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A potent Henipavirus cross-neutralizing antibody reveals a dynamic fusion-triggering pattern of the G-tetramer

Author

Listed:
  • Pengfei Fan

    (Institute of Biotechnology)

  • Mengmeng Sun

    (University of Science and Technology of China)

  • Xinghai Zhang

    (Chinese Academy of Sciences)

  • Huajun Zhang

    (Chinese Academy of Sciences)

  • Yujiao Liu

    (Institute of Biotechnology)

  • Yanfeng Yao

    (Chinese Academy of Sciences)

  • Ming Li

    (University of Science and Technology of China)

  • Ting Fang

    (Institute of Biotechnology)

  • Bingjie Sun

    (Institute of Biotechnology)

  • Zhengshan Chen

    (Institute of Biotechnology)

  • Xiangyang Chi

    (Institute of Biotechnology)

  • Li Chen

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Cheng Peng

    (Chinese Academy of Sciences)

  • Zhen Chen

    (Chinese Academy of Sciences)

  • Guanying Zhang

    (Institute of Biotechnology)

  • Yi Ren

    (Institute of Biotechnology)

  • Zixuan Liu

    (Institute of Biotechnology)

  • Yaohui Li

    (Institute of Biotechnology)

  • Jianmin Li

    (Institute of Biotechnology)

  • Entao Li

    (University of Science and Technology of China)

  • Wuxiang Guan

    (Chinese Academy of Sciences)

  • Shanshan Li

    (University of Science and Technology of China
    University of Science and Technology of China
    University of Science and Technology of China)

  • Rui Gong

    (Chinese Academy of Sciences)

  • Kaiming Zhang

    (University of Science and Technology of China
    University of Science and Technology of China
    University of Science and Technology of China)

  • Changming Yu

    (Institute of Biotechnology)

  • Sandra Chiu

    (University of Science and Technology of China
    University of Science and Technology of China
    Key Laboratory of Anhui Province for Emerging and Reemerging Infectious Diseases)

Abstract

The Hendra and Nipah viruses (HNVs) are highly pathogenic pathogens without approved interventions for human use. In addition, the interaction pattern between the attachment (G) and fusion (F) glycoproteins required for virus entry remains unclear. Here, we isolate a panel of Macaca-derived G-specific antibodies that cross-neutralize HNVs via multiple mechanisms. The most potent antibody, 1E5, confers adequate protection against the Nipah virus challenge in female hamsters. Crystallography demonstrates that 1E5 has a highly similar binding pattern to the receptor. In cryo-electron microscopy studies, the tendency of 1E5 to bind to the upper or lower heads results in two distinct quaternary structures of G. Furthermore, we identify the extended outer loop β1S2-β1S3 of G and two pockets on the apical region of fusion (F) glycoprotein as the essential sites for G-F interactions. This work highlights promising drug candidates against HNVs and contributes deeper insights into the viruses.

Suggested Citation

  • Pengfei Fan & Mengmeng Sun & Xinghai Zhang & Huajun Zhang & Yujiao Liu & Yanfeng Yao & Ming Li & Ting Fang & Bingjie Sun & Zhengshan Chen & Xiangyang Chi & Li Chen & Cheng Peng & Zhen Chen & Guanying , 2024. "A potent Henipavirus cross-neutralizing antibody reveals a dynamic fusion-triggering pattern of the G-tetramer," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-48601-w
    DOI: 10.1038/s41467-024-48601-w
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    1. Patrick O. Byrne & Brian E. Fisher & David R. Ambrozak & Elizabeth G. Blade & Yaroslav Tsybovsky & Barney S. Graham & Jason S. McLellan & Rebecca J. Loomis, 2023. "Structural basis for antibody recognition of vulnerable epitopes on Nipah virus F protein," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
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