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Human prion diseases: from Kuru to variant Creutzfeldt-Jakob disease.

Transmissible spongiform encephalopathies (TSEs) or prion diseases are the names given to the group of fatal neurodegenerative disorders that includes kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker disease (GSS), fatal and sporadic familial insomnia and the novel prion disease variable protease-sensitive prionopathy (PSPr) in humans. Kuru was restricted to natives of the Foré linguistic group in Papua New Guinea and spread by ritualistic endocannibalism. CJD appears as sporadic, familial (genetic or hereditary) and infectious (iatrogenic) forms. Variant CJD is a zoonotic CJD type and of major public health importance, which resulted from transmission from bovine spongiform encephalopathy (BSE) through ingestion of contaminated meat products. GSS is a slowly progressive hereditary autosomal dominant disease and the first human TSE in which a mutation in a gene encoding for prion protein (PrP) was discovered. The rarest human prion disease is fatal insomnia, which may occur, in genetic and sporadic form. More recently a novel prion disease variable protease-sensitive prionopathy (PSPr) was described in humans.TSEs are caused by a still incompletely defined infectious agent known as a "prion" which is widely regarded to be an aggregate of a misfolded isoform (PrP(Sc)) of a normal cellular glycoprotein (PrP(c)). The conversion mechanism of PrP(c) into PrP(Sc) is still not certain.

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