Molecular and clinical classification of human prion disease

Br Med Bull. 2003:66:241-54. doi: 10.1093/bmb/66.1.241.

Abstract

While rare in humans, the prion diseases have become an area of intense clinical and scientific interest. The recognition that variant Creutzfeldt-Jakob disease is caused by the same prion strain as bovine spongiform encephalopathy in cattle has dramatically highlighted the need for a precise understanding of the molecular biology of human prion diseases. Detailed clinical, pathological and molecular data from a large number of human prion disease cases have shown that distinct abnormal isoforms of prion protein are associated with prion protein gene polymorphism and neuropathological phenotypes. A molecular classification of human prion diseases seems achievable through characterisation of structural differences of the infectious agent itself.

Publication types

  • Review

MeSH terms

  • Adult
  • Aged
  • Amyloid / analysis
  • Blotting, Western
  • Brain Chemistry
  • Cerebellar Ataxia / etiology
  • Creutzfeldt-Jakob Syndrome / diagnosis
  • Creutzfeldt-Jakob Syndrome / genetics
  • Dementia / etiology
  • Genetic Diseases, Inborn
  • Genetic Predisposition to Disease
  • Humans
  • Iatrogenic Disease
  • Middle Aged
  • Myoclonus / etiology
  • Palatine Tonsil / chemistry
  • Polymorphism, Genetic*
  • PrPSc Proteins / analysis
  • PrPSc Proteins / genetics*
  • Prion Diseases / classification*
  • Prion Diseases / diagnosis
  • Prion Diseases / genetics*
  • Prion Proteins
  • Prions
  • Protein Precursors / analysis
  • Surgical Instruments
  • Tissue Distribution

Substances

  • Amyloid
  • PRNP protein, human
  • PrPSc Proteins
  • Prion Proteins
  • Prions
  • Protein Precursors