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High flavivirus structural plasticity demonstrated by a non-spherical morphological variant

Author

Listed:
  • Seamus R. Morrone

    (Duke-NUS Medical School
    National University of Singapore)

  • Valerie S. Y. Chew

    (Duke-NUS Medical School
    National University of Singapore)

  • Xin-Ni Lim

    (Duke-NUS Medical School
    National University of Singapore)

  • Thiam-Seng Ng

    (Duke-NUS Medical School
    National University of Singapore)

  • Victor A. Kostyuchenko

    (Duke-NUS Medical School
    National University of Singapore)

  • Shuijun Zhang

    (Duke-NUS Medical School
    National University of Singapore)

  • Melissa Wirawan

    (Duke-NUS Medical School
    National University of Singapore)

  • Pau-Ling Chew

    (Duke-NUS Medical School
    National University of Singapore)

  • Jaime Lee

    (Duke-NUS Medical School
    National University of Singapore)

  • Joanne L. Tan

    (Duke-NUS Medical School
    National University of Singapore)

  • Jiaqi Wang

    (Duke-NUS Medical School
    National University of Singapore)

  • Ter Yong Tan

    (Duke-NUS Medical School
    National University of Singapore)

  • Jian Shi

    (National University of Singapore
    National University of Singapore)

  • Gavin Screaton

    (University of Oxford)

  • Marc C. Morais

    (University of Texas Medical Branch)

  • Shee-Mei Lok

    (Duke-NUS Medical School
    National University of Singapore)

Abstract

Previous flavivirus (dengue and Zika viruses) studies showed largely spherical particles either with smooth or bumpy surfaces. Here, we demonstrate flavivirus particles have high structural plasticity by the induction of a non-spherical morphology at elevated temperatures: the club-shaped particle (clubSP), which contains a cylindrical tail and a disc-like head. Complex formation of DENV and ZIKV with Fab C10 stabilize the viruses allowing cryoEM structural determination to ~10 Å resolution. The caterpillar-shaped (catSP) Fab C10:ZIKV complex shows Fabs locking the E protein raft structure containing three E dimers. However, compared to the original spherical structure, the rafts have rotated relative to each other. The helical tail structure of Fab C10:DENV3 clubSP showed although the Fab locked an E protein dimer, the dimers have shifted laterally. Morphological diversity, including clubSP and the previously identified bumpy and smooth-surfaced spherical particles, may help flavivirus survival and immune evasion.

Suggested Citation

  • Seamus R. Morrone & Valerie S. Y. Chew & Xin-Ni Lim & Thiam-Seng Ng & Victor A. Kostyuchenko & Shuijun Zhang & Melissa Wirawan & Pau-Ling Chew & Jaime Lee & Joanne L. Tan & Jiaqi Wang & Ter Yong Tan &, 2020. "High flavivirus structural plasticity demonstrated by a non-spherical morphological variant," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16925-y
    DOI: 10.1038/s41467-020-16925-y
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