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Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro

Nathan R Deleault1, Richard Kascsak, James C Geoghegan

  • 1Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA.

Biochemistry
|April 10, 2010
PubMed

Insights

Researchers explored prion protein (PrPSc) propagation in vitro, finding species-specific cofactor needs. RNA aids hamster PrPSc, but not mouse or vole PrPSc, suggesting a non-nucleic acid cofactor in brain tissue.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Prion diseases are linked to misfolded prion protein (PrPSc).
  • In vitro propagation methods like sPMCA are crucial for studying PrPSc.
  • Cofactor requirements for PrPSc propagation can vary by species.

Purpose of the Study:

  • To investigate the cofactor preferences for in vitro propagation of PrPSc from different rodent species.
  • To determine if nucleic acids are essential cofactors for PrPSc propagation across species.

Main Methods:

  • Serial protein misfolding cyclic amplification (sPMCA) technique was employed.
  • PrPSc propagation was tested with and without RNA and other polyanions.
  • Brain homogenates from PrP knockout mice were pretreated with nucleases.

Main Results:

  • RNA facilitated hamster PrPSc propagation but not mouse or vole PrPSc.
  • Nuclease pretreatment inhibited hamster PrPSc propagation but not mouse PrPSc.
  • Mouse PrPSc propagation was reconstituted using brain or liver homogenates, indicating a non-nucleic acid cofactor.

Conclusions:

  • Cofactor utilization for PrPSc propagation is species-specific.
  • An endogenous, non-nucleic acid cofactor in brain tissue promotes PrPSc propagation.

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