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Science  05 Oct 2001:
Vol. 294, Issue 5540, pp. 17
DOI: 10.1126/science.294.5540.17a

The transmissible spongiform encephalopathies (TSEs), such as mad cow disease and scrapie, are thought to be caused by aberrations in the expression and conformation of the prion protein (PrP). Disease-inducing forms of the PrP can be transferred from one animal host to another, but the efficiency of disease transmission is affected by the characteristics of the endogenous PrP in the recipient.

In examining the species barrier to transmission of three nonmurine TSEs, Barron et al. discovered that a single amino acid change (from proline to leucine at position 101) in mouse PrP produced a significant reduction in the incubation period when these mice were challenged with inocula from infected hamster and sheep. The same change, however, extended the incubation time for susceptibility to a human source (a patient with variant Creutzfeldt-Jakob disease) of infectivity. The authors speculate that a structurally flexible region in PrP is particularly important in maintaining the species barrier during TSE transmission.—SMH

EMBO J.20, 5070 (2001).

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