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Structure and antigenicity of divergent Henipavirus fusion glycoproteins

Author

Listed:
  • Ariel Isaacs

    (The University of Queensland)

  • Yu Shang Low

    (The University of Queensland)

  • Kyle L. Macauslane

    (The University of Queensland)

  • Joy Seitanidou

    (The University of Queensland)

  • Cassandra L. Pegg

    (The University of Queensland)

  • Stacey T. M. Cheung

    (The University of Queensland)

  • Benjamin Liang

    (The University of Queensland)

  • Connor A. P. Scott

    (The University of Queensland)

  • Michael J. Landsberg

    (The University of Queensland
    The University of Queensland)

  • Benjamin L. Schulz

    (The University of Queensland
    The University of Queensland)

  • Keith J. Chappell

    (The University of Queensland
    The University of Queensland
    Australian Institute for Bioengineering and Nanotechnology)

  • Naphak Modhiran

    (The University of Queensland)

  • Daniel Watterson

    (The University of Queensland
    The University of Queensland)

Abstract

In August 2022, a novel henipavirus (HNV) named Langya virus (LayV) was isolated from patients with severe pneumonic disease in China. This virus is closely related to Mòjiāng virus (MojV), and both are divergent from the bat-borne HNV members, Nipah (NiV) and Hendra (HeV) viruses. The spillover of LayV is the first instance of a HNV zoonosis to humans outside of NiV and HeV, highlighting the continuing threat this genus poses to human health. In this work, we determine the prefusion structures of MojV and LayV F proteins via cryogenic electron microscopy to 2.66 and 3.37 Å, respectively. We show that despite sequence divergence from NiV, the F proteins adopt an overall similar structure but are antigenically distinct as they do not react to known antibodies or sera. Glycoproteomic analysis revealed that while LayV F is less glycosylated than NiV F, it contains a glycan that shields a site of vulnerability previously identified for NiV. These findings explain the distinct antigenic profile of LayV and MojV F, despite the extent to which they are otherwise structurally similar to NiV. Our results carry implications for broad-spectrum HNV vaccines and therapeutics, and indicate an antigenic, yet not structural, divergence from prototypical HNVs.

Suggested Citation

  • Ariel Isaacs & Yu Shang Low & Kyle L. Macauslane & Joy Seitanidou & Cassandra L. Pegg & Stacey T. M. Cheung & Benjamin Liang & Connor A. P. Scott & Michael J. Landsberg & Benjamin L. Schulz & Keith J., 2023. "Structure and antigenicity of divergent Henipavirus fusion glycoproteins," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39278-8
    DOI: 10.1038/s41467-023-39278-8
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    References listed on IDEAS

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    1. Davide Corti & Siro Bianchi & Fabrizia Vanzetta & Andrea Minola & Laurent Perez & Gloria Agatic & Barbara Guarino & Chiara Silacci & Jessica Marcandalli & Benjamin J. Marsland & Antonio Piralla & Elen, 2013. "Cross-neutralization of four paramyxoviruses by a human monoclonal antibody," Nature, Nature, vol. 501(7467), pages 439-443, September.
    2. Olivier Pernet & Bradley S. Schneider & Shannon M. Beaty & Matthew LeBreton & Tatyana E. Yun & Arnold Park & Trevor T. Zachariah & Thomas A. Bowden & Peta Hitchens & Christina M. Ramirez & Peter Dasza, 2014. "Evidence for henipavirus spillover into human populations in Africa," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
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    Cited by:

    1. Yingying Guo & Songyue Wu & Wenting Li & Haonan Yang & Tianhao Shi & Bin Ju & Zheng Zhang & Renhong Yan, 2024. "The cryo-EM structure of homotetrameric attachment glycoprotein from langya henipavirus," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Johannes P. M. Langedijk & Freek Cox & Nicole V. Johnson & Daan Overveld & Lam Le & Ward Hoogen & Richard Voorzaat & Roland Zahn & Leslie Fits & Jarek Juraszek & Jason S. McLellan & Mark J. G. Bakkers, 2024. "Universal paramyxovirus vaccine design by stabilizing regions involved in structural transformation of the fusion protein," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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