In humans, prions are believed to be the cause of CreutzfeldtвЂ“Jakob disease (CJD), its variant (vCJD), GerstmannвЂ“StrГ¤usslerвЂ“Scheinker syndrome (GSS), fatal familial insomnia (FFI), and kuru. This makes disposal and containment of these particles difficult.ДЄ prion disease is a type of proteopathy, or disease of structurally abnormal proteins. 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. Amyloids are also responsible for several other neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. Prions form abnormal aggregates of proteins called amyloids, which accumulate in infected tissue and are associated with tissue damage and cell death. Until 2015, all known mammalian prion diseases were considered to be caused by the prion protein (PrP) however in 2015 multiple system atrophy (MSA) was hypothesized to be caused by a prion form of alpha-synuclein.

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. Prion isoforms of the prion protein (PrP), whose specific function is uncertain, are hypothesized as the cause of transmissible spongiform encephalopathies (TSEs), including scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle (commonly known as 'mad cow disease') and CreutzfeldtвЂ“Jakob disease (CJD) in humans. 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). The word prion derives from 'proteinaceous infectious particle'. It is not known what causes the normal protein to misfold, but the abnormal three-dimensional structure is suspected of conferring infectious properties, collapsing nearby protein molecules into the same shape. They characterize several fatal and transmissible neurodegenerative diseases in humans and many other animals. Prions are misfolded proteins with the ability to transmit their misfolded shape onto normal variants of the same protein. / Л€ p r iЛђ Й’ n/ ( listen), / Л€ p r aЙЄ Й’ n/.

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