Journal
ANNUAL REVIEW OF GENETICS, VOL 53
Volume 53, Issue -, Pages 117-147Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-genet-120213-092352
Keywords
prion protein gene; prion protein; genome-wide association study; quantitative trait locus; inherited prion disease; Creutzfeldt-Jakob disease
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Funding
- Medical Research Council (UK)
- MRC [MC_U123160651, G0400713, MC_UU_00024/9, MC_UU_00024/1, MC_U123160657] Funding Source: UKRI
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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.
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