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PRION DISEASES
  1. R S G Knight,
  2. R G Will
  1. National CJD Surveillance Unit, Western General Hospital, Edinburgh, UK
  1. Correspondence to:
 Dr Richard Knight
 National CJD Surveillance Unit, Bryan Matthews Building, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK; r.knighted.ac.uk

https://doi.org/10.1136/jnnp.2004.036137

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    Prion diseases or transmissible spongiform encephalopathies (table 1) are characterised by the deposition of PrPSc, an abnormal form of a normal cellular protein, PrPC. These diseases exist in sporadic (idiopathic), genetic, and acquired forms.

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    Table 1

    Prion diseases

    PRION PROTEIN

    The normal prion protein, PrPC, is encoded by the prion gene (PRNP) on human chromosome 20, with equivalent prion genes in animals. The function of PrPC is not known but it may have roles in anti-oxidant systems and cellular copper metabolism. In prion diseases, the normal host gene produces the normal host PrPC but there is then an incompletely understood post-translational conformational change to a disease related form, PrPSc. PrPSc is relatively insoluble and relatively protease resistant, and accumulates in tissues forming amyloid structures. The precise pathogenesis of the neurological illness is not known, but PrPSc deposition is associated with the neuropathological changes of neuronal loss, astrocytic gliosis, and spongiform change (fig 1). In the acquired prion diseases, material from an affected host infects another. The infective agent (termed the “prion”) has not been fully characterised, but PrPSc is associated with infectivity.

    Figure 1

    Neuropathological changes in Creutzfeld-Jakob disease (CJD). (A) sCJD: spongiform change in the frontal cortex (haematoxylin and eosin). (B) sCJD: cerebral PrP deposition (KG9 antibody). (C) vCJD: thalamus showing gliotic change (glial fibrillary acidic protein antibody). Courtesy of James Ironside and Linda McCardle, National CJD Surveillance Unit.

    Since the prion protein has such a central role, it is not surprising to find that the prion protein gene, PRNP, is also important (even in non-genetic forms of TSE). In human prion diseases, a common polymorphism at codon 129 has important effects on susceptibility to disease, the resulting clinical characteristics and the incubation period (in acquired forms). At codon 129 of …

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