ArticleEmerging microbes & infections2017
Variability in H9N2 haemagglutinin receptor-binding preference and the pH of fusion.
Article in Emerging microbes & infections, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.
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Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.
- The molecular basis of antigenic variation among A(H9N2) avian influenza viruses.Emerging microbes & infections · 2018Pooled it
- Dominant HA motif 131/132-NT shapes the phenotype of avian H9N2 influenza virus by modulating agglutination property, receptor specificity and infectivity in animals.Virologica Sinica · 2026Article
- The haemagglutinin gene of bovine-origin H5N1 influenza viruses currently retains receptor-binding and pH-fusion characteristics of avian host phenotype.Emerging microbes & infections · 2025Article
- PB2 627V and HA 217 sites synergistically affect the lethality of H9N2 in mice.Virologica Sinica · 2025Article
- Dissecting the role of the HA1-226 leucine residue in the fitness and airborne transmission of an A(H9N2) avian influenza virus.Journal of virology · 2024Article
- Exploring Potential Intermediates in the Cross-Species Transmission of Influenza A Virus to Humans.Viruses · 2024Review
- Recent H9N2 avian influenza virus lost hemagglutination activity due to a K141N substitution in hemagglutinin.Journal of virology · 2024Article
- Article
- Diversity of genotypes and pathogenicity of H9N2 avian influenza virus derived from wild bird and domestic poultry.Frontiers in microbiology · 2024Article
- Characterization of the haemagglutinin properties of the H5N1 avian influenza virus that caused human infections in Cambodia.Emerging microbes & infections · 2023Article
- Antigenic Characterization of Human Monoclonal Antibodies for Therapeutic Use against H7N9 Avian Influenza Virus.Journal of virology · 2023Article
- Evolutionary pressures rendered by animal husbandry practices for avian influenza viruses to adapt to humans.iScience · 2022Review
- Applications of Surface Plasmon Resonance and Biolayer Interferometry for Virus-Ligand Binding.Viruses · 2022Review
- Avian Influenza a H9N2 Viruses in Morocco, 2018-2019.Viruses · 2022Article
- Article
- The PB1 gene from H9N2 avian influenza virus showed high compatibility and increased mutation rate after reassorting with a human H1N1 influenza virus.Virology journal · 2022Article
- Quantification of Receptor Association, Dissociation, and NA-Dependent Motility of Influenza A Particles by Biolayer Interferometry.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Assessing the effects of a two-amino acid flexibility in the Hemagglutinin 220-loop receptor-binding domain on the fitness of Influenza A(H9N2) viruses.Emerging microbes & infections · 2021Article
- Molecular epidemiology and pathogenicity of H5N1 and H9N2 avian influenza viruses in clinically affected chickens on farms in Bangladesh.Emerging microbes & infections · 2021Article
- Amino acid substitutions in the H5N1 avian influenza haemagglutinin alter pH of fusion and receptor binding to promote a highly pathogenic phenotype in chickens.The Journal of general virology · 2021Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
H9N2 avian influenza viruses are primarily a disease of poultry; however, they occasionally infect humans and are considered a potential pandemic threat. Little work has been performed to assess the intrinsic biochemical properties related to zoonotic potential of H9N2 viruses. The objective of this study, therefore, was to investigate H9N2 haemagglutinins (HAs) using two well-known correlates for human adaption: receptor-binding avidity and pH of fusion. Receptor binding was characterized using bio-layer interferometry to measure virus binding to human and avian-like receptor analogues and the pH of fusion was assayed by syncytium formation in virus-infected cells at different pHs. We characterized contemporary H9N2 viruses of the zoonotic G1 lineage, as well as representative viruses of the zoonotic BJ94 lineage. We found that most contemporary H9N2 viruses show a preference for sulphated avian-like receptor analogues. However, the 'Eastern' G1 H9N2 viruses displayed a consistent preference in binding to a human-like receptor analogue. We demonstrate that the presence of leucine at position 226 of the HA receptor-binding site correlated poorly with the ability to bind a human-like sialic acid receptor. H9N2 HAs also display variability in their pH of fusion, ranging between pH 5.4 and 5.85 which is similar to that of the first wave of human H1N1pdm09 viruses but lower than the pH of fusion seen in zoonotic H5N1 and H7N9 viruses. Our results suggest possible molecular mechanisms that may underlie the relatively high prevalence of human zoonotic infection by particular H9N2 virus lineages.
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