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Structural basis of potent Zika–dengue virus antibody cross-neutralization

Author

Listed:
  • Giovanna Barba-Spaeth

    (Institut Pasteur, Unité de Virologie Structurale
    CNRS UMR 3569 Virologie)

  • Wanwisa Dejnirattisai

    (Hammersmith campus, Imperial College London)

  • Alexander Rouvinski

    (Institut Pasteur, Unité de Virologie Structurale
    CNRS UMR 3569 Virologie)

  • Marie-Christine Vaney

    (Institut Pasteur, Unité de Virologie Structurale
    CNRS UMR 3569 Virologie)

  • Iris Medits

    (Medical University of Vienna)

  • Arvind Sharma

    (Institut Pasteur, Unité de Virologie Structurale
    CNRS UMR 3569 Virologie)

  • Etienne Simon-Lorière

    (Institut Pasteur, Unité de Génétique fonctionnelle des maladies infectieuses
    CNRS URA 3012, F-75724)

  • Anavaj Sakuntabhai

    (Institut Pasteur, Unité de Génétique fonctionnelle des maladies infectieuses
    CNRS URA 3012, F-75724)

  • Van-Mai Cao-Lormeau

    (Unit of Emerging Infectious Diseases, Institut Louis Malardé)

  • Ahmed Haouz

    (Institut Pasteur, Plateforme de Cristallographie, CiTech
    CNRS UMR 3528)

  • Patrick England

    (CNRS UMR 3528
    Institut Pasteur, Plateforme de Biophysique des Macromolécules et de leurs Interactions, CiTech)

  • Karin Stiasny

    (Medical University of Vienna)

  • Juthathip Mongkolsapaya

    (Hammersmith campus, Imperial College London
    Dengue Hemorrhagic Fever Research Unit, Office for Research and Development, Siriraj Hospital, Faculty of Medicine, Mahidol University)

  • Franz X. Heinz

    (Medical University of Vienna)

  • Gavin R. Screaton

    (Hammersmith campus, Imperial College London)

  • Félix A. Rey

    (Institut Pasteur, Unité de Virologie Structurale
    CNRS UMR 3569 Virologie)

Abstract

Zika virus is a member of the Flavivirus genus that had not been associated with severe disease in humans until the recent outbreaks, when it was linked to microcephaly in newborns in Brazil and to Guillain–Barré syndrome in adults in French Polynesia. Zika virus is related to dengue virus, and here we report that a subset of antibodies targeting a conformational epitope isolated from patients with dengue virus also potently neutralize Zika virus. The crystal structure of two of these antibodies in complex with the envelope protein of Zika virus reveals the details of a conserved epitope, which is also the site of interaction of the envelope protein dimer with the precursor membrane (prM) protein during virus maturation. Comparison of the Zika and dengue virus immunocomplexes provides a lead for rational, epitope-focused design of a universal vaccine capable of eliciting potent cross-neutralizing antibodies to protect simultaneously against both Zika and dengue virus infections.

Suggested Citation

  • Giovanna Barba-Spaeth & Wanwisa Dejnirattisai & Alexander Rouvinski & Marie-Christine Vaney & Iris Medits & Arvind Sharma & Etienne Simon-Lorière & Anavaj Sakuntabhai & Van-Mai Cao-Lormeau & Ahmed Hao, 2016. "Structural basis of potent Zika–dengue virus antibody cross-neutralization," Nature, Nature, vol. 536(7614), pages 48-53, August.
    • Handle: RePEc:nat:nature:v:536:y:2016:i:7614:d:10.1038_nature18938
    DOI: 10.1038/nature18938
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    Cited by:

    1. Fabian Sesterhenn & Che Yang & Jaume Bonet & Johannes T. Cramer & Xiaolin Wen & Yimeng Wang & Chi I. Chiang & Luciano Andres Abriata & Iga Kucharska & Giacomo Castoro & Sabrina S. Vollers & Marie Gall, 2020. "De novo protein design enables the precise induction of RSV-neutralizing antibodies," Post-Print hal-02677103, HAL.

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