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Prion-like features of misfolded Aβ and tau aggregates

Rodrigo Morales1, Keri Callegari1, Claudio Soto1

  • 1Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, 6431 Fannin Street, Houston, TX 77030, United States.

Virus Research
|January 11, 2015
PubMed

Insights

Misfolded proteins like amyloid-beta (Aβ) and tau exhibit prion-like characteristics, including transmission and conformational diversity, as observed in animal models, though human epidemiological data is limited.

Area of Science:

  • Neuroscience
  • Protein Misfolding Diseases
  • Prion Biology

Background:

  • Misfolded proteins can propagate disease through prion-like mechanisms.
  • The extent of prion-like behavior in non-prion proteinopathies is debated due to limited human data.

Purpose of the Study:

  • To review recent studies on the prion-like features of amyloid-beta (Aβ) and tau.
  • To highlight similarities between Aβ/tau aggregates and bona fide prions.

Main Methods:

  • Review of recent scientific literature on protein misfolding diseases.
  • Analysis of studies involving Aβ and tau aggregates in animal models.
  • Comparison of prion-like characteristics across different proteinopathies.

Main Results:

  • Aβ and tau aggregates display prion-like characteristics in animal models.
  • Evidence supports inter-individual transmission, strain-like conformational diversity, and aggregate spread for Aβ and tau.
  • Similarities observed include transmission via various administration routes.

Conclusions:

  • Misfolded Aβ and tau proteins exhibit significant prion-like features, particularly in experimental settings.
  • Further research is needed to fully understand the implications of these findings for human disease pathogenesis.
  • Prion-like mechanisms offer a framework for studying the spread and progression of neurodegenerative diseases.
Keywords:
Amyloid-βPrionPrion-like mechanismsTau

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