ArticleScientific reports2016
Glycosylation changes in the globular head of H3N2 influenza hemagglutinin modulate receptor binding without affecting virus virulence.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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49 citing papers in PubMed, 56 citations in OpenAlex.
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- N-linked glycosylation sites with low occupancy support sustained circulation of the A(H3N2) influenza A virus in the human population.Journal of virology · 2026Article
- Emergence of Novel Reassortant H3N2 Avian Influenza Viruses in Southern China: Genetic Complexity and Pathogenicity in Chickens and Mice.Animals : an open access journal from MDPI · 2026Article
- Weak selection and stochastic processes limit the emergence of antigenic variants during household transmission of influenza A viruses.PLoS pathogens · 2026Article
- Genetic characterization of influenza A (A/H3N2) viruses reveals antigenic drift in receptor binding domain and possible vaccine mismatch in strains circulating in Riyadh, Saudi Arabia, 2024-2025.BMC infectious diseases · 2026Article
- Structural and immunological characterization of the H3 influenza hemagglutinin during antigenic drift.Nature communications · 2025Article
- Chronology of H3N2 human influenza virus surface glycoprotein adaptation from 1968 to 2019 reveals a surge of adaptation between 1997 and 2002.Journal of virology · 2025Article
- Weak selection and stochastic processes limit the emergence of antigenic variants during household transmission of influenza A viruses.bioRxiv : the preprint server for biology · 2025Article
- Genetic characteristics of influenza A/H3N2 virus in Jiaxing, China (2019-2024).Virology journal · 2025Article
- Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections.FEBS open bio · 2025Review
- Plasma nontargeted metabolomics study of H1N1 and H3N2 influenza in children.Frontiers in cellular and infection microbiology · 2025Article
- Inactivated influenza virus vaccines expressing COBRA hemagglutinin elicited broadly reactive, long-lived protective antibodies.Human vaccines & immunotherapeutics · 2024Article
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- Molecular Markers and Mechanisms of Influenza A Virus Cross-Species Transmission and New Host Adaptation.Viruses · 2024Review
- Combining machine learning with structure-based protein design to predict and engineer post-translational modifications of proteins.PLoS computational biology · 2024Article
- Clinical characteristics and assessment of risk factors in patients with influenza A-induced severe pneumonia after the prevalence of SARS-CoV-2.Open medicine (Warsaw, Poland) · 2024Article
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- 2019-2020 H1N1 clade A5a.1 viruses have better in vitro fitness compared with the co-circulating A5a.2 clade.Scientific reports · 2023Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- α2,3-Linked Sialic Acids Are the Potential Attachment Receptor for Shaan Virus Infection in MARC-145 Cells.Microbiology spectrum · 2022Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
Abstract
Since the emergence of human H3N2 influenza A viruses in the pandemic of 1968, these viruses have become established as strains of moderate severity. A decline in virulence has been accompanied by glycan accumulation on the hemagglutinin globular head, and hemagglutinin receptor binding has changed from recognition of a broad spectrum of glycan receptors to a narrower spectrum. The relationship between increased glycosylation, binding changes, and reduction in H3N2 virulence is not clear. We evaluated the effect of hemagglutinin glycosylation on receptor binding and virulence of engineered H3N2 viruses. We demonstrate that low-binding virus is as virulent as higher binding counterparts, suggesting that H3N2 infection does not require either recognition of a wide variety of, or high avidity binding to, receptors. Among the few glycans recognized with low-binding virus, there were two structures that were bound by the vast majority of H3N2 viruses isolated between 1968 and 2012. We suggest that these two structures support physiologically relevant binding of H3N2 hemagglutinin and that this physiologically relevant binding has not changed since the 1968 pandemic. Therefore binding changes did not contribute to reduced severity of seasonal H3N2 viruses. This work will help direct the search for factors enhancing influenza virulence.
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