ArticleVeterinary research2017
Glycosylation at 11Asn on hemagglutinin of H5N1 influenza virus contributes to its biological characteristics.
Article in Veterinary research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 16 citations in OpenAlex.
- 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
- Structure-Guided Glycosylation of Hemagglutinin Enhances Stability and Modulates Immunogenicity of Influenza Vaccines.Vaccines · 2026Article
- Avian Influenza Virus: Comparative Evolution as the Key for Predicting Host Tropism Expansion.Pathogens (Basel, Switzerland) · 2025Article
- Hemagglutinin glycosylation pattern-specific effects: implications for the fitness of H9.4.2.5-branched H9N2 avian influenza viruses.Emerging microbes & infections · 2024Article
- Avian Influenza Virus Tropism in Humans.Viruses · 2023Review
- N-linked glycosylation enhances hemagglutinin stability in avian H5N6 influenza virus to promote adaptation in mammals.PNAS nexus · 2022Article
- Emerging of H5N6 Subtype Influenza Virus with 129-Glycosylation Site on Hemagglutinin in Poultry in China Acquires Immune Pressure Adaption.Microbiology spectrum · 2022Article
- A Single Vaccination of Chimeric Bivalent Virus-Like Particle Vaccine Confers Protection Against H9N2 and H3N2 Avian Influenza in Commercial Broilers and Allows a Strategy of Differentiating Infected from Vaccinated Animals.Frontiers in immunology · 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
- The role of glycosylation in the N-terminus of the hemagglutinin of a unique H4N2 with a natural polybasic cleavage site in virus fitnessVirulence · 2021Article
- Analysis of the avian coronavirus spike protein reveals heterogeneity in the glycans present.The Journal of general virology · 2021Article
- Human Influenza A Virus Hemagglutinin Glycan Evolution Follows a Temporal Pattern to a Glycan Limit.mBio · 2019Article
- Differences in the ease with which mutant viruses escape from human monoclonal antibodies against the HA stem of influenza A virus.Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology · 2018Article
- Recurring and Adaptable Binding Motifs in Broadly Neutralizing Antibodies to Influenza Virus Are Encoded on the D3-9 Segment of the Ig Gene.Cell host & microbe · 2018Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A stem glycosylation site of hemagglutinin (HA) is important to the stability of the HA trimmer. A previous study shows that the stem 10/11 overlap glycosylation site of the H5 subtype avian influenza virus may influence the cleavage of HA, whereas the exact site and its effect on virulence remain unclear. In this study, site-directed mutagenesis was used to generate single or double mutant rSY-Δ10(10NNAT), rSY-Δ11(10NNSA), and rSY-Δ10/11(10NNAA) of the overlapping glycosylation site (10NNST) on the HA of A/Mallard/Huadong/S/2005(SY). By using Western blot analysis, we show that both rSY-Δ11 and rSY-Δ10/11 mutant viruses had significant delay on HA cleavage and a reduced HA molecular mass compared to the wild-type virus rSY, while the rSY-Δ10 mutant virus exhibited a similar HA molecular mass to that of the wild-type virus rSY. Interestingly, both rSY-Δ11 and rSY-Δ10/11 mutant viruses reverted their glycosylation sites at 11N after passage, indicating that 11N is a true and critical glycosylation site. Compared to the wild-type virus rSY, rSY-Δ11 and rSY-Δ10/11 mutant viruses had decreased growth rates, reduced thermo- and pH-stability, decreased pathogenicity, and limited systemic spread. Therefore, our study suggests that the 11N glycosylation site plays a key role in HA cleavage, structural stability and pathogenicity in H5 subtype avian influenza virus.
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