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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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Related Experiment Video

Updated: Apr 14, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

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Animal models for prion-like diseases.

Natalia Fernández-Borges1, Hasier Eraña1, Vanesa Venegas1

  • 1CIC bioGUNE, Parque tecnológico de Bizkaia, Derio 48160, Bizkaia, Spain.

Virus Research
|April 25, 2015
PubMed
Summary

Prion diseases involve misfolded prion proteins (PrP) causing neurodegeneration. This review explores how other neurodegenerative diseases like Alzheimer's and Parkinson's share similar "prion-like" protein misfolding and propagation mechanisms.

Keywords:
Animal modelsPrionPrion-like disordersScrapieTSE

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • Prion diseases, or Transmissible Spongiform Encephalopathies (TSEs), are fatal neurodegenerative disorders caused by misfolded prion proteins (PrP).
  • These diseases affect various mammals, including Creutzfeldt-Jacob Disease (CJD) in humans, Bovine Spongiform Encephalopathy (BSE) in cattle, and Chronic Wasting Disease (CWD) in cervids.
  • The

Purpose of the Study:

  • To review evidence of shared mechanisms between prion diseases and other protein misfolding disorders.
  • To analyze prion-like features, such as seeding and propagation, in diseases like Alzheimer's, Parkinson's, ALS, and AA amyloidosis.
  • To examine these features using available in vivo models for each disease.

Main Methods:

  • Literature review of prion disease research.
  • Analysis of in vivo models for Alzheimer's Disease (AD), Parkinson's Disease (PD), Amyotrophic Lateral Sclerosis (ALS), and systemic Amyloid A amyloidosis (AA amyloidosis).
  • Comparison of prion-like features (seeding, propagation, neurotoxicity, infectivity, transmission barriers, strains) across diseases.

Main Results:

  • Prion protein (PrP) misfolding into a beta-sheet rich form (PrPSc) drives TSEs.
  • Evidence suggests shared prion-like mechanisms in AD (amyloid-beta, tau), PD (alpha-synuclein), ALS (SOD-1, TDP-43), and AA amyloidosis (serum amyloid A).
  • These shared features include protein aggregation, seeding, propagation, and strain variability.

Conclusions:

  • Misfolded proteins exhibiting prion-like behavior are implicated in a range of neurodegenerative and systemic amyloid diseases.
  • Understanding these shared mechanisms offers potential therapeutic targets for diverse protein misfolding disorders.
  • Prion research provides a valuable framework for investigating other amyloid diseases.