Abstract
Scrapie, Creutzfeldt-Jakob disease and bovine spongiform encephalopathy are the most widely known members of the family of transmissible degenerative encephalopathies. The molecular structure of the pathogen causing these diseases is unknown but its replication, and the timing of disease, is strictly controlled by host genetic loci in man, rodents and ruminants. A candidate product of these survival-time loci is PrP, a neuronal membrane protein which was originally identified as a major component of highly-purified fractions of scrapie infectivity. This protein may behave as a virus receptor and so control the cell tropism and timing of infection. Intriguingly, a spontaneous neurodegeneration, mimicking that of scrapie and its species homologues, is produced in the brains of transgenic mice which express a mutant form of PrP. This has highlighted the possibility that the disease phenotype of a viral-like infection may be mimicked by a genetic disease. To put these exciting developments into perspective, this article reviews the cell biology and pathobiology of PrP and its key role in the development of these enigmatic diseases.
Published Version
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