pseudosclérose spastique

CJD is a human prion disease caused by misfolded prion proteins that accumulate in the brain, resulting in spongiform degeneration and progressive loss of function ^[1][2][3]. The sporadic form arises from spontaneous misfolding of endogenous prion protein, while familial cases stem from mutations in the prion protein gene and iatrogenic cases follow healthcare or biological-product exposure ^[1][3]. It is recognized as a fatal neurodegenerative condition with no available cure ^[2][4].

Classic Creutzfeldt-Jakob disease (CJD) is a rapidly progressive neurodegenerative prion disease that causes dementia and other neurologic problems, with death typically occurring within months to a year after symptom onset ^[1]. Clinical manifestations include psychomotor changes such as cognitive dysfunction, motor disorder, and behavioral abnormalities ^[3]. Sporadic CJD is a fatal neurodegenerative disease caused by misfolded prion proteins, and clinical diagnostic criteria rely on a combination of characteristic neuropsychiatric symptoms together with CSF proteins 14-3-3, MRI, and EEG ^[4]. The disease process involves deposition of misfolded prions in the brain causing apoptosis and spongiform changes ^[3].

Classic CJD is observed globally in older adults, with average onset in the late 60s and very few cases under age 30 ^[1]. The estimated mortality rate is about 1–2 per million people per year, and roughly 500–600 cases are reported annually in the United States ^[1]. Approximately 85% of cases are sporadic, 5–15% familial, and a small remainder iatrogenic ^[1].

The vast majority of CJD cases are sporadic (about 85%) with prion proteins misfolding endogenously for unclear reasons, while about 5-15% are familial due to inherited prion protein gene mutations ^[1]. Iatrogenic transmission occurs through contact with prions in healthcare settings or from biological products: there have been 6 known cases from surgical or medical equipment contaminated with prions from another patient, none reported since 1976 after decontamination procedure changes ^[1]. Additional iatrogenic routes include prion-contaminated human growth hormone received before 1978, dura mater grafts, and corneal transplants from unrecognized CJD donors ^[1]. No cases from contaminated equipment have been reported since enhanced decontamination, underscoring prion-control prevention ^[1].

Because most CJD is sporadic, prevention focuses on averting iatrogenic spread through prion-control measures for instruments and tissues in healthcare contexts ^[1]. Enhanced decontamination of surgical and medical equipment has eliminated reported equipment-linked cases since the late 1970s ^[1]. Avoidance of prion-contaminated biological products, such as untested grafts or historical hormone preparations, remains central to reducing acquired cases ^[1].

GlobalID source-data note: Norway MSIS publishes the source category ‘Prionsykdommer’ (prion diseases). Reported Norwegian cases have predominantly been CJD, but the category and reporting criteria can include other prion diseases; interpret the series as the official source category rather than assuming every value is a subtype-confirmed CJD case.

1. 1 US Centers for Disease Control and Prevention. Classic Creutzfeldt-Jakob Disease | Classic CJD | CDC [Internet]. cited 23 Oct 2026. Available from: https://www.cdc.gov/creutzfeldt-jakob/about/index.html
2. 2 Noor H et al. Creutzfeldt-Jakob disease: A comprehensive review of current understanding and research. J Neurol Sci. 2024 Dec 15. PMID: 39546829. doi: 10.1016/j.jns.2024.123293. PubMed: https://pubmed.ncbi.nlm.nih.gov/39546829/
3. 3 Prusiner SB et al. The prion diseases. Brain Pathol. 1998 Jul. PMID: 9669700. doi: 10.1111/j.1750-3639.1998.tb00171.x. PubMed: https://pubmed.ncbi.nlm.nih.gov/9669700/
4. 4 Hermann P et al. Biomarkers and diagnostic guidelines for sporadic Creutzfeldt-Jakob disease. Lancet Neurol. 2021 Mar. PMID: 33609480. doi: 10.1016/S1474-4422(20)30477-4. PubMed: https://pubmed.ncbi.nlm.nih.gov/33609480/