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Commercial influenza vaccines vary in HA-complex structure and in induction of cross-reactive HA antibodies

Author

Listed:
  • Mallory L. Myers

    (National Institutes of Health)

  • John R. Gallagher

    (National Institutes of Health)

  • Alexander J. Kim

    (National Institutes of Health)

  • Walker H. Payne

    (National Institutes of Health)

  • Samantha Maldonado-Puga

    (National Institutes of Health)

  • Haralabos Assimakopoulos

    (National Institutes of Health)

  • Kevin W. Bock

    (National Institutes of Health)

  • Udana Torian

    (National Institutes of Health
    National Cancer Institute)

  • Ian N. Moore

    (National Institutes of Health
    Emory University)

  • Audray K. Harris

    (National Institutes of Health)

Abstract

Influenza virus infects millions of people annually and can cause global pandemics. Hemagglutinin (HA) is the primary component of commercial influenza vaccines (CIV), and antibody titer to HA is a primary correlate of protection. Continual antigenic variation of HA requires that CIVs are reformulated yearly. Structural organization of HA complexes have not previously been correlated with induction of broadly reactive antibodies, yet CIV formulations vary in how HA is organized. Using electron microscopy to study four current CIVs, we find structures including: individual HAs, starfish structures with up to 12 HA molecules, and novel spiked-nanodisc structures that display over 50 HA molecules along the complex’s perimeter. CIV containing these spiked nanodiscs elicit the highest levels of heterosubtypic cross-reactive antibodies in female mice. Here, we report that HA structural organization can be an important CIV parameter and can be associated with the induction of cross-reactive antibodies to conserved HA epitopes.

Suggested Citation

  • Mallory L. Myers & John R. Gallagher & Alexander J. Kim & Walker H. Payne & Samantha Maldonado-Puga & Haralabos Assimakopoulos & Kevin W. Bock & Udana Torian & Ian N. Moore & Audray K. Harris, 2023. "Commercial influenza vaccines vary in HA-complex structure and in induction of cross-reactive HA antibodies," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-37162-z
    DOI: 10.1038/s41467-023-37162-z
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    References listed on IDEAS

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    1. Linling He & Natalia de Val & Charles D. Morris & Nemil Vora & Therese C. Thinnes & Leopold Kong & Parisa Azadnia & Devin Sok & Bin Zhou & Dennis R. Burton & Ian A Wilson & David Nemazee & Andrew B. W, 2016. "Presenting native-like trimeric HIV-1 antigens with self-assembling nanoparticles," Nature Communications, Nature, vol. 7(1), pages 1-15, November.
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