This title appears in the Scientific Report : 2010 

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. / Nagel-Steger, L. / Weiß, J. / Riesner, D. / Willbold, D. / Birkmann, E.
Strukturbiochemie; ISB-3
JARA - HPC; JARA-HPC
PLoS one, 5 (2010) S. e14283
Lawrence, Kan. PLoS 2010
e14283
21151607
10.1371/journal.pone.0014283
Journal Article
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
Funktion und Dysfunktion des Nervensystems
PLOS One 5
J
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OpenAccess
Please use the identifier: http://dx.doi.org/10.1371/journal.pone.0014283 in citations.
Please use the identifier: http://hdl.handle.net/2128/11182 in citations.
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.