| Literature DB >> 32958232 |
Hamza Arshad1, Matthew E C Bourkas1, Joel C Watts2.
Abstract
The transmission of prions between species is typically an inefficient process due to the species barrier, which represents incompatibility between prion seed and substrate molecules. Bank voles (Myodes glareolus) are an exception to this rule, as they are susceptible to a diverse range of prion strains from many different animal species. In particular, bank voles can be efficiently infected with most types of human prions and have played a critical role in validating variably protease-sensitive prionopathy (VPSPr) and certain forms of Gerstmann-Sträussler-Scheinker (GSS) disease as bona fide prion disorders rather than non-transmissible proteinopathies. The bank vole prion protein (BVPrP) confers a "universal prion acceptor" phenotype when expressed in mice and when used as a substrate for in vitro prion amplification assays, indicating that the unique prion transmission properties of bank voles are mediated by BVPrP. Over-expression of BVPrP in mice can also promote the spontaneous development of prion disease, indicating that BVPrP is intrinsically prone to both spontaneous and template-directed misfolding. Here, we discuss the utility of bank voles and BVPrP for prion research and how they have provided new tools for establishing rapid animal bioassays, modeling spontaneous prion disease, standardizing prion diagnostics, and understanding the molecular basis of the species barrier.Entities:
Keywords: Bank vole; Bioassay; Creutzfeldt-Jakob Disease; PMCA; Prion; Protein misfolding; RT-QuIC; Strain; Transgenic mice; Transmission
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Year: 2020 PMID: 32958232 DOI: 10.1016/bs.pmbts.2020.08.009
Source DB: PubMed Journal: Prog Mol Biol Transl Sci ISSN: 1877-1173 Impact factor: 3.622