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Generating a prion with bacterially expressed recombinant prion protein.

Fei Wang1, Xinhe Wang, Chong-Gang Yuan

  • 1Department of Molecular and Cellular Biochemistry, Ohio State University, Columbus, OH 43210, USA.

Science (New York, N.Y.)
|January 30, 2010
PubMed
Summary

Researchers created a recombinant prion protein that caused prion disease in mice. This supports the prion hypothesis that misfolded prion protein (PrP) causes these fatal neurodegenerative conditions.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Protein Chemistry

Background:

  • Prion diseases are fatal neurodegenerative disorders.
  • The prion hypothesis suggests a misfolded prion protein (PrP) isoform causes infectivity.
  • Understanding PrP misfolding is crucial for disease mechanisms.

Purpose of the Study:

  • To create a recombinant prion with pathogenic characteristics.
  • To test if this recombinant prion can induce prion disease in vivo.
  • To validate the prion hypothesis using a recombinant PrP model.

Main Methods:

  • Purification of recombinant murine prion protein (PrP) from Escherichia coli.
  • Generation of a recombinant prion exhibiting aggregation, protease resistance, and self-propagation.

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  • Intracerebral injection of recombinant prion into wild-type mice.

    • Main Results:

    • Mice injected with recombinant prion developed neurological signs around 130 days.
    • Diseased mice reached terminal stages by approximately 150 days post-injection.
    • Neuropathology, protease-resistant PrP, and disease transmission confirmed prion disease.

    Conclusions:

    • The study successfully generated a recombinant prion capable of causing disease.
    • Findings provide direct experimental support for the prion hypothesis.
    • Infectivity in mammalian prion disease is attributed to an altered PrP conformation.