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A prion () is an infectious agent, composed entirely of protein, presumed to be the cause of the transmissible spongiform encephalopathies (TSEs). The protein it is composed of, called PrP (short for prion protein) can fold in multiple, structurally distinct ways, at least one of which is transmissible to other prion proteins. It is this form of replication that leads to disease that is similar to viral infection. The word ''prion'', coined in 1982 by Stanley B. Prusiner, is short for “proteinaceous infectious particle” derived from the words protein'' and ''infection, hence prion, in reference to a prion's ability to self-propagate and transmit its conformation to other prions.〔(【引用サイトリンク】title=Stanley B. Prusiner — Autobiography )〕 While several yeast proteins have been identified as having prionogenic properties, the first prion protein was discovered in mammals and is referred to as the major prion protein (PrP). This infectious agent causes mammalian transmissible spongiform encephalopathies, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") and scrapie in sheep. In humans, PrP causes Creutzfeldt-Jakob Disease (CJD), variant Creutzfeldt-Jakob Disease (vCJD), Gerstmann–Sträussler–Scheinker syndrome, Fatal Familial Insomnia and kuru.〔(【引用サイトリンク】 Prion Diseases )〕 A protein as an infectious agent stands in contrast to all other known infectious agents such as viruses, bacteria, fungi, or parasites, all of which must contain nucleic acids (either DNA, RNA, or both). For this reason, a minority of researchers still debate whether prions are the cause of the TSEs. All known prion diseases in mammals affect the structure of the brain or other neural tissue and all are currently untreatable and universally fatal. Prions are not considered living organisms because they are misfolded protein molecules which may propagate by transmitting a misfolded protein state. If a prion enters a healthy organism, it induces existing, properly folded proteins to convert into the misfolded prion form. In this way, the prion acts as a template to guide the misfolding of more proteins into prion form. In yeast, this refolding is assisted by chaperone proteins such as Hsp104p. These refolded prions can then go on to convert more proteins themselves, leading to a chain reaction resulting in large amounts of the prion form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. Amyloid aggregates are fibrils, growing at their ends, and replicate when breakage causes two growing ends to become four growing ends. The incubation period of prion diseases is determined by the exponential growth rate associated with prion replication, which is a balance between the linear growth and the breakage of aggregates. (Note that the propagation of the prion depends on the presence of normally folded protein in which the prion can induce misfolding; animals that do not express the normal form of the prion protein can neither develop nor transmit the disease.) Prion aggregates are extremely stable and accumulate in infected tissue, causing tissue damage and cell death. This structural stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult. Prion structure varies slightly between species, but nonetheless prion replication is subject to occasional epimutation and natural selection just like other forms of replication. == Prion Protein (PrP) == 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Prion」の詳細全文を読む スポンサード リンク
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