial for understanding TSE transmission and origins.
  • BSE is strongly implicated as the source of the new variant CJD epidemic.

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