Prion-induced disorders, also known as prion diseases or transmissible spongiform encephalopathies (TSEs), are a group of rare neurodegenerative conditions that affect both humans and animals. These disorders are characterized by the accumulation and misfolding of abnormally-shaped proteins called prions within the brain tissue.
Prions, unlike other infectious agents, lack genetic material such as DNA or RNA. Instead, they consist solely of a misfolded protein form, which is highly stable and resistant to standard methods of decontamination. When a normal protein comes into contact with a prion, it can become misfolded and trigger a chain reaction, leading to the accumulation of malformed proteins throughout the central nervous system.
Prion-induced disorders are typically fatal and can manifest with a multitude of clinical signs, depending on the specific disease. Some examples of prion diseases include Creutzfeldt-Jakob disease (CJD) in humans, bovine spongiform encephalopathy (BSE or "mad cow disease") in cattle, and scrapie in sheep.
Symptoms of prion-induced disorders may include rapid cognitive decline, memory loss, behavioral changes, movement abnormalities, and psychiatric symptoms. As the disease progresses, affected individuals may experience muscle stiffness, difficulty speaking, and eventually develop severe dementia.
The transmission of prion diseases can occur through various routes, including ingestion of prion-contaminated tissue, inheritance of genetic mutations, or exposure to prion-contaminated medical equipment. Due to their transmissible nature and potential for zoonotic transmission, prion-induced disorders pose significant public health concerns.
Currently, there is no cure or effective treatment for prion diseases. Management typically involves supportive care to alleviate symptoms and enhance quality of life. Strict infection
