| Literature DB >> 31537104 |
Simon Mead1, Sarah Lloyd1, John Collinge1.
Abstract
Mammalian prion diseases are a group of neurodegenerative conditions caused by infection of the central nervous system with proteinaceous agents called prions, including sporadic, variant, and iatrogenic Creutzfeldt-Jakob disease; kuru; inherited prion disease; sheep scrapie; bovine spongiform encephalopathy; and chronic wasting disease. Prions are composed of misfolded and multimeric forms of the normal cellular prion protein (PrP). Prion diseases require host expression of the prion protein gene (PRNP) and a range of other cellular functions to support their propagation and toxicity. Inherited forms of prion disease are caused by mutation of PRNP, whereas acquired and sporadically occurring mammalian prion diseases are controlled by powerful genetic risk and modifying factors. Whereas some PrP amino acid variants cause the disease, others confer protection, dramatically altered incubation times, or changes in the clinical phenotype. Multiple mechanisms, including interference with homotypic protein interactions and the selection of the permissible prion strains in a host, play a role. Several non-PRNP factors have now been uncovered that provide insights into pathways of disease susceptibility or neurotoxicity.Entities:
Keywords: Creutzfeldt-Jakob disease; genome-wide association study; inherited prion disease; prion protein; prion protein gene; quantitative trait locus
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Year: 2019 PMID: 31537104 DOI: 10.1146/annurev-genet-120213-092352
Source DB: PubMed Journal: Annu Rev Genet ISSN: 0066-4197 Impact factor: 16.830