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Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
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A Bioluminescent Cell Assay to Quantify Prion Protein Dimerization.

Katharina Annick Wüsten1, Pasham Parameshwar Reddy1, Andrej Smiyakin1

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|September 23, 2018
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A novel bioluminescent prion assay (BPA) quantifies prion protein (PrP) dimerization, a key factor in prion diseases. This assay identified JTC-801 as a potent inhibitor of both PrP dimerization and prion replication.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Prion protein (PrP) misfolding causes fatal neurodegenerative diseases like Creutzfeldt-Jakob disease.
  • The role of PrP dimerization in prion disease pathogenesis remains largely unknown.
  • Developing tools to study PrP dimerization is crucial for understanding disease mechanisms.

Purpose of the Study:

  • To develop and validate a novel assay for quantifying PrP dimerization.
  • To investigate the conditions affecting PrP dimerization.
  • To screen for compounds that inhibit PrP dimerization and prion replication.

Main Methods:

  • A bioluminescent Prion Assay (BPA) was developed using split Gaussia luciferase complementation fused to PrP.
  • PrP dimerization was measured on the surface of RK13 cells (RK13-DC cells).
  • A compound library was screened using BPA to identify inhibitors of PrP dimerization.

Main Results:

  • The BPA successfully quantified PrP dimerization, which was reduced by anti-PrP antibodies.
  • PrP dimerization was induced by cellular stress and was independent of divalent cations.
  • The assay detected prion strain challenges and identified JTC-801 as a potent inhibitor of PrP dimerization and prion replication.

Conclusions:

  • The BPA is a versatile tool for studying prion biology and PrP dimerization.
  • BPA facilitates the identification of novel anti-prion compounds.
  • JTC-801 shows promise as a therapeutic candidate for prion diseases.