Role of the PrP gene in transmissible spongiform encephalopathies.

Details

Serval ID
serval:BIB_9D7840E1077E
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Title
Role of the PrP gene in transmissible spongiform encephalopathies.
Journal
Intervirology
Author(s)
Weissmann C., Büeler H., Fischer M., Aguet M.
ISSN
0300-5526 (Print)
ISSN-L
0300-5526
Publication state
Published
Issued date
1993
Volume
35
Number
1-4
Pages
164-175
Language
english
Abstract
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.
Keywords
Animals, Base Sequence, DNA, Molecular Sequence Data, Prion Diseases/etiology, Prions/genetics
Pubmed
Web of science
Create date
28/01/2008 11:36
Last modification date
20/08/2019 15:03
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