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Prions on the move

Charles Weissmann1, Jiali Li, Sukhvir P Mahal

  • 1Department of Infectology, Scripps Florida, 130 Scripps Way, Jupiter, Florida 33458, USA. charlesw@scripps.edu

EMBO Reports
|October 15, 2011
PubMed

Insights

Prion diseases involve PrP(Sc) aggregates, which exist as diverse strains with varying conformations. These prion populations act as quasi-species, with specific conformers selected for efficient replication in different environments, influencing transmission and drug resistance.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Prion Biology

Background:

  • Prions are infectious proteins, primarily composed of aggregated PrP(Sc) conformers of the host PrP(C).
  • Prions exhibit strain diversity, characterized by distinct conformations despite originating from the same PrP(C) sequence.
  • Prion transmission dynamics suggest evolutionary processes like mutation and selection.

Purpose of the Study:

  • To investigate the concept of prion populations as quasi-species.
  • To explain the mechanisms behind prion strain variation, interspecies transmission efficiency, and drug resistance.

Main Methods:

  • The study proposes a theoretical framework based on existing prion research and experimental observations.
  • Analysis of prion behavior under different conditions, including interspecies transmission and drug exposure.

Main Results:

  • Prion populations contain a variety of conformers, analogous to viral quasi-species.
  • Environmental factors, such as host species or drug presence, select for specific prion conformers.
  • This selection process influences prion transmissibility and the emergence of drug-resistant variants.

Conclusions:

  • Prion propagation is driven by the selection of the most fit conformers within a quasi-species population.
  • This quasi-species model provides a unified explanation for prion strain diversity, adaptation, and resistance.

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