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A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA

Author

Listed:
  • Sandhya Bangaru

    (Vanderbilt University Medical Center)

  • Heng Zhang

    (The Scripps Research Institute
    Institute of High Energy Physics, Chinese Academy of Sciences)

  • Iuliia M. Gilchuk

    (Vanderbilt University Medical Center)

  • Thomas G. Voss

    (Vanderbilt University Medical Center
    Vanderbilt University Medical Center)

  • Ryan P. Irving

    (Vanderbilt University Medical Center)

  • Pavlo Gilchuk

    (Vanderbilt University Medical Center)

  • Pranathi Matta

    (Vanderbilt University Medical Center)

  • Xueyong Zhu

    (The Scripps Research Institute)

  • Shanshan Lang

    (The Scripps Research Institute)

  • Travis Nieusma

    (The Scripps Research Institute)

  • Juergen A. Richt

    (College of Veterinary Medicine, Kansas State University)

  • Randy A. Albrecht

    (at Icahn School of Medicine at Mount Sina)

  • Hillary A. Vanderven

    (Peter Doherty Institute for Infection and Immunity, University of Melbourne)

  • Robin Bombardi

    (Vanderbilt University Medical Center)

  • Stephen J. Kent

    (Peter Doherty Institute for Infection and Immunity, University of Melbourne)

  • Andrew B. Ward

    (The Scripps Research Institute)

  • Ian A. Wilson

    (The Scripps Research Institute
    The Scripps Research Institute)

  • James E. Crowe

    (Vanderbilt University Medical Center
    Vanderbilt University Medical Center
    Vanderbilt University Medical Center)

Abstract

The high rate of antigenic drift in seasonal influenza viruses necessitates frequent changes in vaccine composition. Recent seasonal H3 vaccines do not protect against swine-origin H3N2 variant (H3N2v) strains that recently have caused severe human infections. Here, we report a human VH1-69 gene-encoded monoclonal antibody (mAb) designated H3v-47 that exhibits potent cross-reactive neutralization activity against human and swine H3N2 viruses that circulated since 1989. The crystal structure and electron microscopy reconstruction of H3v-47 Fab with the H3N2v hemagglutinin (HA) identify a unique epitope spanning the vestigial esterase and receptor-binding subdomains that is distinct from that of any known neutralizing antibody for influenza A H3 viruses. MAb H3v-47 functions largely by blocking viral egress from infected cells. Interestingly, H3v-47 also engages Fcγ receptor and mediates antibody dependent cellular cytotoxicity (ADCC). This newly identified conserved epitope can be used in design of novel immunogens for development of broadly protective H3 vaccines.

Suggested Citation

  • Sandhya Bangaru & Heng Zhang & Iuliia M. Gilchuk & Thomas G. Voss & Ryan P. Irving & Pavlo Gilchuk & Pranathi Matta & Xueyong Zhu & Shanshan Lang & Travis Nieusma & Juergen A. Richt & Randy A. Albrech, 2018. "A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA," Nature Communications, Nature, vol. 9(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04704-9
    DOI: 10.1038/s41467-018-04704-9
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    Cited by:

    1. Zhao-Shan Chen & Hsiang-Chi Huang & Xiangkun Wang & Karin Schön & Yane Jia & Michael Lebens & Danica F. Besavilla & Janarthan R. Murti & Yanhong Ji & Aishe A. Sarshad & Guohua Deng & Qiyun Zhu & David, 2025. "Influenza A Virus H7 nanobody recognizes a conserved immunodominant epitope on hemagglutinin head and confers heterosubtypic protection," Nature Communications, Nature, vol. 16(1), pages 1-17, December.

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