Two alternative pathways for generating transmissible prion disease de novo

摘要

IntroductionPrevious studies established that prion disease with unique strain-specific phenotypes could be induced by in vitro-formed recombinant PrP (rPrP) fibrils with structures different from that of authentic prions, or PrP^Sc. To explain the etiology of prion diseases, new mechanism proposed that in animals the transition from rPrP fibrils to PrP^Sc consists of two main steps: the first involves fibril-induced formation of atypical PrPres, a self-replicating but clinically silent state, and the second consists of atypical PrPres-dependent formation of PrP^Sc via rare deformed templating events.