Creutzfeldt-Jacob disease is a rare, neurodegenerative, spongiform encephalopathy based on subacute infection by a pathogenic sterically altered prion protein (PrP). The disease-causing conformational change in PrP may be infection-related or due to pathogenic variants in the coding gene PRNP. Initial manifestations of the disease occur from the 3rd to the 8th decade of life, and the average age of onset is 61.5 years. Most patients die within one year of disease onset.
Creutzfeldt-Jakob disease occurs worldwide with a prevalence of approximately 1:1,000,000. Comparatively, the familial form of CJD is found in Chileans and Libyan Jews (frequency 1:20,000). The proportion of familial CJD cases is about 40-50% in Jews of Libyan origin. Approximately 10% of all cases follow an autosomal dominant mode of inheritance. In more than 70% of the worldwide investigated familial CJD cases, a pathogenic variant in the PRNP gene could be identified (E200K) that is considered to be causative. In addition, some genetic variants in the regulatory regions of the PRNP gene have recently been detected that appear to be associated with the sporadic form of CJD (sCJD). Furthermore, a variant form of CJD (vCJD) has been described in connection with BSE in cattle which appears to be transmissible and thus acquired.
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