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There are 6 letters in PTIONS ( I1N1O1P3S1T1 )
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Prions are misfolded proteins which characterize several fatal neurodegenerative diseases in animals and humans. It is not known what causes the normal prion protein to misfold; the abnormal 3-D structure is suspected to confer infectious properties. The word prion derives from ‘proteinaceous infectious particle’. Prions composed of the prion protein (PrP) are hypothesized as the cause of transmissible spongiform encephalopathies (TSEs), including scrapie in sheep and bovine spongiform encephalopathy (BSE) in cattle—known popularly as "mad cow disease". * In humans, prions have been hypothesized as the cause of Creutzfeldt–Jakob disease (CJD) and its variant (vCJD), Gerstmann–Sträussler–Scheinker syndrome, “fatal familial insomnia”, and kuru. 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. Multiple system atrophy (MSA), a rare human neurodegenerative disease, features a misfolded version of a protein called alpha-synuclein, and is therefore also classifiable as a prion disease. Several yeast proteins have also been identified as having prionogenic properties.The hypothesized role of a protein as an infectious agent stands in contrast to all other known infectious agents such as viruses, bacteria, fungi, and parasites, all of which contain nucleic acids (DNA, RNA, or both). Synthetic prions, created in the laboratory independent of any biological source, have little or no ability to cause infection with TSEs. However, when synthetic prions are administered in combination with cofactors, such as phosphatidylethanolamine and RNA molecules, then this can transmit TSEs.Several scientific observations remain unexplained by the prion hypothesis: It is known that mice with severe combined immunodeficiency do not develop scrapie following inoculation with brain tissue from animals infected with scrapie, suggesting that either the role of immunity in prion pathogenesis is incompletely understood or that there is some other flaw in current understanding of prion pathophysiology. More recently, it has been shown that scrapie and Creutzfeld-Jacob Disease * may require agent specific nucleic acids for transmission of infection. For these reasons, the prion / TSE hypothesis incompletely accounts for the observed data.Prion aggregates are stable, accumulate in infected tissue, and are associated with 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 epimutation and natural selection just like other forms of replication. |