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Structures of Coxsackievirus A10 unveil the molecular mechanisms of receptor binding and viral uncoating

Author

Listed:
  • Ling Zhu

    (Chinese Academy of Sciences)

  • Yao Sun

    (Chinese Academy of Sciences)

  • Jinyan Fan

    (Major Project Department)

  • Bin Zhu

    (Hunan Normal University)

  • Lei Cao

    (Chinese Academy of Sciences)

  • Qiang Gao

    (Sinovac Biotech Co., Ltd)

  • Yanjun Zhang

    (Zhejiang Provincial Center for Disease Control and Prevention)

  • Hongrong Liu

    (Hunan Normal University)

  • Zihe Rao

    (Chinese Academy of Sciences
    Tsinghua University)

  • Xiangxi Wang

    (Chinese Academy of Sciences)

Abstract

Coxsackievirus A10 (CVA10), a human type-A Enterovirus (HEV-A), can cause diseases ranging from hand-foot-and-mouth disease to polio-myelitis-like disease. CVA10, together with some other HEV-As, utilizing the molecule KREMEN1 as an entry receptor, constitutes a KREMEN1-dependent subgroup within HEV-As. Currently, there is no vaccine or antiviral therapy available for treating diseases caused by CVA10. The atomic-resolution structure of the CVA10 virion, which is within the KREMEN1-dependent subgroup, shows significant conformational differences in the putative receptor binding sites and serotype-specific epitopes, when compared to the SCARB2-dependent subgroup of HEV-A, such as EV71, highlighting specific differences between the sub-groups. We also report two expanded structures of CVA10, an empty particle and uncoating intermediate at atomic resolution, as well as a medium-resolution genome structure reconstructed using a symmetry-mismatch method. Structural comparisons coupled with previous results, reveal an ordered signal transmission process for enterovirus uncoating, converting exo-genetic receptor-attachment inputs into a generic RNA release mechanism.

Suggested Citation

  • Ling Zhu & Yao Sun & Jinyan Fan & Bin Zhu & Lei Cao & Qiang Gao & Yanjun Zhang & Hongrong Liu & Zihe Rao & Xiangxi Wang, 2018. "Structures of Coxsackievirus A10 unveil the molecular mechanisms of receptor binding and viral uncoating," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07531-0
    DOI: 10.1038/s41467-018-07531-0
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    Cited by:

    1. Selma Dahmane & Adeline Kerviel & Dustin R. Morado & Kasturika Shankar & Björn Ahlman & Michael Lazarou & Nihal Altan-Bonnet & Lars-Anders Carlson, 2022. "Membrane-assisted assembly and selective secretory autophagy of enteroviruses," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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