Weber P, Giese A, Piening N, Mitteregger G, Thomzig A, Beekes M, Kretzschmar HA (2006): Cell-free formation of misfolded prion protein with authentic prion infectivity
Proc. Natl. Acad. Sci. U. S. A. 103 (43): 15818-15823. Epub 2006 Oct 9.

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 distribution of prion protein aggregates generated in vitro and consecutive differences in regard to biological clearance are abolished.