Prion potentiation after life-long dormancy in mice devoid of PrP.

ABSTRACT: Prions are neurotropic pathogens composed of misfolded assemblies of the host-encoded prion protein PrP^C which replicate by recruitment and conversion of further PrP^C by an autocatalytic seeding polymerization process. While it has long been shown that mouse-adapted prions cannot replicate and are rapidly cleared in transgenic PrP^0/0 mice invalidated for PrP^C, these experiments have not been done with other prions, including from natural resources, and more sensitive methods to detect prion biological activity. Using transgenic mice expressing human PrP to bioassay prion infectivity and RT-QuIC cell-free assay to measure prion seeding activity, we report that prions responsible for the most prevalent form of sporadic Creutzfeldt-Jakob disease in

SUBMITTER: Martin D 

PROVIDER: S-EPMC8111064 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature