Cell-free formation of misfolded prion protein with authentic prion infectivity.
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ABSTRACT:
SUBMITTER: Weber P
PROVIDER: S-EPMC1635086 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
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Cell-free formation of misfolded prion protein with authentic prion infectivity.
Weber Petra P Giese Armin A Piening Niklas N Mitteregger Gerda G Thomzig Achim A Beekes Michael M Kretzschmar Hans A HA
Proceedings of the National Academy of Sciences of the United States of America 20061009 43
Prion propagation has been modeled in vitro; however, the low infectious titer of PrP(Sc) 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 PrP(Sc) and infectivity. Misfolded prion protein generated by protein misfolding cyclic amplification is as infectious as authentic brain-derived PrP(Sc) provided that confounding effects related to differences in the size distri ...[more]
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