ArticleProceedings of the National Academy of Sciences of the United States of America2009
Changes in H5N1 influenza virus hemagglutinin receptor binding domain affect systemic spread.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 109 citations in OpenAlex.
- H5N1 clade 2.3.2.1e lineage transition in Lao PDR during 2023-2024 associated with regional spread and human infection risk-associated receptor-binding features.Frontiers in public health · 2026Article
- Divergent Avian Influenza H10 Viruses from Sympatric Waterbird Species in Italy: Zoonotic Potential Assessment by Molecular Markers.Microorganisms · 2025Article
- Emerging Highly Pathogenic Avian Influenza H5N1 Clade 2.3.4.4b Causes Neurological Disease and Mortality in Scavenging Ducks in Bangladesh.Veterinary sciences · 2025Article
- BIK polymorphism and proteasome regulation unveil host risk factor for severe influenza.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mammalian adaptation risk in HPAI H5N8: a comprehensive model bridging experimental data with mathematical insights.Emerging microbes & infections · 2024Article
- Examining the Influenza A Virus Sialic Acid Binding Preference Predictions of a Sequence-Based Convolutional Neural Network.Influenza and other respiratory viruses · 2024Article
- Continued Circulation of Highly Pathogenic H5 Influenza Viruses in Vietnamese Live Bird Markets in 2018-2021.Viruses · 2023Article
- Phylodynamics and Molecular Mutations of the Hemagglutinin Affecting Global Transmission and Host Adaptation of H5Nx Viruses.Transboundary and emerging diseases · 2023Article
- Article
- Emergence of a Novel Reassortant H5N3 Avian Influenza Virus in Korean Mallard Ducks in 2018.Intervirology · 2022Article
- Neurovirulence of avian influenza virus is dependent on the interaction of viral NP protein with host factor FMRP in the murine brain.Journal of virology · 2021Article
- 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.Veterinary research · 2021Article
- Quantifying within-host diversity of H5N1 influenza viruses in humans and poultry in Cambodia.PLoS pathogens · 2020Article
- Inventory of molecular markers affecting biological characteristics of avian influenza A viruses.Virus genes · 2019Review
- Phylogeny, Pathogenicity, Transmission, and Host Immune Responses of Four H5N6 Avian Influenza Viruses in Chickens and Mice.Viruses · 2019Article
- Orally Efficacious Broad-Spectrum Ribonucleoside Analog Inhibitor of Influenza and Respiratory Syncytial Viruses.Antimicrobial agents and chemotherapy · 2018Article
- Unlocking pandemic potential: prevalence and spatial patterns of key substitutions in avian influenza H5N1 in Egyptian isolates.BMC infectious diseases · 2018Article
- Glycosylation of the Hemagglutinin Protein of H5N1 Influenza Virus Increases Its Virulence in Mice by Exacerbating the Host Immune Response.Journal of virology · 2017Article
- The ecology and adaptive evolution of influenza A interspecies transmission.Influenza and other respiratory viruses · 2017Review
- Highly Pathogenic Avian Influenza H5N6 Viruses Exhibit Enhanced Affinity for Human Type Sialic Acid Receptor and In-Contact Transmission in Model Ferrets.Journal of virology · 2016Article
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Authors and funding
14 authors at 1 institution in 1 country.
Funding
Abstract
The HA of influenza virus is a receptor-binding and fusion protein that is required to initiate infection. The HA receptor-binding domain determines the species of sialyl receptors recognized by influenza viruses. Here, we demonstrate that changes in the HA receptor-binding domain alter the ability of the H5N1 virus to spread systemically in mice. The A/Vietnam/1203/04 (VN1203) and A/Hong Kong/213/03 (HK213) viruses are consistently lethal to domestic chickens but differ in their pathogenicity to mammals. Insertion of the VN1203 HA and neuraminidase (NA) genes into recombinant HK213 virus expanded its tissue tropism and increased its lethality in mice; conversely, insertion of HK213 HA and NA genes into recombinant VN1203 virus decreased its systemic spread and lethality. The VN1203 and HK213 HAs differ by 10 aa, and HK213 HA has shown greater binding affinity for synthetic alpha2,6-linked sialyl receptor. Introduction of an S227N change and removal of N-linked glycosylation at residue 158 increased the alpha2,6-binding affinity of VN1203 HA. Recombinant VN1203 virus carrying the S227N change alone or with the residue-158 glycosylation site removed showed reduced lethality and systemic spread in mice but not in domestic chickens. Wild-type VN1203 virus exhibited the greatest efficiency in systemic spread after intramuscular inoculation and in infection of mouse bone marrow-derived dendritic cells and conventional pulmonary dendritic cells. These results show that VN1203 HA glycoprotein confers pathogenicity by facilitating systemic spread in mice; they also suggest that a minor change in receptor binding domain may modulate the virulence of H5N1 viruses.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.