The elusive role of the prion protein and the mechanism of toxicity in prion disease

[PrP.sup.Sc], a misfolded, aggregation-prone isoform of the cellular prion protein ([PrP.sup.C]), is the infectious prion agent responsible for incurable brain diseases such as scrapie of sheep, bovine spongiform encephalopathy, and its human counterpart, variant Creutzfeldt-Jakob disease. In these...

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Bibliographic Details
Published in:PLoS pathogens 2015-05, Vol.11 (5), p.e1004745-e1004745
Main Author: Chiesa, Roberto
Format: Article
Language:English
Subjects:
Animals
Brain diseases
Creutzfeldt-Jakob disease
Health aspects
Humans
Identification and classification
Models, Theoretical
Neurons - metabolism
Pearls
Physiological aspects
Prion Diseases - metabolism
Prions
Prions (Proteins)
Prions - metabolism
Protein folding
Proteostasis Deficiencies
PrPC Proteins - metabolism
Rodents
Toxicity
Zebrafish
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Summary:[PrP.sup.Sc], a misfolded, aggregation-prone isoform of the cellular prion protein ([PrP.sup.C]), is the infectious prion agent responsible for incurable brain diseases such as scrapie of sheep, bovine spongiform encephalopathy, and its human counterpart, variant Creutzfeldt-Jakob disease. In these disorders, collectively known as prion diseases, exogenous [PrP.sup.Sc] propagates in the infected host by imprinting its aberrant conformation onto endogenous [PrP.sup.C], eventually triggering a rapidly progressing neurodegenerative process that invariably leads to death. But what is the function of [PrP.sup.C] besides serving as a substrate for the generation of [PrP.sup.Sc]? And how does [PrP.sup.C] misfolding cause neurological disease?
ISSN:1553-7374
1553-7366
1553-7374
DOI:10.1371/journal.ppat.1004745