Role of the PrP gene in transmissible spongiform encephalopathies.

Détails

ID Serval
serval:BIB_9D7840E1077E
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Titre
Role of the PrP gene in transmissible spongiform encephalopathies.
Périodique
Intervirology
Auteur⸱e⸱s
Weissmann C., Büeler H., Fischer M., Aguet M.
ISSN
0300-5526 (Print)
ISSN-L
0300-5526
Statut éditorial
Publié
Date de publication
1993
Volume
35
Numéro
1-4
Pages
164-175
Langue
anglais
Résumé
The transmissible agent that causes spongiform encephalopathies such as scrapie, the prion, is believed to be devoid of nucleic acid and identical with PrPSc, a modified form of PrPC. PrPC is a normal host protein encoded by a single copy gene (Prn-p) and is found predominantly on the surface of neurons. PrPSc, in contrast to PrPC, is resistant to protease and accumulates intracellularly. Prusiner proposed that PrPSc, when introduced into a normal host, causes the conversion of PrPC or its precursor into PrPSc ('protein only' hypothesis). If indeed PrP is an essential component of the prion, then an animal devoid of the PrP protein should be resistant to scrapie. We generated homozygous PrP 'knockout' mice. These Prn-p0/0 mice showed no gross abnormalities, and microscopic examination of brain sections of normal and Prn-p0/0 mice revealed no differences. Prn-p0/0, Prn-p+/+ and Prn-p0/+ mice were inoculated with scrapie agent; the clinical response as well as the prion titer at different time points are being determined.
Mots-clé
Animals, Base Sequence, DNA, Molecular Sequence Data, Prion Diseases/etiology, Prions/genetics
Pubmed
Web of science
Création de la notice
28/01/2008 11:36
Dernière modification de la notice
20/08/2019 15:03
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