PRIONS-compressed
Overview
Title: Group 2 BS Biology 2C
Kuru Disease
Observation: In the 1950s, a medical officer in New Guinea identified a fatal disease in the Fore tribe called kuru (which means "trembling in fear").
Symptoms: Initial inability to walk, followed by loss of swallowing ability, significant weight loss, and death.
Cause: Kuru is a prion disease caused by abnormal prion proteins.
Understanding Prions
Definition and Properties
Prion: Short for Proteinaceous Infectious Particle, responsible for Transmissible Spongiform Encephalopathies (TSE), affecting the central nervous system.
Mechanism: Prions become abnormal, clump together, and cause brain damage, leading to memory issues, personality changes, and movement difficulties.
Fatal Nature: These disorders are often fatal; prion diseases are not well understood.
Structure of Prion Protein
Normal Form (PrPC): 200-250 amino acids, twisted into helices.
Infectious Form (PrPSc): Configured differently but composed of the same amino acids; significantly smaller than the smallest virus.
Genes Related to Prions
Prnp: Encodes normal prion protein (PrPC) on chromosome 2 (mice) and chromosome 20 (humans).
Prnd: Encodes Doppel, related to male reproductive health.
Sprn: Encodes a protein called Shadoo, expressed in the central nervous system.
Properties of Prions
Nucleic Acid: Prions do not contain DNA or RNA.
Resistance: Highly resistant to heat, chemicals, and biologically difficult to decompose. Remain in soil for years.
Discovery of Prions
Introduction: Discovered by Stanley Prusiner in 1982 during studies on scrapie (a sheep neurological disorder).
Nobel Prize: Prusiner was awarded the Nobel Prize in Physiology or Medicine in 1997 for this discovery.
Nature of Pathogenicity: Misfolded proteins cause similar proteins to misfold, leading to diseases.
Prion Forms
Two forms: PrP-sen (sensitive) and PrP-res (resistant)
PrP-sen: normal form found mainly in neurons.
PrP-res: Disease-causing form, resistant to breakdown, leading to spongiform disease.
Pathological Effects of Prions
Amyloid Fibers: Toxic to cells, leading to cell death. Abnormal protein accumulation results in neuron damage.
Cellular Response: Astrocytes digest neurons, leaving 'holes' in the brain, while amyloid fibers persist.
Prion Propagation
Mechanism: When a prion enters a healthy organism, it induces normal proteins to misfold, thereby creating more infectious prions, which then propagate.
Chain Reaction: This process triggers extensive production of prion forms, leading to widespread dysfunction.
Prion Diseases in Humans and Animals
Major Diseases
Transmissible Spongiform Encephalopathies (TSEs): Including Creutzfeldt-Jakob Disease (CJD) and Kuru. All are untreatable and fatal.
Bovine Spongiform Encephalopathy (BSE): Transmissible through contaminated feed leading to neurological degeneration in cattle, often resulting in severe symptoms and death.
Common Symptoms Across Prion Diseases
Memory issues, motor dysfunction, behavioral changes, and severe cognitive decline.
Infection typically leads to a rapid progression of symptoms, usually resulting in death within months.
Case Studies and Epidemiology
Case Report Highlights
CJD Case: Diagnosis based on clinical evaluation and CSF analysis, confirmed via autopsy.
Kuru: Symptoms evolve through stages, initiated by cannibalism in New Guinea.
Fatal Familial Insomnia (FFI): Linked to genetic mutations in the PRNP gene; symptoms include severe insomnia followed by cognitive decline.
BSE in Cattle: Transmitted through contaminated feed; major outbreaks recorded in Britain.
Prevention and Management
Prevention measures include regulations against importing cattle from BSE-affected regions, and stringent sterilization of medical instruments.
Current understanding of prion diseases focuses on managing symptoms, as no cures exist.
Conclusion
Prion diseases remain a significant area of medical research due to their unique properties, transmission mechanisms, and fatal outcomes.