Structure of the full-length HCV IRES in solution

Julien Pérard, Cédric Leyrat, Florence Baudin, Emmanuel Drouet and Marc Jamin ()
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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
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

Nature Communications, 2013, vol. 4, issue 1, 1-11

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms2611

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