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Pathogenic type of misfolded protein / From Wikipedia, the free encyclopedia

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A prion /ˈprɒn/ (Loudspeaker.svglisten) is a misfolded protein that can transmit its misfolded shape onto normal variants of the same protein. Prions are the causative agent of prion diseases known as transmissible spongiform encephalopathies (TSEs) that are transmissible, fatal neurodegenerative diseases in humans and other animals.[3][4] The proteins may misfold sporadically, due to genetic mutations, or by exposure to an already misfolded protein.[5] The consequent abnormal three-dimensional structure confers them the ability to cause misfolding of other proteins.

Quick facts: Prion diseases, Pronunciation, Specialty...
Prion diseases
Micrograph showing spongiform degeneration (vacuoles that appear as holes in tissue sections) in the cerebral cortex of a patient who had died of a prion disease (Creutzfeldt-Jakob disease). H&E stain. Scale bar = 30 microns (0.03 mm).
SpecialtyInfectious disease

The word prion is derived from the term "proteinaceous infectious particle".[6][7] The hypothesized role of a protein as an infectious agent stands in contrast to all other known infectious agents such as viroids, viruses, bacteria, fungi, and parasites, all of which contain nucleic acids (DNA, RNA, or both).

Prion isoforms of the major prion protein (PrP), whose specific function is uncertain, are hypothesized as the cause of transmissible spongiform encephalopathies (TSEs).[8] These include scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle (commonly known as "mad cow disease") and Creutzfeldt–Jakob disease (CJD) in humans.

All known prion diseases in mammals affect the structure of the brain or other neural tissue; all are progressive, have no known effective treatment, and are always fatal.[9] All known mammalian prion diseases were caused by the prion protein (PrP) until 2015, when a prion form of alpha-synuclein was hypothesized to cause multiple system atrophy (MSA).[10]

Prions are a type of intrinsically disordered protein, which change their conformation unless they are bound to a specific partner such as another protein. With a prion, two protein chains are stabilized if one binds to another in the same conformation. The probability of this happening is low, but once it does, the combination of the two is very stable. Then more units can get added, making a sort of "fibril".[11] Prions form abnormal aggregates of proteins called amyloids, which accumulate in infected tissue and are associated with tissue damage and cell death.[12] Amyloids are also responsible for several other neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.[13][14]

A prion disease is a type of proteopathy, or disease of structurally abnormal proteins. In humans, prions are believed to be the cause of Creutzfeldt–Jakob disease (CJD), its variant (vCJD), Gerstmann–Sträussler–Scheinker syndrome (GSS), fatal familial insomnia (FFI), and kuru.[15] There is also evidence suggesting prions may play a part in the process of Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS); these have been termed prion-like diseases.[16][17][18][19] Several yeast proteins have also been identified as having prionogenic properties,[20][21] as well as a protein involved in modification of synapses during the formation of memories[22][11] (see Eric Kandel § Molecular changes during learning). Prion replication is subject to epimutation and natural selection just as for other forms of replication, and their structure varies slightly between species.[23]

Prion aggregates are stable, and this structural stability means that prions are resistant to denaturation by chemical and physical agents: they cannot be destroyed by ordinary disinfection or cooking. This makes disposal and containment of these particles difficult, and the risk of iatrogenic spread through medical instruments a growing concern.