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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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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.

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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.

Keywords:
Alzheimer's diseaseCreutzfeldt–Jakob diseaseamyloid β-proteinautomated scrapie cell assayprion

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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.