---
title: "Low-occupancy N-linked glycosylation on HA supports A(H3N2) influenza circulation"
id: "pubmed-42663462"
canonical_url: "https://medichelpline.com/clinical-feed/pubmed-42663462"
content_type: "clinical_feed_article"
specialty: "Infectious Disease"
source_name: "PubMed / NCBI"
source_url: "https://pubmed.ncbi.nlm.nih.gov/42663462/"
doi: "10.1128/jvi.00662-26"
published_at: "2026-09-22T00:00:00.000Z"
evidence_level: "Journal Article"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Low-occupancy N-linked glycosylation on HA supports A(H3N2) influenza circulation
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/pubmed-42663462
- **Specialty:** [Infectious Disease](https://medichelpline.com/clinical-feed/infectious-disease.md)
- **Primary Source:** PubMed / NCBI
- **Source URL:** [Original Journal Publication](https://pubmed.ncbi.nlm.nih.gov/42663462/)
- **DOI:** [10.1128/jvi.00662-26](https://doi.org/10.1128%2Fjvi.00662-26)
- **Published At:** 2026-09-22T00:00:00.000Z
- **Evidence Rating:** Journal Article
## Executive GIST (TL;DR)
- Glycosylation of influenza A virus **hemagglutinin** (HA) is important for viral fitness and immune evasion; contemporary human A(H3N2) viruses can have up to 13 putative N-linked glycosylation sites. - Glycan occupancy across HA sites is heterogeneous: most sites are nearly fully occupied, while some sites (notably at amino acid residues **45** and **144**) are only partially occupied and are evolutionarily unstable. - The functional effects of highly occupied HA glycans are well described, but the roles of **low-occupancy** glycosylation sites have been less clear. - Using reverse-genetics A(H3N2) viruses engineered to lack glycans at residue 45, residue 144, or both, investigators assessed receptor binding, thermal stability, fusion, replication in cell culture, and immune responses in mice. - Loss of glycans at these low-occupancy sites reduced receptor binding, thermal stability, and fusion efficiency, but did not reduce viral growth in Madin-Darby canine kidney (MDCK) epithelial cell culture. - In mice, the presence of low-level glycosylation at residues 45 and 144 decreased antibody titers that correlate with virus neutralization and protection, indicating an effect on immune recognition. - The study authors propose that transient introduction of low-occupancy glycosylation sites allows A(H3N2) viruses to reduce antibody pressure on antigenic and receptor binding sites without markedly compromising replication or virulence. - This balance—partial immune evasion with minimal fitness cost—may help sustain circulation of A(H3N2) viruses in human populations. - Keywords highlighted in the source include **glycosylation**, **hemagglutinin**, immune evasion, influenza, and viral evolution.
## Clinical Analysis & Structured Key Points
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Epub 2026 Aug 28. # N-linked glycosylation sites with low occupancy support sustained circulation of the A(H3N2) influenza A virus in the human population [Irina V Alymova](https://pubmed.ncbi.nlm.nih.gov/?term=Alymova+IV&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Betlehem Mekonnen](https://pubmed.ncbi.nlm.nih.gov/?term=Mekonnen+B&cauthor_id=42663462)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-2 "Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-3 "Oak Ridge Institute for Science and Education, Oak Ridge, Tennessee, USA."), [Dongxia Wang](https://pubmed.ncbi.nlm.nih.gov/?term=Wang+D&cauthor_id=42663462)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-2 "Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Ram P Kamal](https://pubmed.ncbi.nlm.nih.gov/?term=Kamal+RP&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-4 "Federal Civilian Division, General Dynamics Information Technology, Atlanta, Georgia, USA."), [Wen-Pin Tzeng](https://pubmed.ncbi.nlm.nih.gov/?term=Tzeng+W-P&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Alexander S Jureka](https://pubmed.ncbi.nlm.nih.gov/?term=Jureka+AS&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 5 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-5 "Chippewa