Cited by 563Influenza Virus Research StudiesCarbohydrate Chemistry and SynthesisGlycosylation and Glycoproteins Research

Contemporary H3N2 influenza viruses have a glycosylation site that alters binding of antibodies elicited by egg-adapted vaccine strains

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Zost, Seth J., Parkhouse, Kaela, Gumina, Megan E., Kim, Kangchon, Diaz Perez, Sebastian, Wilson, Patrick C., Treanor, John J., Sant, Andrea J. +2 more·2017·Proceedings of the National Academy of Sciences

Abstract

Significance: The majority of influenza vaccine antigens are prepared in chicken eggs. Human vaccine strains grown in eggs often possess adaptive mutations that increase viral attachment to chicken cells. Most of these adaptive mutations are in the hemagglutinin protein, which functions as a viral attachment factor. Here, we identify a hemagglutinin mutation in the current egg-adapted H3N2 vaccine strain that alters antigenicity. We show that ferrets and humans exposed to the current egg-adapted H3N2 vaccine strain produce antibodies that poorly neutralize H3N2 viruses that circulated during the 2016–2017 influenza season. These studies highlight the challenges associated with producing influenza vaccine antigens in eggs, while offering a potential explanation of why there was only moderate vaccine effectiveness during the 2016–2017 influenza season.

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Authors
Zost, S. J., Parkhouse, K., Gumina, M. E., Kim, K., Diaz Perez, S., Wilson, P. C., Treanor, J. J., Sant, A. J., Cobey, S., & Hensley, S. E.
Affiliations
  • University of Pennsylvania (US)
  • University of Chicago (US)
  • Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104;
  • University of Rochester Medicine (US)
Corresponding author
Hensley, Scott E.
Venue
Proceedings of the National Academy of Sciences
Published
2017-11-06
Volume
114
Issue
47
Pages
12578-12583
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2767495920
Cited by
563
References
49
Citations by year
2026: 42 · 2025: 37 · 2024: 60 · 2023: 51 · 2022: 59 · 2021: 70 · 2020: 82 · 2019: 89 · 2018: 64 · 2017: 8
FWCI
52.28
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • Knowledge@UChicago (University of Chicago) (submittedVersion, cc-by-nc-nd)
  • University of Chicago
Funders
  • HHS | National Institutes of Health (1R01AI113047, 1R01AI108686, DP2AI117921, HHSN272201400005C)
  • Burroughs Wellcome Fund (1015433)
Topics
  • Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Keywords
H3N2 influenza virus, antibody neutralization, vaccine effectiveness, 2016-2017 influenza season, ferret model
MeSH terms
Immunogenicity, Vaccine, Animals, Antibodies, Viral, Antigens, Viral, Chickens, Ferrets, Glycosylation, Humans, Influenza, Human, Influenza Vaccines, Mutation, Neutralization Tests, Ovum, Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H3N2 Subtype

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