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Flavivirus maturation leads to the formation of an occupied lipid pocket in the surface glycoproteins

Author

Listed:
  • Max Renner

    (University of Oxford)

  • Wanwisa Dejnirattisai

    (University of Oxford)

  • Loïc Carrique

    (University of Oxford)

  • Itziar Serna Martin

    (Faculty of Science, Utrecht University)

  • Dimple Karia

    (University of Oxford)

  • Serban L. Ilca

    (University of Oxford)

  • Shu F. Ho

    (University of Oxford)

  • Abhay Kotecha

    (University of Oxford)

  • Jeremy R. Keown

    (University of Oxford)

  • Juthathip Mongkolsapaya

    (University of Oxford
    Mahidol University)

  • Gavin R. Screaton

    (University of Oxford)

  • Jonathan M. Grimes

    (University of Oxford
    Diamond Light Source Ltd)

Abstract

Flaviviruses such as Dengue (DENV) or Zika virus (ZIKV) assemble into an immature form within the endoplasmatic reticulum (ER), and are then processed by furin protease in the trans-Golgi. To better grasp maturation, we carry out cryo-EM reconstructions of immature Spondweni virus (SPOV), a human flavivirus of the same serogroup as ZIKV. By employing asymmetric localised reconstruction we push the resolution to 3.8 Å, enabling us to refine an atomic model which includes the crucial furin protease recognition site and a conserved Histidine pH-sensor. For direct comparison, we also solve structures of the mature forms of SPONV and DENV to 2.6 Å and 3.1 Å, respectively. We identify an ordered lipid that is present in only the mature forms of ZIKV, SPOV, and DENV and can bind as a consequence of rearranging amphipathic stem-helices of E during maturation. We propose a structural role for the pocket and suggest it stabilizes mature E.

Suggested Citation

  • Max Renner & Wanwisa Dejnirattisai & Loïc Carrique & Itziar Serna Martin & Dimple Karia & Serban L. Ilca & Shu F. Ho & Abhay Kotecha & Jeremy R. Keown & Juthathip Mongkolsapaya & Gavin R. Screaton & J, 2021. "Flavivirus maturation leads to the formation of an occupied lipid pocket in the surface glycoproteins," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21505-9
    DOI: 10.1038/s41467-021-21505-9
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    Cited by:

    1. Marie-Christine Vaney & Mariano Dellarole & Stéphane Duquerroy & Iris Medits & Georgios Tsouchnikas & Alexander Rouvinski & Patrick England & Karin Stiasny & Franz X. Heinz & Félix A. Rey, 2022. "Evolution and activation mechanism of the flavivirus class II membrane-fusion machinery," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Sarah Goellner & Giray Enkavi & Vibhu Prasad & Solène Denolly & Sungmin Eu & Giulia Mizzon & Leander Witte & Waldemar Kulig & Zina M. Uckeley & Teresa M. Lavacca & Uta Haselmann & Pierre-Yves Lozach &, 2023. "Zika virus prM protein contains cholesterol binding motifs required for virus entry and assembly," Nature Communications, Nature, vol. 14(1), pages 1-20, December.

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