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Glycan repositioning of influenza hemagglutinin stem facilitates the elicitation of protective cross-group antibody responses

Author

Listed:
  • Seyhan Boyoglu-Barnum

    (National Institutes of Health)

  • Geoffrey B. Hutchinson

    (National Institutes of Health)

  • Jeffrey C. Boyington

    (National Institutes of Health)

  • Syed M. Moin

    (National Institutes of Health)

  • Rebecca A. Gillespie

    (National Institutes of Health)

  • Yaroslav Tsybovsky

    (Electron Microscopy Laboratory, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute, ATRF)

  • Tyler Stephens

    (Electron Microscopy Laboratory, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research sponsored by the National Cancer Institute, ATRF)

  • John R. Vaile

    (National Institutes of Health)

  • Julia Lederhofer

    (National Institutes of Health)

  • Kizzmekia S. Corbett

    (National Institutes of Health)

  • Brian E. Fisher

    (National Institutes of Health)

  • Hadi M. Yassine

    (Qatar University)

  • Sarah F. Andrews

    (National Institutes of Health)

  • Michelle C. Crank

    (National Institutes of Health)

  • Adrian B. McDermott

    (National Institutes of Health)

  • John R. Mascola

    (National Institutes of Health)

  • Barney S. Graham

    (National Institutes of Health)

  • Masaru Kanekiyo

    (National Institutes of Health)

Abstract

The conserved hemagglutinin (HA) stem has been a focus of universal influenza vaccine efforts. Influenza A group 1 HA stem-nanoparticles have been demonstrated to confer heterosubtypic protection in animals; however, the protection does not extend to group 2 viruses, due in part to differences in glycosylation between group 1 and 2 stems. Here, we show that introducing the group 2 glycan at Asn38HA1 to a group 1 stem-nanoparticle (gN38 variant) based on A/New Caledonia/20/99 (H1N1) broadens antibody responses to cross-react with group 2 HAs. Immunoglobulins elicited by the gN38 variant provide complete protection against group 2 H7N9 virus infection, while the variant loses protection against a group 1 H5N1 virus. The N38HA1 glycan thus is pivotal in directing antibody responses by controlling access to group-determining stem epitopes. Precise targeting of stem-directed antibody responses to the site of vulnerability by glycan repositioning may be a step towards achieving cross-group influenza protection.

Suggested Citation

  • Seyhan Boyoglu-Barnum & Geoffrey B. Hutchinson & Jeffrey C. Boyington & Syed M. Moin & Rebecca A. Gillespie & Yaroslav Tsybovsky & Tyler Stephens & John R. Vaile & Julia Lederhofer & Kizzmekia S. Corb, 2020. "Glycan repositioning of influenza hemagglutinin stem facilitates the elicitation of protective cross-group antibody responses," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14579-4
    DOI: 10.1038/s41467-020-14579-4
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