Government Solutions, LLC, Sault Sainte Marie, Michigan, USA."), [John R Barr](https://pubmed.ncbi.nlm.nih.gov/?term=Barr+JR&cauthor_id=42663462)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-2 "Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Shane Gansebom](https://pubmed.ncbi.nlm.nih.gov/?term=Gansebom+S&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-4 "Federal Civilian Division, General Dynamics Information Technology, Atlanta, Georgia, USA."), [Ian A York](https://pubmed.ncbi.nlm.nih.gov/?term=York+IA&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#full-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.") Affiliations Expand ### Affiliations * 1 Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA. * 2 Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA. * 3 Oak Ridge Institute for Science and Education, Oak Ridge, Tennessee, USA. * 4 Federal Civilian Division, General Dynamics Information Technology, Atlanta, Georgia, USA. * 5 Chippewa Government Solutions, LLC, Sault Sainte Marie, Michigan, USA. * PMID: **42663462** * DOI: [ 10.1128/jvi.00662-26 ](https://doi.org/10.1128/jvi.00662-26) Item in Clipboard # N-linked glycosylation sites with low occupancy support sustained circulation of the A(H3N2) influenza A virus in the human population Irina V Alymova et al. J Virol. 2026. Show details Display options Display options Format Abstract PubMed PMID J Virol Actions * [ Search in PubMed ](https://pubmed.ncbi.nlm.nih.gov/?term=%22J+Virol%22%5Bjour%5D&sort=date&sort_order=desc) * [ Search in NLM Catalog ](https://www.ncbi.nlm.nih.gov/nlmcatalog?term=%22J+Virol%22%5BTitle+Abbreviation%5D) * [ Add to Search ](https://pubmed.ncbi.nlm.nih.gov/42663462/) . 2026 Sep 22;100(9):e0066226. doi: 10.1128/jvi.00662-26. Epub 2026 Aug 28. ### Authors [Irina V Alymova](https://pubmed.ncbi.nlm.nih.gov/?term=Alymova+IV&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Betlehem Mekonnen](https://pubmed.ncbi.nlm.nih.gov/?term=Mekonnen+B&cauthor_id=42663462)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-2 "Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 3 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-3 "Oak Ridge Institute for Science and Education, Oak Ridge, Tennessee, USA."), [Dongxia Wang](https://pubmed.ncbi.nlm.nih.gov/?term=Wang+D&cauthor_id=42663462)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-2 "Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Ram P Kamal](https://pubmed.ncbi.nlm.nih.gov/?term=Kamal+RP&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-4 "Federal Civilian Division, General Dynamics Information Technology, Atlanta, Georgia, USA."), [Wen-Pin Tzeng](https://pubmed.ncbi.nlm.nih.gov/?term=Tzeng+W-P&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Alexander S Jureka](https://pubmed.ncbi.nlm.nih.gov/?term=Jureka+AS&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 5 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-5 "Chippewa Government Solutions, LLC, Sault Sainte Marie, Michigan, USA."), [John R Barr](https://pubmed.ncbi.nlm.nih.gov/?term=Barr+JR&cauthor_id=42663462)[ 2 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-2 "Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA."), [Shane Gansebom](https://pubmed.ncbi.nlm.nih.gov/?term=Gansebom+S&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.")[ 4 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-4 "Federal Civilian Division, General Dynamics Information Technology, Atlanta, Georgia, USA."), [Ian A York](https://pubmed.ncbi.nlm.nih.gov/?term=York+IA&cauthor_id=42663462)[ 1 ](https://pubmed.ncbi.nlm.nih.gov/42663462/#short-view-affiliation-1 "Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA.") ### Affiliations * 1 Immunology and Pathogenesis Branch, Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control & Prevention, Atlanta, Georgia, USA. * 2 Division of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control & Prevention, Atlanta, Georgia, USA. * 3 Oak Ridge Institute for Science and Education, Oak Ridge, Tennessee, USA. * 4 Federal Civilian Division, General Dynamics Information Technology, Atlanta, Georgia, USA. * 