Molecular and clinical classification of human prion disease.
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.
Wadsworth
Jonathan D F
JD
MRC Prion Unit and Department of Neurodegenerative Disease, Institute of Neurology, University College, London, UK.
Hill
Andrew F
AF
Beck
Jonathan A
JA
Collinge
John
J
D000328:Adult; D000368:Aged; D000682:Amyloid / Q000032:analysis; D015153:Blotting, Western; D001923:Brain Chemistry; D002524:Cerebellar Ataxia / Q000209:etiology; D007562:Creutzfeldt-Jakob Syndrome / Q000175:diagnosis / Q000235:genetics; D003704:Dementia / Q000209:etiology; D030342:Genetic Diseases, Inborn; D020022:Genetic Predisposition to Disease; D006801:Humans; D007049:Iatrogenic Disease; D008875:Middle Aged; D009207:Myoclonus / Q000209:etiology; D014066:Palatine Tonsil / Q000737:chemistry; D011110:Polymorphism, Genetic; D018620:PrPSc Proteins / Q000032:analysis / Q000235:genetics*; D017096:Prion Diseases / Q000145:classification* / Q000175:diagnosis / Q000235:genetics*; D000072002:Prion Proteins; D011328:Prions; D011498:Protein Precursors / Q000032:analysis; D013525:Surgical Instruments; D014018:Tissue Distribution
D000682:Amyloid; C512656:PRNP protein, human; D018620:PrPSc Proteins; D000072002:Prion Proteins; D011328:Prions; D011498:Protein Precursors