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process whereby a portion of its ␣-helical and coil structure is refolded into ␤ sheet (Pan et al., 1993). This struc- ‡ Department of Pathology § Department of Molecular and Cellular Pharmacology tural transition is accompanied by profound changes in the physicochemical properties of the PrP. While PrP C

Transgenic (Tg) mice expressing human (Hu) and chimeric prion protein (PrP) genes were inoculated with brain extracts from humans with inherited or sporadic prion disease to investigate the mechanism by which PrPC is transformed into PrPSc. Although Tg(HuPrP) mice expressed high levels of HuPrPC, they were resistant to human prions. They became susceptible to human prions upon ablation of the mouse (Mo) PrP gene. In contrast, mice expressing low levels of the chimeric transgene were susceptible to human prions and registered only a modest decrease in incubation times upon MoPrP gene disruption. These and other findings argue that a species-specific macromolecule, provisionally designated protein X, participates in prion formation. While the results demonstrate that PrPSc binds to PrPC in a region delimited by codons 96 to 167, they also suggest that PrPC binds protein X through residues near the C-terminus. Protein X might function as a molecular chaperone in the formation of PrPSc.

No abstract

We describe fast new algorithms to implement recent cryptosystems based on the Tate pairing. In particular, our techniques improve pairing evaluation speed by a factor of about 55 compared to previously known methods in characteristic 3, and attain performance comparable to that of RSA in larger characteristics. We also propose faster algorithms for scalar multiplication in characteristic 3 and square root extraction over Fpm , the latter technique being also useful in contexts other than that of pairing-based cryptography.