A particle of protein that is thought to be able to self-replicate and to be the agent of infection in a variety of diseases of the nervous system, such as mad cow disease. Prion replication (in which strings of amino acids are reproduced) stands as an exception to a central tenet of biology stating that only nucleic acids, such as DNA, can self-replicate. The mechanism of prion replication is not clearly understood.
A Closer Look In 1997 Stanley Prusiner was awarded the Nobel Prize for physiology or medicine for his theory that a deviant form of a harmless protein could be an infectious agent, a transmitter of disease. Named prions (short for proteinaceous infectious particle),
these misshapen proteins cause healthy proteins to misfold, fatally clumping together in the brain. Unlike other disease-causing agents, prions lack genetic material (DNA and RNA). Neurodegenerative prion diseases are often called spongiform encephalopathies because they leave the brain riddled with holes like a sponge. In animals, prion diseases include scrapie in sheep and bovine spongiform encephalopathy, commonly known as mad cow disease in cattle. In humans, diseases such as kuru and Creutzfeldt-Jakob disease (CJD) are also thought to be caused by prions. All the diseases are characterized by loss of motor control, dementia, paralysis, and eventual death due to massive destruction of brain tissue. Humans are thought to contract prion disease most commonly by eating prion-contaminated flesh. Kuru, a rare and fatal brain disorder, brought prion disease to the forefront. First described in the 1950s, kuru was most common among the Fore people of Papua New Guinea, who had a custom of eating the brains of their dead during funeral feasts. It is speculated that a tribe member developed CJD, his or her contaminated brain tissue was ingested, and the disease spread. Kuru reached epidemic levels in the 1960s, but the disease declined after the government discouraged the practice of cannibalism and now it has almost completely disappeared.