Prion-related protein scrapie

With the background of the mad cow crisis in Europe, questions relating to the prion diseases have attracted intensive interest. It is now widely accepted that prion diseases, such as Creutzfeldt-Jakob disease (CJd) in humans and bovine spongiform encephalopathy (BSE) are caused by a conformational change of the prion protein (PrP) from a normally folded cellular form, PrP ", to an alternate, aggregation-prone, pathogenic scrapie form,... 

Another group of organisms that straddle the life - non-life border are the prions. These have come to public attention recently because of their controversial association with Creutzfeld-Jacob disease (CJD), a fatal infection of the brain in humans, so-called scrapie in sheep, and bovine spongiform encephalopathy (BSE), a related disease in cattle, as discussed by Heaphy (2004) and in Prusiner (2004). Several other neurological diseases in animals and humans are also linked with prions which are proteinaceous particles and thus earbon-based. Unlike other disease-causing organisms, prions do not contain nucleic acids and consist of modified forms of normal cellular protein. They ean be ineubated in brain tissue for long periods before they have an effeet whieh involves impairment of tissue function and ultimately impairment of human/animal funetion prior to death. How prions enter the body and infeet brain tissue has not yet been aseertained in detail. 

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