Prion Diseases

Trevor A. Crowell, M.D.


  • Prions are abnormally folded versions of cell membrane proteins otherwise normally found throughout the human body.
    • Abnormal versions are resistant to most types of proteolytic degradation, including resistance to many chemicals and physical methods of inactivation.
    • The origin of initial conversion to the abnormal version is unclear but, once present, can induce the conversion of nearby proteins from the normal cellular prion protein (PrPC) form to the abnormal and infective prion scrapie (PrPSc) form.
    • Normal PrPC and abnormal PrPSc forms share identical protein primary structures, so the abnormal PrPSc does not seem to trigger an immune response.
    • Normal PrPC plays an important role in the organogenesis and development of the central nervous system; it also affects the pathogenesis of neurodegenerative diseases and cancers
  • Prions cause transmissible spongiform encephalopathies (TSEs).
  • Epidemiology: Annual incidence is about 1.2 cases per million people in the U.S.; it increases with age.

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Last updated: May 19, 2023