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Prion strain discrimination using luminescent conjugated polymers
Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.ORCID iD: 0000-0002-5582-140X
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2007 (English)In: Nature Methods, ISSN 1548-7091, E-ISSN 1548-7105, Vol. 4, no 12, 1023-1030 p.Article in journal (Refereed) Published
Abstract [en]

The occurrence of multiple strains of prions may reflect conformational variability of PrPSc, a disease-associated, aggregated variant of the cellular prion protein, PrPC. 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.

Place, publisher, year, edition, pages
2007. Vol. 4, no 12, 1023-1030 p.
National Category
Natural Sciences
URN: urn:nbn:se:liu:diva-41995DOI: 10.1038/nmeth1131Local ID: 59514OAI: diva2:262850
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2014-04-08

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Nilsson, PeterHammarström, Per
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