ArticleVeterinary research2021
N-linked glycosylation at site 158 of the HA protein of H5N6 highly pathogenic avian influenza virus is important for viral biological properties and host immune responses.
Article in Veterinary research, 2021. 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.
- Article
- Post-translational modification networks as master regulators of influenza virus replication, host adaptation, and immune evasion.Frontiers in immunology · 2026Review
- Genetic characterization of highly pathogenic avian influenza A/H5N8 virus isolated from commercial poultry farms in Egypt reveals zoonotic potential.Archives of virology · 2025Article
- Therapeutic Targeting of Viral N-Glycosylation Modification: From Molecular Mechanisms to Clinical Application Prospects.Infectious diseases and therapy · 2025Review
- Article
- Epidemiological, phylogenetic, and pathogenicity analysis of H4 subtype avian influenza viruses in China, 2011-2022.Virologica Sinica · 2025Article
- Applications of virus-like particles in the prevention of protozoan parasite infection.Nanomedicine (London, England) · 2025Review
- Molecular Evolution of Influenza A Viruses From Mauritius, 2017-2019.Influenza and other respiratory viruses · 2025Article
- Effects of the Glycosylation of the HA Protein of H9N2 Subtype Avian Influenza Virus on the Pathogenicity in Mice and Antigenicity.Transboundary and emerging diseases · 2024Article
- A sequence-based machine learning model for predicting antigenic distance for H3N2 influenza virus.Frontiers in microbiology · 2024Article
- Article
- Article
- Phylodynamics and Molecular Mutations of the Hemagglutinin Affecting Global Transmission and Host Adaptation of H5Nx Viruses.Transboundary and emerging diseases · 2023Article
- Genetic characterization and pathogenicity of a Eurasian avian-like H1N1 swine influenza reassortant virus.Virology journal · 2022Article
- Rational engineering of adeno-associated virus capsid enhances human hepatocyte tropism and reduces immunogenicity.Cell proliferation · 2022Article
- Evidence for Different Virulence Determinants and Host Response after Infection of Turkeys and Chickens with Highly Pathogenic H7N1 Avian Influenza Virus.Journal of virology · 2022Article
- The Unique Glycosylation at Position 986 on the E2 Glycoprotein of Classical Swine Fever Virus Is Responsible for Viral Attenuation and Protection against Lethal Challenge.Journal of virology · 2022Article
- Identification of Hemagglutinin Mutations Caused by Neuraminidase Antibody Pressure.Microbiology spectrum · 2021Article
- Emergence of a young case infected with avian influenza A (H5N6) in Anhui Province, East China during the COVID-19 pandemic.Journal of medical virology · 2021Article
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13 authors.
Funding
Abstract
Since 2014, clade 2.3.4.4 has become the dominant epidemic branch of the Asian lineage H5 subtype highly pathogenic avian influenza virus (HPAIV) in southern and eastern China, while the H5N6 subtype is the most prevalent. We have shown earlier that lack of glycosylation at position 158 of the hemagglutinin (HA) glycoprotein due to the T160A mutation is a key determinant of the dual receptor binding property of clade 2.3.4.4 H5NX subtypes. Our present study aims to explore other effects of this site among H5N6 viruses. Here we report that N-linked glycosylation at site 158 facilitated the assembly of virus-like particles and enhanced virus replication in A549, MDCK, and chicken embryonic fibroblast (CEF) cells. Consistently, the HA-glycosylated H5N6 virus induced higher levels of inflammatory factors and resulted in stronger pathogenicity in mice than the virus without glycosylation at site 158. However, H5N6 viruses without glycosylation at site 158 were more resistant to heat and bound host cells better than the HA-glycosylated viruses. H5N6 virus without glycosylation at this site triggered the host immune response mechanism to antagonize the viral infection, making viral pathogenicity milder and favoring virus spread. These findings highlight the importance of glycosylation at site 158 of HA for the pathogenicity of the H5N6 viruses.
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