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Structure of Ljungan virus provides insight into genome packaging of this picornavirus

Author

Listed:
  • Ling Zhu

    (University of Oxford, The Henry Wellcome Building for Genomic Medicine
    The Pirbright Institute)

  • Xiangxi Wang

    (National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science)

  • Jingshan Ren

    (University of Oxford, The Henry Wellcome Building for Genomic Medicine)

  • Claudine Porta

    (University of Oxford, The Henry Wellcome Building for Genomic Medicine
    The Pirbright Institute)

  • Hannah Wenham

    (The Pirbright Institute)

  • Jens-Ola Ekström

    (Linnaeus University)

  • Anusha Panjwani

    (The Pirbright Institute)

  • Nick J. Knowles

    (The Pirbright Institute)

  • Abhay Kotecha

    (University of Oxford, The Henry Wellcome Building for Genomic Medicine)

  • C. Alistair Siebert

    (University of Oxford, The Henry Wellcome Building for Genomic Medicine)

  • A. Michael Lindberg

    (Linnaeus University)

  • Elizabeth E. Fry

    (University of Oxford, The Henry Wellcome Building for Genomic Medicine)

  • Zihe Rao

    (National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science
    Laboratory of Structural Biology, School of Medicine, Tsinghua University)

  • Tobias J. Tuthill

    (The Pirbright Institute)

  • David I. Stuart

    (University of Oxford, The Henry Wellcome Building for Genomic Medicine
    Diamond Light Sources, Harwell Science and Innovation Campus)

Abstract

Picornaviruses are responsible for a range of human and animal diseases, but how their RNA genome is packaged remains poorly understood. A particularly poorly studied group within this family are those that lack the internal coat protein, VP4. Here we report the atomic structure of one such virus, Ljungan virus, the type member of the genus Parechovirus B, which has been linked to diabetes and myocarditis in humans. The 3.78-Å resolution cryo-electron microscopy structure shows remarkable features, including an extended VP1 C terminus, forming a major protuberance on the outer surface of the virus, and a basic motif at the N terminus of VP3, binding to which orders some 12% of the viral genome. This apparently charge-driven RNA attachment suggests that this branch of the picornaviruses uses a different mechanism of genome encapsidation, perhaps explored early in the evolution of picornaviruses.

Suggested Citation

  • Ling Zhu & Xiangxi Wang & Jingshan Ren & Claudine Porta & Hannah Wenham & Jens-Ola Ekström & Anusha Panjwani & Nick J. Knowles & Abhay Kotecha & C. Alistair Siebert & A. Michael Lindberg & Elizabeth E, 2015. "Structure of Ljungan virus provides insight into genome packaging of this picornavirus," Nature Communications, Nature, vol. 6(1), pages 1-9, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9316
    DOI: 10.1038/ncomms9316
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