Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1867
Fischer, M B; Rülicke, T; Raeber, A; Sailer, A; Moser, M; Oesch, B; Brandner, S; Aguzzi, A; Weissmann, C (1996). Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. The EMBO Journal, 15(6):1255-1264.
The 'protein only' hypothesis postulates that the prion, the agent causing transmissible spongiform encephalopathies, is PrP(Sc), an isoform of the host protein PrP(C). Protease treatment of prion preparations cleaves off approximately 60 N-terminal residues of PrP(Sc) but does not abrogate infectivity. Disruption of the PrP gene in the mouse abolishes susceptibility to scrapie and prion replication. We have introduced into PrP knockout mice transgenes encoding wild-type PrP or PrP lacking 26 or 49 amino-proximal amino acids which are protease susceptible in PrP(Sc). Inoculation with prions led to fatal disease, prion propagation and accumulation of PrP(Sc) in mice expressing both wild-type and truncated PrPs. Within the framework of the 'protein only' hypothesis, this means that the amino-proximal segment of PrP(C) is not required either for its susceptibility to conversion into the pathogenic, infectious form of PrP or for the generation of PrP(Sc).
|Item Type:||Journal Article, refereed|
|Communities & Collections:||04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology|
|DDC:||570 Life sciences; biology|
610 Medicine & health
|Date:||15 March 1996|
|Deposited On:||11 Feb 2008 13:26|
|Last Modified:||06 Dec 2013 09:43|
|Publisher:||European Molecular Biology Organization ; Nature Publishing Group|
|Citations:||Web of Science®. Times Cited: 585|
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