Abstract
Prions are the infectious agents causing transmissible spongiform encephalopathies (TSEs), which comprise human Creutzfeldt–Jakob disease (CJD), scrapie of sheep, bovine spongiform encephalopathy (BSE), and several other rare ailments of various species. According to the protein-only hypothesis (1), prions are composed solely of PrPSc, a misfolded form of the cellular protein PrPC. PrPSc typically forms highly ordered fibrillary aggregates, also termed “amyloid.” The term “prion strain” denotes individual prion isolates sharing the same PrP sequence but giving rise to distinct, stable disease traits with different incubation periods and lesion profiles upon serial transmission in congenic hosts. The propagation of different strains in mice congenic with respect to their Prnp allelotypes is difficult to explain by the protein-only hypothesis because the epigenetic strain characteristics of prions appear to dominate over the primary prion protein sequence of the infected host (2, 3).
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