NR AOQK
AU Bieschke,J.G.; Weber,P.; Sarafoff,N.; Beekes,M.; Giese,A.; Kretzschmar,H.A.
TI Loss of infectivity in autocatalytic self-propagation of misfolded prion protein
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - BR-48
PT Konferenz-Poster
AB Prions are thought to replicate in an autocatalytic process that converts cellular prion protein PrPc to the misfolded PrPsc isoform. Our study scrutinizes this hypothesis by in vitro protein misfolding cyclic amplification (PMCA). In serial transmission PMCA experiments, newly formed misfolded and proteinase K-resistant PrP (PrPres) catalysed the structural conversion of PrPc as efficiently as PrPsc seeds, which confirms an autocatalytic PrP misfolding cascade as postulated by the prion hypothesis. However, the autocatalytic formation of PrPres was not paralleled by replication of biological infectivity. Thus, propagation of transmissible prions appears to require factors additional to autocatalytic PrP misfolding.
AD Jan G. Bieschke, Petra Weber, Nikolaus Sarafoff, Armin Giese, Hans A. Kretzschmar, Institute for Neuropathology, Ludwig-Maximilians-University Munich, Germany; Michael Beekes, Robert-Koch-Institute, Berlin, Germany
SP englisch
PO Deutschland