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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Frameshifted prion proteins as pathological agents: quantitative considerations.

Peter R Wills1

  • 1Integrative Transcriptomics, Center for Bioinformatics Tübingen, University of Tübingen, Sand 14, Tübingen 72076, Germany. p.wills@auckland.ac.nz

Journal of Theoretical Biology
|March 5, 2013
PubMed
Summary
This summary is machine-generated.

Transmissible spongiform encephalopathy agents may involve prion protein (PrP) variants with frameshifted elements. This study proposes a replication mechanism and calculates variant concentrations, resolving infectivity correlations.

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Protein Misfolding Cyclic Amplification of Prions
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Published on: November 7, 2012

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases.
  • The precise nature of the infectious prion agent remains incompletely understood.
  • Quantitative discrepancies exist between infectivity titers and prion protein (PrP) variant concentrations.

Purpose of the Study:

  • To provide a quantitatively consistent explanation for TSE infectivity titers.
  • To propose a mechanism for the replication of specific prion protein variants.
  • To resolve the correlation gap between infectivity and PrP variant detection.

Main Methods:

  • Theoretical modeling of prion protein variant populations.
  • Calculations of frameshifted PrP variant concentrations in various biological samples.
  • Analysis of prion protein misfolding cyclic amplification products.

Main Results:

  • A model where TSE agents comprise a small fraction of frameshifted PrP variants.
  • Estimates for the concentration of these variants in normal and infected brain tissue.
  • Demonstration of variant enrichment in protein misfolding cyclic amplification.

Conclusions:

  • Frameshifted PrP variants offer a quantitative explanation for prion infectivity.
  • The proposed replication mechanism supports their etiological role.
  • Experimental validation is proposed to confirm or refute this hypothesis.