NR AVOF

AU Weber,P.; Giese,A.; Piening,N.; Mitteregger,G.; Thomzig,A.; Beekes,M.; Kretzschmar,H.A.

TI Cell-free formation of misfolded prion protein with authentic prion infectivity

QU Proceedings of the National Academy of Sciences of the United States of America 2006 Oct 24; 103(43): 15818-23

PT journal article; research support, non-u.s. gov't

AB Prion propagation has been modeled in vitro; however, the low infectious titer of PrPsc thus generated has cast doubt on the "protein-only" hypothesis. Here we show that prion delivery on suitable nitrocellulose carrier particles abrogates the apparent dissociation of PrPsc and infectivity. Misfolded prion protein generated by protein misfolding cyclic amplification is as infectious as authentic brain-derived PrPsc provided that confounding effects related to differences in the size distribution of prion protein aggregates generated in vitro and consecutive differences in regard to biological clearance are abolished.

MH Animals; Biological Assay; Brain/metabolism; Cell Line; Cell-Free System; Collodion; Cricetinae; Mice; Mice, Inbred C57BL; Prion Diseases/*metabolism; Prions/*metabolism/*pathogenicity; *Protein Folding; Survival Rate

AD Center for Neuropathology and Prion Research, Ludwig Maximilians University of Munich, Feodor-Lynen-Strasse 23, 81377 Munich, Germany.

SP englisch

PO USA

EA pdf-Datei und supporting information

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