Creutzfeldt-Jakob disease: a case study

Creutzfeldt-Jakob disease (CJD) is a human prion disease that exists in four forms; sporadic, genetic, iatrogenic and variant.1 Human prion diseases share common neuropathological features such as spongiform degeneration, astrocytic gliosis and neuronal loss associated with amyloid plaques.2 The prion protein is a cellular protein that changes through an unknown mechanism from its normal structure (PrPc) to PrPsc, which is insoluble, resistant to protease degradation, accumulates is tissues and causes amyloid deposits.1 Sporadic CJD (sCJD) was first identified in the 1920’s as a rare atypical form of dementia.2 The annual UK mortality rate for sporadic CJD (sCJD) was 1.69 cases/million