Contemporary H3N2 influenza viruses have a glycosylation site that alters binding of antibodies elicited by egg-adapted vaccine strains
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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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Loss of a glycosylation site in egg-grown influenza vaccines was associated with poor efficacy during the 2016-2017 season.
“For example, loss of a glycosylation site in egg-grown vaccines was associated with poor efficacy during the 2016–2017 season139.”
From mRNA vaccines for infectious diseases: principles, delivery and clinical translation (2021) · cites this paper as [139]
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mRNA vaccines for infectious diseases: principles, delivery and clinical translation
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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.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-11-06
- Volume
- 114
- Issue
- 47
- Pages
- 12578-12583
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5703309
- 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
- hybrid
- doi.org
- Licence
- 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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