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Inactivation of the scrapie agent by pronase

Insights

Scrapie infectivity is eliminated by treating the agent with both proteinase and sodium dodecyl sulfate. This confirms that a protein component is essential for scrapie transmission.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Infectious Diseases

Background:

  • Scrapie is a fatal neurodegenerative disease affecting sheep and goats.
  • The causative agent of scrapie is known as a prion, a misfolded protein.
  • Understanding the prion's composition is crucial for developing diagnostics and therapeutics.

Purpose of the Study:

  • To investigate the biochemical composition of the scrapie agent.
  • To determine the role of protein and nucleic acid components in scrapie infectivity.

Main Methods:

  • Partial purification of the scrapie agent from infected mouse brain using agarose-polyacrylamide gel electrophoresis.
  • Treatment of the purified agent with RNase A, DNase I, pronase, sodium dodecyl sulfate (SDS), and a combination of SDS-pronase.

Main Results:

  • Treatment with RNase A or DNase I did not significantly reduce scrapie infectivity.
  • Treatment with pronase or SDS alone reduced infectivity by approximately 98%.
  • Combined treatment with SDS and pronase almost completely inactivated scrapie infectivity.

Conclusions:

  • The results strongly indicate that a protein component is essential for scrapie infectivity.
  • Nucleic acids (RNA or DNA) are not required for scrapie transmission.
  • These findings support the prion hypothesis, which posits that prions are infectious proteins.

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