ArticleArchives of virology2016
Amino acid residues at positions 222 and 227 of the hemagglutinin together with the neuraminidase determine binding of H5 avian influenza viruses to sialyl Lewis X.
Article in Archives of virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 70 citations in OpenAlex.
- Hemagglutinin double-mutation enhances binding of human-infecting avian influenza virus clade 2.3.4.4b H5Ny to human and SLeEMBO reports · 2026Article
- Distribution of influenza A virus receptors in tissues of South American marine wildlife.Veterinary research communications · 2026Article
- Length and density of α2-3 sialyllactose-containing chains on glycopolymers determine receptor binding of avian influenza viruses.Archives of virology · 2026Article
- Evolution, spread and impact of highly pathogenic H5 avian influenza A viruses.Nature reviews. Microbiology · 2026Review
- The receptor binding properties of H5Ny influenza A viruses have evolved to bind to avian-type mucin-like O-glycans.PLoS pathogens · 2026Article
- Chemoenzymatic Synthesis of Asymmetric Bisecting Bi-, Tri-, and Tetra-AntennaryJournal of the American Chemical Society · 2025Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.bioRxiv : the preprint server for biology · 2025Article
- The sweet side of H5N1 influenza virus infection.PLoS pathogens · 2025Article
- The mammary glands of cows abundantly display receptors for circulating avian H5 viruses.Journal of virology · 2024Article
- Multivalent interactions between fully glycosylated influenza virus hemagglutinins mediated by glycans at distinct N-glycosylation sites.Npj viruses · 2024Article
- Receptor Binding Specificity of a Bovine A(H5N1) Influenza Virus.bioRxiv : the preprint server for biology · 2024Article
- Chemoenzymatic Synthesis of Tri-antennary N-Glycans Terminating in Sialyl-LewisChemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift.FEMS microbiology reviews · 2024Review
- ComplexJournal of virology · 2024Article
- The Sialyl Lewis X Glycan Receptor Facilitates Infection of Subtype H7 Avian Influenza A Viruses.Journal of virology · 2022Article
- Article
- Pathobiology of highly pathogenic H5 avian influenza viruses in naturally infected Galliformes and Anseriformes in France during winter 2015-2016.Veterinary research · 2022Article
- Structural analysis of N-glycans in chicken trachea and lung reveals potential receptors of chicken influenza viruses.Scientific reports · 2022Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Influenza viruses isolated from ducks are rarely able to infect chickens; it is therefore postulated that these viruses need to adapt in some way to be able to be transmitted to chickens in nature. Previous studies revealed that sialyl Lewis X (3'SLeX), which is fucosylated α2,3 sialoside, was predominantly detected on the epithelial cells of the chicken trachea, whereas this glycan structure is not found in the duck intestinal tract. To clarify the mechanisms of the interspecies transmission of influenza viruses between ducks and chickens, we compared the receptor specificity of low-pathogenic avian influenza viruses isolated from these two species. Glycan-binding analysis of the recombinant hemagglutinin (HA) of a chicken influenza virus, A/chicken/Ibaraki/1/2005 (H5N2), revealed a binding preference to α1,3 fucosylated sialosides. On the other hand, the HA of a duck influenza virus, A/duck/Mongolia/54/2001 (H5N2) (Dk/MNG), particularly bound to non-fucosylated α2,3 sialosides such as 3'-sialyllactosamine (3'SLacNAc). Computational analysis along with binding analysis of the mutant HAs revealed that this glycan-binding specificity of the HA was determined by amino acid residues at positions 222 and 227. Inconsistent with the glycan-binding specificity of the recombinant HA protein, virions of Dk/MNG bound to both 3'SLacNAc and 3'SLeX. Glycan-binding analysis in the presence of a neuraminidase (NA) inhibitor revealed that the NA conferred binding to 3'SLeX to virions of Dk/MNG. The present results reveal the molecular basis of the interaction between fucosylated α2,3 sialosides and influenza viruses.
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