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Variable tau accumulation in murine models with abnormal prion protein deposits.

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Infectious prions and proteinopathies.

Rona M Barron1

  • 1a Neurobiology Division, The Roslin Institute and Royal Dick School of Veterinary Studies, University of Edinburgh , Easter Bush , UK.

Prion
|March 11, 2017
PubMed
Summary
This summary is machine-generated.

Synthetic prion protein (PrP) fibrils do not always cause transmissible spongiform encephalopathies (TSEs). Misfolded PrP can seed amyloid plaques, but infectivity may depend on specific subpopulations, not all misfolded PrP.

Keywords:
TSEamyloidprionprion-likesynthetic prions

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Infectious Diseases

Background:

  • Transmissible spongiform encephalopathies (TSEs) are linked to misfolded prion protein (PrP).
  • The prion agent propagates by converting normal PrP to abnormal forms.
  • Synthetic prions (rec-PrP fibrils) are used to study PrP aggregation and infectivity.

Purpose of the Study:

  • To determine if recombinant PrP (rec-PrP) fibrils alone are infectious prions.
  • To investigate whether PrP aggregates inevitably cause TSE disease.
  • To explore the relationship between PrP misfolding, seeding, and infectivity.

Main Methods:

  • Inoculation of rec-PrP fibrils into PrP-P101L knock-in transgenic mice (101LL).
  • Monitoring for clinical TSE disease and changes in infectious titre.
  • Observation of PrP amyloid plaque formation.

Main Results:

  • Inoculation of rec-PrP fibrils did not consistently induce TSE disease or increase infectious titre.
  • rec-PrP fibrils were capable of seeding PrP amyloid plaques in 101LL mice.
  • These findings suggest a distinction between protein misfolding and prion infectivity.

Conclusions:

  • Protein misfolding, including that of PrP, does not automatically result in infectious TSE disease.
  • Only specific subpopulations of misfolded PrP may be infectious and neurotoxic.
  • The study highlights the complexity of prion diseases and protein misfolding disorders.