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{{Short description|Pathogenic type of misfolded protein}} {{About||the bird|Prion (bird)|the theoretical subatomic particle|Preon}} {{Distinguish|Major prion protein}} {{Good article}} {{use mdy dates|date=September 2022}}<!--Looks like the preference to me.--> {{cs1 config|name-list-style=vanc|display-authors=6}} {{Infobox medical condition | name = Prion | image = PDB 6DU9.png | caption = 3D structure of [[major prion protein]] | specialty = [[Infectious diseases (medical specialty)|Infectious diseases]] | pronounce = {{IPAc-en|audio=Pronunciation prion.ogg|ˈ|p|r|iː|ɒ|n}}, {{IPAc-en|ˈ|p|r|aɪ|ɒ|n}}<ref>{{cite web |title=English pronunciation of prion |url=https://dictionary.cambridge.org/pronunciation/english/prion |website=Cambridge Dictionary |publisher=Cambridge University Press |access-date=30 March 2020 |archive-url=https://web.archive.org/web/20170424075831/http://dictionary.cambridge.org/pronunciation/english/prion |archive-date=24 April 2017 |url-status=live}}</ref><ref>{{cite web |title=Definition of Prion |year=2021 |website=[[Dictionary.com]] |publisher=Random House, Inc. |at=Definition 2 of 2 |url=https://www.dictionary.com/browse/prion#luna-section |access-date=2021-09-12 |url-status=live |archive-date=2021-09-12 |archive-url=https://web.archive.org/web/20210912092658/https://www.dictionary.com/browse/prion#luna-section}}</ref> }} A '''prion''' ({{IPAc-en|audio=Pronunciation prion.ogg|ˈ|p|r|iː|ɒ|n}}) is a [[Proteinopathy|misfolded protein]] that induces misfolding in normal variants of the same protein, leading to [[cellular death]]. Prions are responsible for prion diseases, known as [[transmissible spongiform encephalopathy]] (TSEs), which are fatal and transmissible [[neurodegenerative disease]]s affecting both humans and animals.<ref name="NINDS">{{cite web |title=Transmissible Spongiform Encephalopathies |url=https://www.ninds.nih.gov/health-information/disorders/transmissible-spongiform-encephalopathies |website=National Institute of Neurological Disorders and Stroke |access-date=23 April 2023 |language=en}}</ref><ref>{{cite web |url=https://www.niaid.nih.gov/diseases-conditions/prion-diseases |title=Prion diseases |series=Diseases and conditions |publisher=National Institute of Health |access-date=2018-06-20 |archive-date=2020-05-22 |archive-url=https://web.archive.org/web/20200522095052/https://www.niaid.nih.gov/diseases-conditions/prion-diseases |url-status=live }}</ref> These proteins can misfold sporadically, due to genetic mutations, or by exposure to an already misfolded protein, leading to an abnormal [[Protein tertiary structure|three-dimensional structure]] that can propagate misfolding in other proteins.<ref>{{Cite book | vauthors = Kumar V |title=Robbins & Cotran Pathologic Basis of Disease |year=2021 |edition=10th}}</ref> The term ''prion'' comes from "proteinaceous infectious particle".<ref>{{cite magazine |url=https://www.scientificamerican.com/article/what-is-a-prion-specifica/ |title=What Is a Prion? |magazine=Scientific American |access-date=15 May 2018 |archive-date=16 May 2018 |archive-url=https://web.archive.org/web/20180516174822/https://www.scientificamerican.com/article/what-is-a-prion-specifica/ |url-status=live }}</ref><ref>{{cite encyclopedia |url=https://www.britannica.com/science/prion-infectious-agent |article=Prion infectious agent |title=Encyclopaedia Britannica |access-date=15 May 2018 |archive-date=16 May 2018 |archive-url=https://web.archive.org/web/20180516183206/https://www.britannica.com/science/prion-infectious-agent |url-status=live }}</ref> Unlike other infectious agents such as viruses, bacteria, and fungi, prions do not contain [[nucleic acid]]s ([[DNA]] or [[RNA]]). Prions are mainly twisted [[Protein isoform|isoforms]] of the [[major prion protein]] (PrP), a naturally occurring protein with an uncertain function. They are the hypothesized cause of various [[transmissible spongiform encephalopathy|TSEs]], including [[scrapie]] in sheep, [[chronic wasting disease]] (CWD) in deer, [[bovine spongiform encephalopathy]] (BSE) in cattle (mad cow disease), and [[Creutzfeldt–Jakob disease]] (CJD) in humans.<ref>{{cite journal | vauthors = Prusiner SB | title = Molecular biology of prion diseases | journal = Science | volume = 252 | issue = 5012 | pages = 1515–22 | date = June 1991 | pmid = 1675487 | doi = 10.1126/science.1675487 | bibcode = 1991Sci...252.1515P | s2cid = 22417182 }}</ref> All known prion diseases in [[mammal]]s affect the structure of the [[brain]] or other [[neuron|neural]] tissues. These diseases are progressive, have no known effective treatment, and are invariably fatal.<ref name=":0">{{cite journal | vauthors = Prusiner SB | title = Prions | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 23 | pages = 13363–83 | date = November 1998 | pmid = 9811807 | pmc = 33918 | doi = 10.1073/pnas.95.23.13363 | doi-access = free | bibcode = 1998PNAS...9513363P }}</ref> Most prion diseases were thought to be caused by PrP until 2015 when a prion form of [[alpha-synuclein]] was linked to [[multiple system atrophy]] (MSA).<ref name="pmid26324905" /> Misfolded proteins are also linked to other neurodegenerative diseases like [[Alzheimer's disease]], [[Parkinson's disease]], and [[amyotrophic lateral sclerosis]] (ALS), which are sometimes referred to as ''prion-like diseases''.<ref name="pmid19242475">{{cite journal | vauthors = Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM | title = Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers | journal = Nature | volume = 457 | issue = 7233 | pages = 1128–32 | date = February 2009 | pmid = 19242475 | pmc = 2748841 | doi = 10.1038/nature07761 | bibcode = 2009Natur.457.1128L }}</ref><ref name="Olanow">{{cite journal | vauthors = Olanow CW, Brundin P | title = Parkinson's disease and alpha synuclein: is Parkinson's disease a prion-like disorder? | journal = Movement Disorders | volume = 28 | issue = 1 | pages = 31–40 | date = January 2013 | pmid = 23390095 | doi = 10.1002/mds.25373 | s2cid = 38287298 }}</ref> Prions are a type of [[intrinsically disordered protein]] that continuously changes conformation unless bound to a specific partner, such as another protein. Once a prion binds to another in the same conformation, it stabilizes and can form a [[fibril]], leading to abnormal protein aggregates called [[amyloids]]. These amyloids accumulate in infected tissue, causing damage and cell death.<ref>{{cite journal | vauthors = Dobson CM | title = The structural basis of protein folding and its links with human disease | journal = Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences | volume = 356 | issue = 1406 | pages = 133–145 | date = February 2001 | pmid = 11260793 | pmc = 1088418 | doi = 10.1098/rstb.2000.0758 }}</ref> The structural stability of prions makes them resistant to [[denaturation (biochemistry)|denaturation]] by chemical or physical agents, complicating disposal and containment, and raising concerns about [[Iatrogenesis|iatrogenic spread]] through medical instruments.
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