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Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
Published on: October 3, 2012
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Soluble Aβ aggregates can inhibit prion propagation
Claire J Sarell1, Emma Quarterman1, Daniel C-M Yip1
1MRC Prion Unit at UCL, UCL Institute of Prion Diseases, National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK.
Open Biology
|November 17, 2017
Summary
Soluble amyloid-beta (Aβ) assemblies that bind to prion protein (PrPC) can inhibit prion propagation. This suggests Aβ may compete with prions, offering insights into neurodegenerative disease mechanisms.
Area of Science:
- Neurodegenerative diseases
- Prion biology
- Alzheimer's disease pathogenesis
Background:
- Mammalian prions cause fatal neurodegenerative diseases like Creutzfeldt-Jakob disease (CJD), involving misfolded prion protein (PrPC).
- Ligands binding to PrPC can impede prion spread and neurotoxicity.
- Soluble amyloid-beta (Aβ) assemblies, implicated in Alzheimer's disease (AD), bind tightly to PrPC.
Purpose of the Study:
- To investigate if soluble Aβ assemblies can inhibit prion propagation.
- To explore the role of Aβ-PrPC interactions in prion disease.
Main Methods:
- Utilized cellular models of prion infection and propagation.
- Employed distinct preparations of soluble amyloid-beta (Aβ) assemblies.
- Assessed the binding affinity of Aβ assemblies to PrPC in vitro.
Main Results:
- Aβ assemblies with high PrPC binding affinity inhibited prion infection and propagation.
- Aβ forms with minimal PrPC binding showed no attenuation of prion propagation.
- Demonstrated that Aβ aggregates compete with prions for PrPC binding.
Conclusions:
- Soluble Aβ aggregates can act as inhibitors of prion propagation.
- Highlights the bidirectional interplay between Aβ and PrPC in AD and prion diseases.
- Suggests Aβ's inhibitory effect on prion propagation may explain reduced CJD incidence in older individuals with high Aβ deposition.
