ArticleScientific reports2018
Unravelling the Role of O-glycans in Influenza A Virus Infection.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 1,240 citations in OpenAlex.
- The receptor landscape of influenza A viruses.Journal of virology · 2026Review
- Genetic variation and vaccine match of influenza B virus in Riyadh, Saudi Arabia during three consecutive seasons, 2020-2023.Virus genes · 2026Article
- Molecular Surveillance, Evolution, and Vaccine Strain Match of theInternational journal of molecular sciences · 2026Article
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Cell-based sialoglycan arrays for directly comparing influenza A virus receptor requirements for binding and infection.iScience · 2025Article
- Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy.Glycobiology · 2024Review
- Membrane attachment and fusion of HIV-1, influenza A, and SARS-CoV-2: resolving the mechanisms with biophysical methods.Biophysical reviews · 2022Review
- Article
- Influenza Virus Infections in Polarized Cells.Viruses · 2022Review
- Article
- The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021Review
- Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Top-Down Mass Spectrometry.Journal of the American Chemical Society · 2021Article
- Conserved Sequence Analysis of Influenza A Virus HA Segment and Its Application in Rapid Typing.Diagnostics (Basel, Switzerland) · 2021Article
- Chemoenzymatic modular assembly of O-GalNAc glycans for functional glycomics.Nature communications · 2021Article
- Adhesion ofFrontiers in molecular biosciences · 2021Review
- O-Glycosylation Landscapes of SARS-CoV-2 Spike Proteins.Frontiers in chemistry · 2021Article
- Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020Review
- MDCK-B4GalNT2 cells disclose a α2,3-sialic acid requirement for the 2009 pandemic H1N1 A/California/04/2009 and NA aid entry of A/WSN/33.Emerging microbes & infections · 2019Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The initial stage of host cell infection by influenza A viruses (IAV) is mediated through interaction of the viral haemagglutinin (HA) with cell surface glycans. The binding requirement of IAVs for Galβ(1,4)Glc/ GlcNAc (lactose/lactosamine) glycans with a terminal α(2,6)-linked (human receptors) or α(2,3)-linked (avian receptors) N-acetylneuraminic residue commonly found on N-glycans, is well-established. However the role and significance of sialylated Galβ(1,3)GalNAc (core 1) epitopes that are typical O-glycoforms in influenza virus pathogenesis remains poorly detailed. Here we report a multidisciplinary study using NMR spectroscopy, virus neutralization assays and molecular modelling, into the potential for IAV to engage sialyl-Galβ(1,3)GalNAc O-glycoforms for cell attachment. H5 containing virus like particles (VLPs) derived from an H5N1 avian IAV strain show a significant involvement of the O-glycan-specific GalNAc residue, coordinated by a EQTKLY motif conserved in highly pathogenic avian influenza (HPAI) strains. Notably, human pandemic H1N1 influenza viruses shift the preference from 'human-like' α(2,6)-linkages in sialylated Galβ(1,4)Glc/GlcNAc fragments to 'avian-like' α(2,3)-linkages in sialylated Galβ(1,3)GalNAc without involvement of the GalNAc residue. Overall, our study suggests that sialylated Galβ(1,3)GalNAc as O-glycan core 1 glycoforms are involved in the influenza A virus life cycle and play a particularly crucial role during infection of HPAI strains.
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