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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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.
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|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology|
|Dewey Decimal Classification:||570 Life sciences; biology
610 Medicine & health
|Deposited On:||23 Jul 2012 12:38|
|Last Modified:||05 Apr 2016 15:48|
|Publisher:||Nature Publishing Group|
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