Prions and their partners in crime

Nature. 2006 Oct 19;443(7113):803-10. doi: 10.1038/nature05294.


Prions, the infectious agents of transmissible spongiform encephalopathies (TSEs), have defied full characterization for decades. The dogma has been that prions lack nucleic acids and are composed of a pathological, self-inducing form of the host's prion protein (PrP). Recent progress in propagating TSE infectivity in cell-free systems has effectively ruled out the involvement of foreign nucleic acids. However, host-derived nucleic acids or other non-PrP molecules seem to be crucial. Interactions between TSE-associated PrP and its normal counterpart are also pathologically important, so the physiological functions of normal PrP and how they might be corrupted by TSE infections have been the subject of recent research.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Animals
  • Copper / metabolism
  • Copper / pharmacology
  • Glycosylphosphatidylinositols / metabolism
  • Humans
  • Ligands
  • Prion Diseases / genetics
  • Prion Diseases / metabolism*
  • Prion Diseases / pathology
  • Prion Diseases / physiopathology*
  • Prions / chemistry
  • Prions / metabolism*
  • Prions / toxicity


  • Glycosylphosphatidylinositols
  • Ligands
  • Prions
  • Copper