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Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
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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

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Protein Misfolding Cyclic Amplification of Prions
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TDP-43 Prions.

Takashi Nonaka1, Masato Hasegawa1

  • 1Dementia Research Project, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, Japan 156-8506.

Cold Spring Harbor Perspectives in Medicine
|January 22, 2017
PubMed
Summary

Neurodegenerative diseases involve protein misfolding. Aberrant TAR-DNA binding protein of 43 kDa (TDP-43) aggregates spread like prions, offering new therapeutic targets.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • Neurodegenerative diseases like Alzheimer's and Parkinson's are linked to protein misfolding and aggregate formation in neurons.
  • TAR-DNA binding protein of 43 kDa (TDP-43) is implicated in these conditions.

Purpose of the Study:

  • To investigate the prion-like behavior of TAR-DNA binding protein of 43 kDa (TDP-43) aggregates.
  • To explore the potential for novel therapeutic strategies targeting TDP-43 aggregate propagation.

Main Methods:

  • In vitro studies of TDP-43 aggregation.
  • Classification of insoluble TDP-43 strains from patient brains.
  • Cell-to-cell transfer experiments of TDP-43 aggregates.

Main Results:

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  • TDP-43 forms aggregates in vitro in a seed-dependent, self-templating, prion-like manner.
  • Insoluble TDP-43 from patient brains can be classified into distinct strains.
  • These TDP-43 strains exhibit cell-to-cell transmissibility in vitro.

Conclusions:

  • TDP-43 aggregation and propagation share mechanisms with prion diseases.
  • Aberrant TDP-43 aggregates may spread between cells in a prion-like fashion.
  • Targeting TDP-43 aggregate spread presents a potential therapeutic avenue for neurodegenerative diseases.