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July 16, 2025Open Access

Membrane-anchored PrPSc is the trigger for prion synaptotoxicity

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Authors

JGJean R.P. GatdulaRMRobert C.C. MercerJVJanelle S. Vultaggio

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Overview

Experimental strategies reveal that membrane-anchored PrP Sc initiates synaptotoxic signaling in neurons, suggesting potential therapeutic approaches.

Key Points

  • New findings indicate that membrane-anchored PrP Sc is essential for initiating synaptotoxic signaling in prion diseases.
  • Using specific PrP C mutations, the study demonstrates impaired conversion to PrP Sc reduces synaptic damage in neurons.
  • Dendritic spine density decreased due to prion exposure, but was prevented by the G126V PrP mutation.
  • These results point to new therapeutic strategies targeting PrP Sc formation to combat prion-mediated neurodegeneration.

Cite This Study

Gatdula et al. (2025) studied this question.

synapsesocial.com/papers/689a02c9e6551bb0af8ccdedhttps://doi.org/10.1101/2025.07.11.664221
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Full atomistic model of prion structure and conversion2019 · 118 citations
  2. 2The G126V Mutation in the Mouse Prion Protein Hinders Nucleation-Dependent Fibril Formation by Slowing Initial Fibril Growth and by Increasing the Critical Concentration2017 · 26 citations
  3. 3Formation of native prions from minimal components <i>in vitro</i>2007 · 636 citations
  4. 4Identifying Key Components of the PrPC-PrPSc Replicative Interface2008 · 31 citations
  5. 5Prions activate a p38 MAPK synaptotoxic signaling pathway2018 · 74 citations