5 Chippewa Government Solutions, LLC, Sault Sainte Marie, Michigan, USA. * PMID: **42663462** * DOI: [ 10.1128/jvi.00662-26 ](https://doi.org/10.1128/jvi.00662-26) Item in Clipboard Full text links Cite Display options Display options Format Abstract PubMed PMID ## Abstract Glycosylation of the influenza A virus hemagglutinin is crucial for viral fitness and immune evasion. The hemagglutinin of contemporary human A(H3N2) influenza A viruses is extensively glycosylated with up to 13 putative glycosylation sites. Glycan types and occupancy of these sites are not uniform: while most are nearly completely occupied by glycans, some, such as those at amino acid residues 45 and 144, are only partially occupied and are evolutionarily unstable. While the effects of highly occupied glycosylated sites of hemagglutinin on A(H3N2) influenza A virus biology are well studied, there is limited information on the functional impact of the low-occupancy glycosylation sites on the viral hemagglutinin. Here, by using reverse-genetics A(H3N2) influenza A viruses lacking glycans at either residue 45 or 144, or both in hemagglutinin, we demonstrate that, despite reduced receptor binding, thermal stability, and fusion, the presence of a low level of glycosylation at these positions does not impact virus growth in Madin-Darby canine kidney epithelial cell culture. In contrast, these low-occupancy sites do affect immune responses in mice, by reducing titers of antibodies that correlate with virus neutralization and protection against influenza disease. We suggest that the temporary introduction of sites with low glycosylation allows influenza viruses to reduce the immune pressure on antigenic and receptor binding sites of hemagglutinin without significantly compromising viral virulence. This mechanism may help support the sustained circulation of A(H3N2) influenza A virus in human populations. **Importance:** Many of the glycosylation sites on the hemagglutinin of influenza A viruses are near antigenic sites, such that the glycans block antibody recognition and help evade population immunity. However, glycans may also reduce viral replication and virulence. Glycosylation sites at amino acid residues 45 and 144 of the hemagglutinin of contemporary A(H3N2) influenza A viruses are minimally occupied, with fewer than 10% of the sites containing glycans. This is still sufficient to partially evade antibody-based population immunity, while minimizing the impact on replication and virulence. Over time, A(H3N2) viruses have used both these sites only during limited periods, suggesting that even a low level of glycan occupancy may confer some negative selection pressure that is compensated by evasion of human population immunity. Data from this study provide a better understanding of the mechanisms that allow viruses to evade antibody-based immunity and maintain circulation in the human population. **Keywords:** glycosylation; hemagglutinin; immune evasion; influenza; viral evolution. [PubMed Disclaimer](https://pubmed.ncbi.nlm.nih.gov/disclaimer/) ## Conflict of interest statement The authors declare no conflict of interest. ## Similar articles * [ Plasticity of Amino Acid Residue 145 Near the Receptor Binding Site of H3 Swine Influenza A Viruses and Its Impact on Receptor Binding and Antibody Recognition. ](https://pubmed.ncbi.nlm.nih.gov/30355680/) Santos JJS, Abente EJ, Obadan AO, Thompson AJ, Ferreri L, Geiger G, Gonzalez-Reiche AS, Lewis NS, Burke DF, Rajão DS, Paulson JC, Vincent AL, Perez DR.Santos JJS, et al.J Virol. 2019 Jan 4;93(2):e01413-18. doi: 10.1128/JVI.01413-18. Print 2019 Jan 15.J Virol. 2019.PMID: 30355680Free PMC article. * [ N-Linked Glycan Sites on the Influenza A Virus Neuraminidase Head Domain Are Required for Efficient Viral Incorporation and Replication. ](https://pubmed.ncbi.nlm.nih.gov/32699088/) Östbye H, Gao J, Martinez MR, Wang H, de Gier JW, Daniels R.Östbye H, et al.J Virol. 2020 Sep 15;94(19):e00874-20. doi: 10.1128/JVI.00874-20. Print 2020 Sep 15.J Virol. 2020.PMID: 32699088Free PMC article. * [ Human Influenza A
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