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- W1617122023 abstract "The prion, the transmissible agent that causes spongiform encephalopathies is believed to be devoid of nucleic acid and identical with a modified form of the normal host protein PrPC. The “protein only” hypothesis predicts that an animal devoid of PrPC should be resistant to prion diseases. We generated homozygous PrP null mice (Prnp o/o ) mice and showed that, after inoculation with prions, they remained free of scrapie for at least 2 years while wild-type controls all died within 6 months. There was no propagation of prions in the Prnp o/o animals. Surprisingly, heterozygous Prnp o/+ mice, which express PrPC at about half the normal level, also showed enhainced resistance to scrapie disease despite high levels of infectious agent and PrPSc, a protease-resistant form of PrP, in the brain early on. After introduction of murine PrP transgenes Prnp o/o mice became highly susceptible to mouse but not to hamster prions, while the insertion of Syrian hamster PrP transgenes rendered them susceptible to hamster but to a much lesser extent to mouse prions. These complementation experiments paved the way to the application of reverse genetics. We have prepared animals transgenic for genes encoding PrP with amino terminal deletions of various lengths and have found that PrP lacking 48 amino proximal amino acids, which comprise four of the five octa repeats of PrP, is still capable of mediating susceptibility to scrapie to PrP null mice." @default.
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- W1617122023 date "1996-12-01" @default.
- W1617122023 modified "2023-10-18" @default.
- W1617122023 title "The use of transgenic mice in the investigation of transmissible spongiform encephalopathies." @default.
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