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Prions and the potential transmissibility of protein misfolding diseases

Allison Kraus1, Bradley R Groveman, Byron Caughey

  • 1Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840;

Annual Review of Microbiology
|July 2, 2013
PubMed

Insights

Prions are infectious proteins causing transmissible spongiform encephalopathies (TSEs) through self-propagation. Evidence suggests prion-like spreading in other protein misfolding diseases, raising concerns about their role in pathogenesis.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Prions, or infectious proteins, are a key area in infectious agent research.
  • Transmissible spongiform encephalopathies (TSEs) in mammals are caused by misfolded prion proteins.
  • Prion structures are ill-defined but are self-propagating, highly structured, fibrillar multimers.

Purpose of the Study:

  • To define the structural characteristics of TSE prions.
  • To explore the potential for prion-like propagation in other protein misfolding diseases.
  • To investigate the role of prion-like mechanisms in disease pathogenesis and prevalence.

Main Methods:

  • Characterization of purified TSE prions.
  • Review of recent reports on cell-to-cell protein propagation.
  • Analysis of structural similarities between TSE prions and amyloid fibrils.

Main Results:

  • TSE prions are typically amyloid fibrils, which are self-seeding structures.
  • Amyloid fibrils are common in neurodegenerative diseases like Alzheimer's and Parkinson's.
  • Evidence indicates prion-like propagation of misfolded proteins between cells.

Conclusions:

  • Misfolded proteins in various diseases may propagate in a prion-like manner.
  • This prion-like spreading could contribute to disease development and spread.
  • Further research is needed to understand the implications of prion-like mechanisms in neurodegeneration.

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