CreutzfeldtJakobachtige

Creutzfeldt-Jakob disease (CJD) is a rare, fatal neurodegenerative disorder caused by prions, misfolded proteins that accumulate in the brain and cause rapid neuronal damage. The condition is transmissible only in rare circumstances and is not caused by a conventional infectious agent like a bacterium or virus.

Most cases are sporadic. Familial CJD results from PRNP gene mutations; iatrogenic CJD has occurred after contaminated medical procedures; a variant form (vCJD) is linked to exposure to bovine spongiform encephalopathy (mad cow disease).

Clinical onset includes rapidly progressive dementia, memory impairment, and personality changes, with movement disorders such as myoclonus, ataxia, and visual or speech disturbances. The course is typically months, with most patients dying within a year.

Diagnosis combines clinical features with investigations: MRI often shows cortical ribboning and basal ganglia hyperintensity on diffusion-weighted imaging; EEG may show periodic sharp waves; CSF 14-3-3 can support the diagnosis, and RT-QuIC is highly specific. Brain biopsy is rarely needed.

Pathology shows spongiform changes and PrPSc deposition, with little inflammatory response.

There is no approved treatment to halt progression. Care is supportive, focusing on symptom control, nutrition, hydration, safety, and caregiver support. Median survival is several months to about a year from onset.

Public health efforts emphasize preventing iatrogenic transmission and variant CJD through strict sterilization and surveillance of food sources, with ongoing research into diagnostics and potential therapies.

Epidemiology: incidence is about one case per million people per year; sporadic CJD accounts for the majority, with rarer familial, iatrogenic, and variant forms.