In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc).

@article{Bocharova2005InVC,
  title={In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc).},
  author={Olga V. Bocharova and Leonid Breydo and Alexander S Parfenov and Vadim V. Salnikov and Ilia V Baskakov},
  journal={Journal of molecular biology},
  year={2005},
  volume={346 2},
  pages={645-59}
}
The "protein only" hypothesis postulates that the infectious agent of prion diseases, PrP(Sc), is composed of the prion protein (PrP) converted into an amyloid-specific conformation. However, cell-free conversion of the full-length PrP into the amyloid conformation has not been achieved. In an effort to understand the mechanism of PrP(Sc) formation, we developed a cell-free conversion system using recombinant mouse full-length PrP with an intact disulfide bond (rPrP). We demonstrate that rPrP… CONTINUE READING
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