The consequences of pathogenic mutations to the human prion protein

Marc W van der Kamp, Valerie Daggett

Research output: Contribution to journalArticle (Academic Journal)peer-review

68 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)461-8
Number of pages8
JournalProtein Engineering, Design and Selection
Issue number8
Publication statusPublished - Aug 2009


  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Humans
  • Protein Folding
  • Point Mutation
  • Protein Structure, Tertiary
  • Prions


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