ArticlePloS one2016
Glycosylation of Residue 141 of Subtype H7 Influenza A Hemagglutinin (HA) Affects HA-Pseudovirus Infectivity and Sensitivity to Site A Neutralizing Antibodies.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 22 citations in OpenAlex.
- Neutralizing and protective monoclonal antibodies identify antigenic sites in influenza H7 hemagglutinin and select for amino acid substitutions rarely observed at the global level.Microbiology spectrum · 2026Article
- Marked neurotropism and potential adaptation of H5N1 clade 2.3.4.4.b virus in naturally infected domestic cats.Emerging microbes & infections · 2025Article
- Mammalian adaptation and zoonotic risk of influenza A viruses in companion animals.Journal of veterinary science · 2025Review
- Pan-H7 influenza human antibody virus neutralization depends on avidity and steric hindrance.JCI insight · 2025Article
- A synthetic TLR4 agonist significantly increases humoral immune responses and the protective ability of an MDCK-cell-derived inactivated H7N9 vaccine in mice.Archives of virology · 2024Article
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift.FEMS microbiology reviews · 2024Review
- Antigenic Characterization of Human Monoclonal Antibodies for Therapeutic Use against H7N9 Avian Influenza Virus.Journal of virology · 2023Article
- Hemagglutination Inhibition (HAI) antibody landscapes after vaccination with H7Nx virus like particles.PloS one · 2021Article
- Glycosylation generates an efficacious and immunogenic vaccine against H7N9 influenza virus.PLoS biology · 2020Article
- Immune Escape Adaptive Mutations in the H7N9 Avian Influenza Hemagglutinin Protein Increase Virus Replication Fitness and Decrease Pandemic Potential.Journal of virology · 2020Article
- Loss of Fitness of Mexican H7N3 Highly Pathogenic Avian Influenza Virus in Mallards after Circulating in Chickens.Journal of virology · 2019Article
- Characterization of Mouse Monoclonal Antibodies Against the HA of A(H7N9) Influenza Virus.Viruses · 2019Article
- Amino Acid Residue 217 in the Hemagglutinin Glycoprotein Is a Key Mediator of Avian Influenza H7N9 Virus Antigenicity.Journal of virology · 2019Article
- Article
- Conformational Stability of the Hemagglutinin of H5N1 Influenza A Viruses Influences Susceptibility to Broadly Neutralizing Stem Antibodies.Journal of virology · 2018Article
- The S128N mutation combined with an additional potential N-linked glycosylation site at residue 133 in hemagglutinin affects the antigenicity of the human H7N9 virus.Emerging microbes & infections · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human infections with H7 subtype influenza virus have been reported, including an H7N7 outbreak in Netherlands in 2003 and H7N9 infections in China in 2013. Previously, we reported murine monoclonal antibodies (mAbs) that recognize the antigenic site A of H7 hemagglutinin (HA). To better understand protective immunity of H7 vaccines and vaccine candidate selection, we used these mAbs to assess the antigenic relatedness among two H7 HA isolated from past human infections and determine residues that affect susceptibility to neutralization. We found that these mAbs neutralize pseudoviruses bearing HA of A/Shanghai/02/2013(H7N9), but not A/Netherlands/219/2003(H7N7). Glycosylation of the asparagine residue at position 141 (N141) (N133, H3 HA numbering) in the HA of A/Netherlands/219/2003 HA is responsible for this resistance, and it affects the infectivity of HA-pseudoviruses. The presence of threonine at position 143 (T135, H3 HA numbering) in the HA of A/Netherlands/219/2003, rather than an alanine found in the HA of A/Shanghai/02/2013(H7N9), accounts for these differences. These results demonstrate a key role for glycosylation of residue N141 in affecting H7 influenza HA-mediated entry and sensitivity to neutralizing antibodies, which have implications for candidate vaccine design.
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