Prion Diseases in Focus: A Review of Diagnosis and Treatment

Prion diseases, or transmissible spongiform encephalopathies (TSEs), are rare and invariably fatal neurodegenerative disorders characterized by the misfolding of the cellular prion protein (PrP C ) into its pathogenic isoform (PrP Sc ).This protein transfiguration plays a central role in disease pathogenesis and leads to progressive neuronal dysfunction and neurodegeneration.Despite advances in understanding the molecular mechanisms underlying prion diseases, accurate diagnosis remains challenging because of their clinical and pathological resemblances to other neurodegenerative disorders.This narrative review aims to recapitulate current diagnostic approaches and emerging therapeutic strategies for prion diseases.A comprehensive literature search was conducted using the PubMed database between the year 2024 and 2026 to identify recent studies on the diagnosis and treatment of prion diseases.Diagnosis depends on clinical assessment, neuroimaging, CSF biomarkers, and detection of abnormal prion proteins.Protein amplification technologies, including protein misfolding cyclic amplification (PMCA), realtime quaking-induced conversion (RT-QuIC), and timed amyloid seeding assays (tASA), have demonstrated promising diagnostic sensitivity and specificity.The potential detection of prion proteins in blood represents an important emerging approach that may enable a rapid, minimally invasive technique and help reduce the risk of iatrogenic transmission from asymptomatic individuals.Although no curative therapies currently exist, several experimental approaches targeting prion protein misfolding are under exploration.These include anti-PrP monoclonal antibodies, anti-PrP Sc compounds, polyanionic molecules, Congo red derivatives, low-molecular-weight compounds, and recombinant prion proteins designed to inhibit pathogenic conversion.