Abstract
Propagation of misfolded prion protein (PrP) is associated with a wide range of prion diseases in mammals. Variations in the amino acid sequence of PrP appear to play a key role in determining the disease susceptibility for any species. Several single-point mutations in PrP have been identified as protecting against prion infections, apparently by preventing PrP misfolding and/or conversion. However, the mechanism by which these mutations act to protect against disease is unclear. Here we investigate two such protective mutants: G127V, found in humans and N159D, found in canids.
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