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Soluble dimeric prion protein binds PrP(Sc) in vivo and antagonizes prion disease

Philipp Meier1, Nicolas Genoud, Marco Prinz

  • 1Institute of Neuropathology, Schmelzbergstrasse, University Hospital of Zürich, Zürich, Switzerland.

Cell
|April 8, 2003
PubMed

Insights

Soluble prion protein derivatives, like PrP-Fc(2), can block the conversion of normal cellular prion protein (PrP(C)) into infectious PrP(Sc) forms, thus inhibiting prion replication and disease.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Cellular prion protein (PrP(C)) converts to pathological PrP(Sc) via an unknown mechanism.
  • Prion diseases, like scrapie, are characterized by PrP(Sc) accumulation and neurodegeneration.

Purpose of the Study:

  • To investigate the role of soluble prion protein derivatives in prion conversion and disease pathogenesis.
  • To determine if PrP-Fc(2) can inhibit prion replication in vivo.

Main Methods:

  • Generated transgenic mice expressing PrP(C) fused to immunoglobulin Fcgamma (PrP-Fc(2)).
  • Inoculated mice with infectious prions and monitored disease progression.
  • Analyzed PrP(Sc) accumulation, agent replication, and PrP-Fc(2) localization and conversion in the brain.

Main Results:

  • PrP-Fc(2) expression delayed PrP(Sc) accumulation, agent replication, and disease onset in wild-type mice.
  • PrP-Fc(2) localized to lipid rafts and associated with PrP(Sc) but resisted conversion.
  • Mice lacking endogenous PrP(C) but expressing PrP-Fc(2) were resistant to scrapie and did not transmit the disease.

Conclusions:

  • PrP-Fc(2) interferes with prion propagation and scrapie pathogenesis by resisting conversion.
  • Soluble prion protein derivatives show potential as novel antagonists of prion replication.

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