Prion protein diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of rare and fatal neurodegenerative disorders characterized by the abnormal accumulation and aggregation of a misfolded protein in the brain. These diseases affect both humans and animals, and they include conditions such as Creutzfeldt-Jakob disease, variant Creutzfeldt-Jakob disease, kuru, fatal familial insomnia, Gerstmann-Sträussler-Scheinker syndrome, and bovine spongiform encephalopathy (BSE or "mad cow" disease).
Prion protein diseases are unique as they can occur sporadically, be inherited through genetic mutations, or acquired through exposure to infected tissues. The misfolded prion protein is believed to have the ability to convert normal, healthy prion proteins into its abnormal conformation, leading to their accumulation and subsequent damage to brain tissue. This, in turn, causes characteristic symptoms including dementia, neurological deficits, behavioral changes, and eventually death.
The term "transmissible spongiform encephalopathies" refers to the observation that affected brains exhibit a sponge-like appearance under microscopy due to the formation of microscopic holes in the tissue. Currently, there is no known cure for prion protein diseases, and treatment mainly focuses on managing symptoms and providing comfort to affected individuals.
Prion protein diseases have garnered significant attention due to their potential for zoonotic transmission, as seen in the case of BSE where it can be transmitted from infected animals to humans. This has led to elaborate surveillance measures, strict regulations, and precautions in the handling, processing, and consumption of animal products to reduce the risk of transmission.
