Keywords
Infectious agent, protein aggregation, protein conformation multiplicity, protein-encoded infectivity, protein-encoded inheritance, strains
Definition
Prions are protein-based elements of infection and inheritance. Prions are made by alternate protein conformations that by acting as templates propagate their conformations to the precursor proteins. In general, this propagative state is an insoluble polymer, rich in tightly packed β-sheets and displaying amyloid staining features. This state is not structurally unique but polymorphic allowing strains. The protein undergoing prion conversion loses its normal function and acquires the ability to transform the precursor into its like. This protein conformational code provides physiological switches for fast environmental adaptation and underlies the spread of the mammalian neurodegenerative diseases known as transmissible spongiform encephalopathies.
History
The unique inactivation pattern displayed by the infectious agent causing...
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References and Further Reading
Aguzzi A, Calella AM (2009) Prions: protein aggregation and infectious diseases. Physiol Rev 89:1105–1152
Aguzzi A, Rajendran L (2009) The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64:783–790
Alper T, Cramp WA, Haig DA, Clarke MC (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214:764–766
Colby DW, Wain R, Baskakov IV, Legname G, Palmer CG, Nguyen HO, Lemus A, Cohen FE, DeArmond SJ, Prusiner SB (2010) Protease-sensitive synthetic prions. PLoS Pathog 6:e1000736
Deleault NR, Harris BT, Rees JR, Supattapone S (2007) Formation of native prions from minimal components in vitro. Proc Natl Acad Sci USA 104:9741–9746
Griffith JS (1967) Self-replication and scrapie. Nature 215:1043–1044
Halfmann R, Alberti S, Lindquist S (2010) Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol 20:125–133
Maddelein ML, Dos Reis S, Duvezin-Caubet S, Coulary-Salin B, Saupe SJ (2002) Amyloid aggregates of the HET-s prion protein are infectious. Proc Natl Acad Sci USA 99:7402–7407
Makarava N, Kovacs GG, Bocharova O, Savtchenko R, Alexeeva I, Budka H, Rohwer RG, Baskakov IV (2010) Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 119:177–187
Prusiner SB (1982) Novel proteinaceous infectious particle causing scrapie. Science 216:136–144
Prusiner SB (1998) Prions. Proc Natl Acad Sci USA 95:13363–13383
Wickner RB (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264:566–569
Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D (2009) Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol 16:973–978
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2011 Springer-Verlag Berlin Heidelberg
About this entry
Cite this entry
Gasset, M. (2011). Prion. In: Gargaud, M., et al. Encyclopedia of Astrobiology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-11274-4_1276
Download citation
DOI: https://doi.org/10.1007/978-3-642-11274-4_1276
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-11271-3
Online ISBN: 978-3-642-11274-4
eBook Packages: Physics and AstronomyReference Module Physical and Materials ScienceReference Module Chemistry, Materials and Physics