prion

Also known as prions, proteinaceous infectious particle, protineaceous infectious particles, PrpSc, Pr P, Human and Animal Prions, Proteinaceous and infection, fungal prion

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Key facts

Medical condition.name: Prion
Medical condition.image: PDB 6DU9.png
Medical condition.caption: 3D structure of major prion protein
Medical condition.specialty: Infectious diseases
Medical condition.pronounce: ,

via Wikipedia infobox

Research

24,833 papers

Anti-Prion Systems in Saccharomyces cerevisiae.ReviewJournal of neurochemistry · 2025Wickner RB, Hayashi Y, Edskes HKDOI: 10.1111/jnc.70045
[Prion].ReviewUirusu · 2002Sakaguchi S
Prion-like proteins: from computational approaches to proteome-wide analysis.ReviewFEBS open bio · 2021Gil-Garcia M, Iglesias V, Pallarès I et al.DOI: 10.1002/2211-5463.13213
Prion-prion interactions.ReviewPrion · 2007Derkatch IL, Liebman SWDOI: 10.4161/pri.1.3.4837
Prion diseases.ReviewJournal of neurovirology · 2003McKintosh E, Tabrizi SJ, Collinge JDOI: 10.1080/13550280390194082
Prion diseases.ReviewClinics in laboratory medicine · 2010Venneti SDOI: 10.1016/j.cll.2009.11.002
Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry.ReviewViruses · 2022Son M, Wickner RBDOI: 10.3390/v14091945
Prion stability.ReviewPrion · 2007Cox BS, Byrne LJ, Tuite MFDOI: 10.4161/pri.1.3.4839

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Wikidata facts

Image: Histology bse.jpg

Show 2 more facts

Commons category: Prions
time of discovery or invention: 1982-00-00

Sources (4)

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~40 min read

Article

31 sections

Contents

Etymology and pronunciation
Prion protein
Structure
PrPC
PrPSc
PrPres
Normal function of PrP
PrP and regulated cell death
PrP and long-term memory
PrP and stem cell renewal
PrP and innate immunity
Replication
Transmissible spongiform encephalopathies
Transmission
Genetic susceptibility
Prions in plants
Sterilization
Degradation resistance in nature
Degradation by living beings
Fungi
Treatments
In other diseases
Role in neurodegenerative disease
TDP-43
RNPA2B1, RNPA1
Aβ
Alpha-synuclein
History
See also
References
External links

A prion () is a misfolded protein that induces folding problems in normal variants of the same protein, leading to cellular death. Prions are responsible for prion diseases, which are fatal and transmissible neurodegenerative diseases affecting animals including humans. These proteins can misfold sporadically, due to genetic mutations, or by exposure to an already misfolded protein, leading to an abnormal three-dimensional structure that can propagate misfolding in other proteins.

The term prion comes from "proteinaceous infectious particle". Unlike other infectious agents such as viruses, bacteria, and fungi, prions do not contain nucleic acids (DNA or RNA). Prions are mainly twisted isoforms of the major prion protein (PrP), a naturally occurring protein with an uncertain function. They are the hypothesized cause of various diseases, 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.