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
Article
31 sectionsContents
- Etymology and pronunciation
- Prion protein
- Structure
- PrP<sup>C</sup>
- PrP<sup>Sc</sup>
- PrP<sup>res</sup>
- 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.