Prions
Identifieur interne : 002C35 ( Main/Exploration ); précédent : 002C34; suivant : 002C36Prions
Auteurs : I. S. Shkundina [Russie] ; M. D. Ter-Avanesyan [Russie]Source :
- Biochemistry (Moscow) [ 0006-2979 ] ; 2007-12-01.
English descriptors
- KwdEn :
Abstract
Abstract: Prions were originally defined as infectious agents of protein nature, which caused neurodegenerative diseases in animals and humans. The prion concept implies that the infectious agent is a protein in special conformation that can be transmitted to the normal molecules of the same protein through protein-protein interactions. Until the 1990s, the prion phenomenon was associated with the single protein named PrP. Discovery of prions in lower eukaryotes, the yeast Saccharomyces cerevisiae and fungus Podospora anserina, suggests that prions have wider significance. Prions of lower eukaryotes are not related to diseases; their propagation caused by aggregation of prion-like proteins underlies the inheritance of phenotypic traits and most likely has adaptive significance. This review covers prions of mammals and lower eukaryotes, mechanisms of their appearance de novo and maintenance, structure of prion particles, and prospects for the treatment of prion diseases. Recent data concerning the search for new prion-like proteins is included. The paper focuses on the [PSI +] prion of S. cerevisiae, since at present it is the most investigated one. The biological significance of prions is discussed.
Url:
DOI: 10.1134/S0006297907130081
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Abstract: Prions were originally defined as infectious agents of protein nature, which caused neurodegenerative diseases in animals and humans. The prion concept implies that the infectious agent is a protein in special conformation that can be transmitted to the normal molecules of the same protein through protein-protein interactions. Until the 1990s, the prion phenomenon was associated with the single protein named PrP. Discovery of prions in lower eukaryotes, the yeast Saccharomyces cerevisiae and fungus Podospora anserina, suggests that prions have wider significance. Prions of lower eukaryotes are not related to diseases; their propagation caused by aggregation of prion-like proteins underlies the inheritance of phenotypic traits and most likely has adaptive significance. This review covers prions of mammals and lower eukaryotes, mechanisms of their appearance de novo and maintenance, structure of prion particles, and prospects for the treatment of prion diseases. Recent data concerning the search for new prion-like proteins is included. The paper focuses on the [PSI +] prion of S. cerevisiae, since at present it is the most investigated one. The biological significance of prions is discussed.</div>
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