Prion Diseases—When Proteins Turn Lethal: Creutzfeldt–Jakob Disease (CJD) and the Quest for Classification, Diagnosis, Therapeutic Approaches, and Emerging Research

Creutzfeldt–Jakob disease (CJD) is a rare and still fatal neurodegenerative disorder caused by prion protein misfolding in the central nervous system. Accumulation of the pathogenic isoform leads to neuronal damage, spongiform degeneration, and rapidly progressive dementia. The disease is divided into sporadic, familial, iatrogenic, and variant forms, with sporadic cases accounting for the majority of cases. Diagnosis remains challenging and relies on a combination of clinical assessment, neuroimaging, and laboratory biomarkers. Key diagnostic methods include electroencephalography, Magnetic Resonance Imaging, and cerebrospinal fluid analysis for proteins as well as advanced amplification tests that improve diagnostic accuracy. Despite these advances, early detection remains challenging and misdiagnosis can occur. Currently, there is no effective disease-modifying therapy, and treatment is primarily supportive, focusing on symptom control and palliative care. Ongoing research aims to better understand the molecular mechanisms underlying prion propagation and develop targeted therapeutic strategies. This review summarizes current diagnostic methods and therapeutic approaches, focusing on molecular applications and their potential clinical implications.