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Structure of the full-length HCV IRES in solution

Author

Listed:
  • Julien Pérard

    (UMI 3265 UJF-EMBL-CNRS, Unit of Virus Host-Cell Interactions)

  • Cédric Leyrat

    (UMI 3265 UJF-EMBL-CNRS, Unit of Virus Host-Cell Interactions)

  • Florence Baudin

    (UMI 3265 UJF-EMBL-CNRS, Unit of Virus Host-Cell Interactions
    European Molecular Biology Laboratory (EMBL))

  • Emmanuel Drouet

    (UMI 3265 UJF-EMBL-CNRS, Unit of Virus Host-Cell Interactions)

  • Marc Jamin

    (UMI 3265 UJF-EMBL-CNRS, Unit of Virus Host-Cell Interactions)

Abstract

The 5′-untranslated region of the hepatitis C virus genome contains an internal ribosome entry site (IRES) that initiates cap-independent translation of the viral RNA. Until now, the structural characterization of the entire (IRES) remained limited to cryo-electron microscopy reconstructions of the (IRES) bound to different cellular partners. Here we report an atomic model of free full-length hepatitis C virus (IRES) refined by selection against small-angle X-ray scattering data that incorporates the known structures of different fragments. We found that an ensemble of conformers reproduces small-angle X-ray scattering data better than a single structure suggesting in combination with molecular dynamics simulations that the hepatitis C virus (IRES) is an articulated molecule made of rigid parts that move relative to each other. Principal component analysis on an ensemble of physically accessible conformers of hepatitis C virus (IRES) revealed dominant collective motions in the molecule, which may underlie the conformational changes occurring in the (IRES) molecule upon formation of the initiation complex.

Suggested Citation

  • Julien Pérard & Cédric Leyrat & Florence Baudin & Emmanuel Drouet & Marc Jamin, 2013. "Structure of the full-length HCV IRES in solution," Nature Communications, Nature, vol. 4(1), pages 1-11, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2611
    DOI: 10.1038/ncomms2611
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