NEET BIOLOGY

Detailed explanation-1: -The misfolding and aggregation of the human prion protein (PrP) is associated with a number of fatal neurodegenerative disorders designated as transmissible spongiform encephalopathies (TSEs), including Kuru, Creutzfeldt–Jakob disease, fatal familial insomnia, and mad cow disease (1).

Detailed explanation-2: -Transmissible spongiform encephalopathies (TSEs or prion diseases) are a rare group of invariably fatal neurodegenerative disorders that affect humans and other mammals. TSEs are protein misfolding diseases that involve the accumulation of an abnormally aggregated form of the normal host prion protein (PrP).

Detailed explanation-3: -Protein misfolding is a common cellular event that can occur throughout the lifetime of a cell, caused by different events including genetic mutations, translational errors, abnormal protein modifications, thermal or oxidative stress, and incomplete complex formations.

Detailed explanation-4: -A prion is a type of protein that can trigger normal proteins in the brain to fold abnormally. Prion diseases can affect both humans and animals and are sometimes spread to humans by infected meat products. The most common form of prion disease that affects humans is Creutzfeldt-Jakob disease (CJD).

Detailed explanation-5: -Misfolded proteins (also called toxic conformations) are typically insoluble, and they tend to form long linear or fibrillar aggregates known as amyloid deposits.