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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-62286

Sigurdson, Christina J; Nilsson, K Peter R; Hornemann, Simone; Manco, Giuseppe; Polymenidou, Magdalini; Schwarz, Petra; Leclerc, Mario; Hammarström, Per; Wüthrich, Kurt; Aguzzi, Adriano (2007). Prion strain discrimination using luminescent conjugated polymers. Nature Methods, 4(12):1023-1030.

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Abstract

The occurrence of multiple strains of prions may reflect conformational variability of PrP(Sc), a disease-associated, aggregated variant of the cellular prion protein, PrP(C). Here we used luminescent conjugated polymers (LCPs), which emit conformation-dependent fluorescence spectra, for characterizing prion strains. LCP reactivity and emission spectra of brain sections discriminated among four immunohistochemically indistinguishable, serially mouse-passaged prion strains derived from sheep scrapie, chronic wasting disease (CWD), bovine spongiform encephalopathy (BSE), and mouse-adapted Rocky Mountain Laboratory scrapie prions. Furthermore, using LCPs we differentiated between field isolates of BSE and bovine amyloidotic spongiform encephalopathy, and identified noncongophilic deposits in prion-infected deer and sheep. We found that fibrils with distinct morphologies generated from chemically identical recombinant PrP yielded unique LCP spectra, suggesting that spectral characteristic differences resulted from distinct supramolecular PrP structures. LCPs may help to detect structural differences among discrete protein aggregates and to link protein conformational features with disease phenotypes.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2007
Deposited On:23 Jul 2012 14:38
Last Modified:04 Dec 2013 15:32
Publisher:Nature Publishing Group
ISSN:1548-7091
Publisher DOI:10.1038/nmeth1131
PubMed ID:18026110
Citations:Web of Science®. Times Cited: 131
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