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PEDS Advance Access published online on July 14, 2009
Protein Engineering Design and Selection, doi:10.1093/protein/gzp039
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© The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Review

The consequences of pathogenic mutations to the human prion protein

Marc W. van der Kamp and Valerie Daggett1

Department of Bioengineering, University of Washington, Seattle, 98195-5013 WA, USA

1 To whom correspondence should be addressed. E-mail: daggett{at}u.washington.edu

Prion diseases, in which the conformational transition of the native prion protein (PrP) to a misfolded form causes aggregation and subsequent neurodegeneration, have fascinated the scientific community as this transmissible disease appears to be purely protein-based. Disease can arise due to genetic factors only. At least 30 single point mutations have been indicated to cause disease in humans. Somehow, these mutations must influence the stability, processing and/or cellular interactions of PrP, such that aggregation can occur and disease develops. In this review, the current evidence for such effects of single point mutations is discussed, indicating that PrP can be affected in many different ways, although questions remain about the mechanism by which mutations cause disease.

Keywords: aggregation/genetics/protein stability/TSE

Received June 12, 2009; revised June 12, 2009; accepted June 17, 2009.


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