Prion Biology and Diseases (Cold Spring Harbor Monograph by Stanley B. Prusiner PDF

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Extra resources for Prion Biology and Diseases (Cold Spring Harbor Monograph Series)

Sample text

1996). However, such a mechanism, while accounting for specific patterns of PrPSc distribution, does not seem to influence to any measurable degree the properties of the resulting PrPSc molecule. In fact, molecular modeling and NMR structural studies may provide an explanation for such phenomena since the asparagine-linked oligosaccharides appear to be on the face of PrP opposite that where PrPC and PrPSc are expected to interact during the formation of nascent PrPSc (Huang et al. 1994, 1995; Zhang et al.

In contrast to most species-specific variations in the PrP sequence, all of the known point mutations in PrP occur either within or adjacent to regions of putative secondary structure in PrP and, as such, appear to destabilize the structure of PrP (Huang et al. 1994; Zhang et al. 1995; Riek et al. 1996). Why mutations of the PrP gene that produce seemingly unstable PrPC molecules require many decades in humans to be manifest as CNS dysfunction is unknown. In Tg(MoPrP-P101L) mice, the level of expression of the mutant transgene is inversely related to the age of disease onset.

In contrast to sheep, different breeds of cattle have no specific PrP polymorphisms. The only polymorphism recorded in cattle is a variation in the number of octarepeats: most cattle, like humans, have five octarepeats but some have six (Goldmann et al. 1991b; Prusiner et al. 1993b); however, the presence of six octarepeats does not seem to be overrepresented in BSE (Goldmann et al. 1991b; Prusiner et al. 1993b; Hunter et al. 1994). Bovine Spongiform Encephalopathy Prion strains and the species barrier are of paramount importance in understanding the BSE epidemic in Britain, in which it is estimated that almost one million cattle were infected with prions (Anderson et al.

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