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Meier, Philipp; Genoud, Nicolas; Prinz, M; Maissen, M; Rülicke, T; Zurbriggen, A; Raeber, A J; Aguzzi, A (2003). Soluble dimeric prion protein binds PrP(Sc) in vivo and antagonizes prion disease. Cell, 113(1):49-60.

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Conversion of cellular prion protein (PrP(C)) into a pathological conformer (PrP(Sc)) is thought to be promoted by PrP(Sc) in a poorly understood process. Here, we report that in wild-type mice, the expression of PrP(C) rendered soluble and dimeric by fusion to immunoglobulin Fcgamma (PrP-Fc(2)) delays PrP(Sc) accumulation, agent replication, and onset of disease following inoculation with infective prions. In infected PrP-expressing brains, PrP-Fc(2) relocates to lipid rafts and associates with PrP(Sc) without acquiring protease resistance, indicating that PrP-Fc(2) resists conversion. Accordingly, mice expressing PrP-Fc(2) but lacking endogenous PrP(C) are resistant to scrapie, do not accumulate PrP-Fc(2)(Sc), and do not transmit disease to others. These results indicate that various PrP isoforms engage in a complex in vivo, whose distortion by PrP-Fc(2) affects prion propagation and scrapie pathogenesis. The unique properties of PrP-Fc(2) suggest that soluble PrP derivatives may represent a new class of prion replication antagonists.


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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Date:4 April 2003
Deposited On:11 Feb 2008 12:26
Last Modified:05 Apr 2016 12:20
Publisher DOI:10.1016/S0092-8674(03)00201-0
Related URLs:http://linkinghub.elsevier.com/retrieve/pii/S0092867403002010
PubMed ID:12679034

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