MIC1007 PRION DISEASE

Описание: GROUP 2

Members:
1. OMAR BIN IDI FAZLUL - 24002149
2. KOAY JIA YAN - 25006499
3. NUR ERIYANA BINTI MOHD ISMAIL - 24002258
4. AINUL MARDHIYAH BINTI MOHD FARIZAN -
25006501
5. SITI NURUL NAJIHAH BINTI KHAIRUL ANWAR -
24002847
6. KASIH AMANI BINTI MUDZAFFAR - 24002416

Prion diseases represent a unique class of fatal neurodegenerative disorders caused by "prions," defined as proteinaceous infectious particles that lack DNA or RNA. Unlike conventional pathogens, prions arise from the misfolding of a normal host-encoded protein (PrPc) into a pathological isoform (PrPsc). This transition involves a structural shift from a soluble, alpha-helix-rich state to an insoluble, beta-sheet-rich conformation that acts as a template to induce further misfolding. Because the infectious agent is a host protein, the immune system fails to recognize it as foreign, resulting in no inflammatory response.

Pathologically, the accumulation of these aggregates leads to amyloid fibril formation, neuronal apoptosis, and characteristic
"spongiform" (hole-like) degeneration of brain tissue. Human manifestations are classified by etiology: sporadic forms such as Sporadic Creutzfeldt-Jakob Disease (sCJD), which accounts for the majority of cases; genetic forms including Fatal Familial Insomnia (FFI); and acquired forms like Kuru and Variant CJD (VCJD).

Clinically, patients present with rapid dementia, ataxia, and myoclonus. Diagnosis is supported by specific markers: MRI showing cortical ribboning, EEG displaying periodic sharp wave complexes, and CSF analysis for biomarkers like 14-3-3 or RT-QUIC activity. Currently, there is no curative treatment, and management is strictly supportive. However, understanding these agents is critical for developing sterilization protocols effective against their extreme resistance to heat and radiation, and serves as a model for other protein-misfolding disorders like Alzheimer's disease.