Prion diseases (e.g., Creutzfeldt-Jakob disease) are characterized by spongiform encephalopathy. The pathogenic mechanism involves:

• A Viral DNA integration causing neuronal apoptosis
• B Conformational change of normal PrPC to misfolded, protease-resistant PrPSc that templates further misfolding ✓
• C Autoantibodies against NMDA receptors causing neuronal death
• D Mitochondrial dysfunction from mtDNA mutation

Explanation

Prion diseases result from the conformational conversion of the normal cellular prion protein (PrPC, alpha-helix rich, protease-sensitive) to the misfolded scrapie isoform (PrPSc, beta-sheet rich, protease-resistant). PrPSc catalyzes the further conversion of PrPC in a self-propagating process without nucleic acid, explaining transmissibility without a conventional pathogen. Accumulation of PrPSc causes neuronal vacuolation (spongiform change), gliosis, and neuronal loss.

Reference: Robbins & Cotran Pathologic Basis of Disease, 10th ed.

High-yield for: NEET PGINI-CETNExTFMGEUSMLEPLABMRCP

Written and medically reviewed by the StethoPrep medical team.