EVERYDAY SCIENCE

Detailed explanation-1: -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-2: -The misfolding and aggregation of the human prion protein (PrP) is associated with transmissible spongiform encephalopathies (TSEs). Intermediate conformations forming during the conversion of the cellular form of PrP into its pathological scrapie conformation are key drivers of the misfolding process.

Detailed explanation-3: -Misfolded proteins (also called toxic conformations) are typically insoluble, and they tend to form long linear or fibrillar aggregates known as amyloid deposits.

Detailed explanation-4: -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-5: -Prions arise when normal proteins acquire an alternative conformation that becomes self-propagating. The most well-studied mammalian prions are composed of PrPSc proteins that cause Creutzfeldt-Jakob disease (CJD) in humans, scrapie in sheep, chronic wasting disease (CWD) in deer and elk, and mad cow disease.