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- W3021469972 abstract "The transmissible agent that causes spongiform encephalopathies such as scrapie, the prion, is believed to be devoid of nucleic acid and identical with PrPSc, a modified form of PrPc. PrPc is a normal host protein encoded by a single copy gene (Prn-p) and is found predominantly on the surface of neurons. PrPSc, in contrast to PrPc, is resistant to protease and accumulates intracellularly. Prusiner proposed that PrPSc, when introduced into a nominal host, causes the conversion of PrPc or its precursor into PrPSc (”protein only” hypothesis). We generated homozygous Prn-pο/ο(“PrP knockout”) mice devoid of PrPc. Prn-pο/ο mice inoculated with mouse scrapie prions remained free of scrapie symptoms for at least 2 years while wild-type controls all died within 6 months. There was no propagation of prions in the Prn-pο/ο animals. Introduction of murine PrP transgenes rendered Prn-pο/ο mice highly susceptible to mouse but not to hamster prions, while the introduction of Syrian hamster PrP transgenes rendered them susceptible to hamster but to a much lesser extent to mouse prions. Our experiments show that PrPc, possibly at close to normal levels, is required for the usual susceptibility to scrapie and that lack of homology between incoming prions and the host’s PrP genes decreases susceptibility to disease. They also suggest that cattle or sheep devoid of the PrP gene might be viable and resistant to scrapie.KeywordsPrion DiseaseSingle Copy GeneAntisense TechnologyMixed Genetic BackgroundBovine GeneThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves." @default.
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- W3021469972 date "1997-01-01" @default.
- W3021469972 modified "2023-09-27" @default.
- W3021469972 title "Molecular Biology of Prion Diseases" @default.
- W3021469972 doi "https://doi.org/10.1007/978-94-011-5404-8_1" @default.
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