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Structural basis for a human broadly neutralizing influenza A hemagglutinin stem-specific antibody including H17/18 subtypes

Author

Listed:
  • Yulu Chen

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

  • Fei Wang

    (Chinese Academy of Sciences)

  • Liwei Yin

    (Chinese Academy of Sciences)

  • Haihai Jiang

    (Chinese Academy of Sciences)

  • Xishan Lu

    (Chinese Academy of Sciences)

  • Yuhai Bi

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

  • Wei Zhang

    (Chinese Academy of Sciences)

  • Yi Shi

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

  • Roberto Burioni

    (Università Vita-Salute San Raffaele)

  • Zhou Tong

    (Chinese Academy of Sciences)

  • Hao Song

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

  • Jianxun Qi

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

  • George F. Gao

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

Abstract

Influenza infection continues are a persistent threat to public health. The identification and characterization of human broadly neutralizing antibodies can facilitate the development of antibody drugs and the design of universal influenza vaccines. Here, we present structural information for the human antibody PN-SIA28’s heterosubtypic binding of hemagglutinin (HA) from circulating and emerging potential influenza A viruses (IAVs). Aside from group 1 and 2 conventional IAV HAs, PN-SIA28 also inhibits membrane fusion mediated by bat-origin H17 and H18 HAs. Crystallographic analyses of Fab alone or in complex with H1, H14, and H18 HA proteins reveal that PN-SIA28 binds to a highly conserved epitope in the fusion domain of different HAs, with the same CDRHs but different CDRLs for different HAs tested, distinguishing it from other structurally characterized anti-stem antibodies. The binding characteristics of PN-SIA28 provides information to support the design of increasingly potent engineered antibodies, antiviral drugs, and/or universal influenza vaccines.

Suggested Citation

  • Yulu Chen & Fei Wang & Liwei Yin & Haihai Jiang & Xishan Lu & Yuhai Bi & Wei Zhang & Yi Shi & Roberto Burioni & Zhou Tong & Hao Song & Jianxun Qi & George F. Gao, 2022. "Structural basis for a human broadly neutralizing influenza A hemagglutinin stem-specific antibody including H17/18 subtypes," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-35236-y
    DOI: 10.1038/s41467-022-35236-y
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    References listed on IDEAS

    as
    1. Wenshuai Wang & Xiaoyu Sun & Yanbing Li & Jinpeng Su & Zhiyang Ling & Tianlong Zhang & Fang Wang & Hong Zhang & Hualan Chen & Jianping Ding & Bing Sun, 2016. "Human antibody 3E1 targets the HA stem region of H1N1 and H5N6 influenza A viruses," Nature Communications, Nature, vol. 7(1), pages 1-12, December.
    2. Umut Karakus & Thiprampai Thamamongood & Kevin Ciminski & Wei Ran & Sira C. Günther & Marie O. Pohl & Davide Eletto & Csaba Jeney & Donata Hoffmann & Sven Reiche & Jan Schinköthe & Reiner Ulrich & Jul, 2019. "MHC class II proteins mediate cross-species entry of bat influenza viruses," Nature, Nature, vol. 567(7746), pages 109-112, March.
    Full references (including those not matched with items on IDEAS)

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