TY  - JOUR
AU  - Panza, G.
AU  - Luers, L.
AU  - Stöhr, J.
AU  - Nagel-Steger, L.
AU  - Weiß, J.
AU  - Riesner, D.
AU  - Willbold, D.
AU  - Birkmann, E.
TI  - Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro
JO  - PLoS one
VL  - 5
SN  - 1932-6203
CY  - Lawrence, Kan.
PB  - PLoS
M1  - PreJuSER-14241
SP  - e14283
PY  - 2010
N1  - 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.
AB  - 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.
KW  - Amyloid: chemistry
KW  - Animals
KW  - Brain: metabolism
KW  - Cattle
KW  - Circular Dichroism
KW  - Cricetinae
KW  - Kinetics
KW  - Mesocricetus
KW  - Mice
KW  - Neurodegenerative Diseases: metabolism
KW  - Prion Diseases: genetics
KW  - Prion Diseases: metabolism
KW  - Prion Diseases: transmission
KW  - Prions: chemistry
KW  - Protein Structure, Secondary
KW  - Recombinant Proteins: chemistry
KW  - Sheep
KW  - Sodium Dodecyl Sulfate: chemistry
KW  - Species Specificity
KW  - Ultracentrifugation
KW  - Amyloid (NLM Chemicals)
KW  - Prions (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - Sodium Dodecyl Sulfate (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:21151607
C2  - pmc:PMC3000319
UR  - <Go to ISI:>//WOS:000285135800013
DO  - DOI:10.1371/journal.pone.0014283
UR  - https://juser.fz-juelich.de/record/14241
ER  -