Prions and their partners in crime.
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.
Caughey
Byron
B
National Institute of Allergy and Infectious Disease, National Institutes of Health, Rocky Mountain Laboratories, 903 South 4th Street, Hamilton, Montana 59840, USA. bcaughey@nih.gov
Baron
Gerald S
GS
D000818:Animals; D003300:Copper / Q000378:metabolism / Q000494:pharmacology; D017261:Glycosylphosphatidylinositols / Q000378:metabolism; D006801:Humans; D008024:Ligands; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology*; D011328:Prions / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity
D017261:Glycosylphosphatidylinositols; D008024:Ligands; D011328:Prions; D003300:Copper