Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro

Panza, G.; Luers, L.; Stöhr, J.; Willbold, D.; Birkmann, E.; Riesner, D.; Nagel-Steger, L.; Weiß, J.

doi:10.1371/journal.pone.0014283

Journal Article

Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro

Panza, G. ; Luers, L.FZJ* ; Stöhr, J. ; Nagel-Steger, L. ; Weiß, J. ; Riesner, D. ; Willbold, D.FZJ* ; Birkmann, E.FZJ*

2010
PLoS Lawrence, Kan.

PLoS one 5, e14283 (2010) [10.1371/journal.pone.0014283]

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Please use a persistent id in citations: http://hdl.handle.net/2128/11182 doi:10.1371/journal.pone.0014283

Abstract: Prion diseases like Creutzfeldt-Jakob disease in humans, Scrapie in sheep or bovine spongiform encephalopathy are fatal neurodegenerative diseases, which can be of sporadic, genetic, or infectious origin. Prion diseases are transmissible between different species, however, with a variable species barrier. The key event of prion amplification is the conversion of the cellular isoform of the prion protein (PrP(C)) into the pathogenic isoform (PrP(Sc)). We developed a sodiumdodecylsulfate-based PrP conversion system that induces amyloid fibril formation from soluble α-helical structured recombinant PrP (recPrP). This approach was extended applying pre-purified PrP(Sc) as seeds which accelerate fibrillization of recPrP. In the present study we investigated the interspecies coherence of prion disease. Therefore we used PrP(Sc) from different species like Syrian hamster, cattle, mouse and sheep and seeded fibrillization of recPrP from the same or other species to mimic in vitro the natural species barrier. We could show that the in vitro system of seeded fibrillization is in accordance with what is known from the naturally occurring species barriers.

Keyword(s): Amyloid: chemistry (MeSH) ; Animals (MeSH) ; Brain: metabolism (MeSH) ; Cattle (MeSH) ; Circular Dichroism (MeSH) ; Cricetinae (MeSH) ; Kinetics (MeSH) ; Mesocricetus (MeSH) ; Mice (MeSH) ; Neurodegenerative Diseases: metabolism (MeSH) ; Prion Diseases: genetics (MeSH) ; Prion Diseases: metabolism (MeSH) ; Prion Diseases: transmission (MeSH) ; Prions: chemistry (MeSH) ; Protein Structure, Secondary (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Sheep (MeSH) ; Sodium Dodecyl Sulfate: chemistry (MeSH) ; Species Specificity (MeSH) ; Ultracentrifugation (MeSH) ; Amyloid ; Prions ; Recombinant Proteins ; Sodium Dodecyl Sulfate ; J

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Biology

Note: This authors were funded by the European Union: (Network of Excellence "NeuroPrion", FOOD-CT-2004-506579, http://www.neuroprion.org/en/index. html); "Presidentenfond der Helmholtzgemeinschaft" (HGF, "Virtual Institute of Structural Biology"), http://www.vibs-rhine-ruhr.org/; and Food Standards Agency UK (M03R0005/004) http://www.food.gov.uk/. Lars Luers was a fellow of the Graduiertenkolleg 1033. Jan Stohr was supported by a postdoctoral fellowship of the Deutsche Forschungsgemeinschaft (DFG). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

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Appears in the scientific report 2010

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