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Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24

Author

Listed:
  • Yoko Fujita-Fujiharu

    (Kyoto University
    Kyoto University
    Japan Science and Technology Agency
    Max Planck Institute of Biochemistry)

  • Shangfan Hu

    (Kyoto University
    Kyoto University
    Japan Science and Technology Agency)

  • Ai Hirabayashi

    (Kyoto University
    Japan Science and Technology Agency)

  • Yuki Takamatsu

    (Nagasaki University)

  • Yen Ni Ng

    (Kyoto University
    Kyoto University
    Japan Science and Technology Agency)

  • Kazuya Houri

    (Kyoto University
    Kyoto University
    Japan Science and Technology Agency)

  • Yukiko Muramoto

    (Kyoto University
    Kyoto University
    Japan Science and Technology Agency)

  • Masahiro Nakano

    (Kyoto University
    Kyoto University
    Japan Science and Technology Agency)

  • Yukihiko Sugita

    (Kyoto University
    Kyoto University
    Kyoto University)

  • Takeshi Noda

    (Kyoto University
    Kyoto University
    Japan Science and Technology Agency
    Kyoto University)

Abstract

The Ebola virus, a member of the Filoviridae family, causes severe hemorrhagic fever in humans. Filamentous virions contain a helical nucleocapsid responsible for genome transcription, replication, and packaging into progeny virions. The nucleocapsid consists of a helical nucleoprotein (NP)–viral genomic RNA complex forming the core structure, to which VP24 and VP35 bind externally. Two NPs, each paired with a VP24 molecule, constitute a repeating unit. However, the detailed nucleocapsid structure remains unclear. Here, we determine the nucleocapsid-like structure within virus-like particles at 4.6 Å resolution using single-particle cryo-electron microscopy. Mutational analysis identifies specific interactions between the two NPs and two VP24s and demonstrates that each of the two VP24s in different orientations distinctively regulates nucleocapsid assembly, viral RNA synthesis, intracellular transport of the nucleocapsid, and infectious virion production. Our findings highlight the sophisticated mechanisms underlying the assembly and functional regulation of the nucleocapsid and provide insights into antiviral development.

Suggested Citation

  • Yoko Fujita-Fujiharu & Shangfan Hu & Ai Hirabayashi & Yuki Takamatsu & Yen Ni Ng & Kazuya Houri & Yukiko Muramoto & Masahiro Nakano & Yukihiko Sugita & Takeshi Noda, 2025. "Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24," Nature Communications, Nature, vol. 16(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57236-4
    DOI: 10.1038/s41467-025-57236-4
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    References listed on IDEAS

    as
    1. Yukihiko Sugita & Hideyuki Matsunami & Yoshihiro Kawaoka & Takeshi Noda & Matthias Wolf, 2018. "Cryo-EM structure of the Ebola virus nucleoprotein–RNA complex at 3.6 Å resolution," Nature, Nature, vol. 563(7729), pages 137-140, November.
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