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Related Experiment Videos

Comparative sequence analysis, in vitro expression and biosynthesis of mouse PrP.

B Caughey1, R Race, B Chesebro

  • 1Laboratory of Persistent Viral Diseases, National Institute of Allergy and Infectious Diseases, Hamilton, MT 59840.

Progress in Clinical and Biological Research
|January 1, 1989
PubMed
Summary

Researchers investigated if the prion protein (PrP) itself is the infectious agent behind scrapie. In vitro expression of PrP from infected brains did not cause scrapie, suggesting PrP may not be the agent or requires modification.

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Neuropathology and applied neurobiology·2012

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Infectious Diseases

Background:

  • The prion protein (PrP) is implicated in transmissible spongiform encephalopathies (TSEs) like scrapie.
  • A hypothesis suggests PrP from infected brains constitutes the infectious scrapie agent.
  • The normal function of PrP remains undetermined.

Purpose of the Study:

  • To directly test if PrP messenger RNA (mRNA) from scrapie-infected brains can encode the infectious agent.
  • To investigate PrP biosynthesis in normal and scrapie-infected cells to identify potential alterations.

Main Methods:

  • In vitro expression of PrP cDNA cloned from scrapie-infected mouse brain.
  • Transmission studies inoculating expressed PrP into susceptible mice.
  • Analysis of PrP biosynthesis in normal and scrapie-infected mouse neuroblastoma cells.

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Main Results:

  • In vitro expressed PrP failed to transmit scrapie to mice.
  • No scrapie-associated modifications in PrP biosynthesis were observed in infected cells.
  • Metabolically labeled PrP was not resistant to proteinase K in either cell type.

Conclusions:

  • PrP expressed in vitro may not be the infectious scrapie agent, or it requires post-translational modification for infectivity.
  • Scrapie infection in vitro did not alter PrP biosynthesis.
  • Conserved structural features in PrP across species suggest potential functional significance.