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Darwinian evolution of prions in cell culture

Academic Article
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Overview

authors

  • Li, J. L.
  • Browning, S.
  • Mahal, S. P.
  • Oelschlegel, A. M.
  • Weissmann, Charles

publication date

  • February 2010

journal

  • Science  Journal

abstract

  • Prions are infectious proteins consisting mainly of PrP(Sc), a beta sheet-rich conformer of the normal host protein PrP(C), and occur in different strains. Strain identity is thought to be encoded by PrP(Sc) conformation. We found that biologically cloned prion populations gradually became heterogeneous by accumulating "mutants," and selective pressures resulted in the emergence of different mutants as major constituents of the evolving population. Thus, when transferred from brain to cultured cells, "cell-adapted" prions outcompeted their "brain-adapted" counterparts, and the opposite occurred when prions were returned from cells to brain. Similarly, the inhibitor swainsonine selected for a resistant substrain, whereas, in its absence, the susceptible substrain outgrew its resistant counterpart. Prions, albeit devoid of a nucleic acid genome, are thus subject to mutation and selective amplification.

subject areas

  • Animals
  • Brain Chemistry
  • Cell Line
  • Cell Line, Tumor
  • Culture Media
  • Culture Media, Conditioned
  • Evolution, Molecular
  • Mice
  • Mice, Inbred C57BL
  • Mutation
  • PrPSc Proteins
  • Prion Diseases
  • Prions
  • Protein Conformation
  • Swainsonine
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Identity

PubMed Central ID

  • PMC2848070

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1183218

PubMed ID

  • 20044542
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Additional Document Info

start page

  • 869

end page

  • 872

volume

  • 327

issue

  • 5967

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