ArticleVirology2014
The roles of hemagglutinin Phe-95 in receptor binding and pathogenicity of influenza B virus.
Article in Virology, 2014. 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.
- Retooling a novel influenza B hemagglutinin to redirect neutralizing antibodies against B/Victoria strains.Vaccine · 2026Article
- N-glycosylation at the receptor binding site drives differences in receptor binding specificity between influenza B virus lineages.Journal of virology · 2025Article
- Engineering a cleaved, prefusion-stabilized influenza B virus hemagglutinin by identification and locking of all six pH switches.PNAS nexus · 2024Article
- Review
- Natural History of Influenza B Virus-Current Knowledge on Treatment, Resistance and Therapeutic Options.Current issues in molecular biology · 2023Review
- Existing Evidence for Influenza B Virus Adaptations to Drive Replication in Humans as the Primary Host.Viruses · 2023Review
- Elimination of receptor binding by influenza hemagglutinin improves vaccine-induced immunity.NPJ vaccines · 2022Article
- Functionality of the putative surface glycoproteins of the Wuhan spiny eel influenza virus.Nature communications · 2021Article
- Review
- Article
- Host Receptors of Influenza Viruses and Coronaviruses-Molecular Mechanisms of Recognition.Vaccines · 2020Review
- Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The structural variability of the influenza A hemagglutinin receptor-binding site.Briefings in functional genomics · 2018Review
- Conformations of the type-1 lacto-N-biose I unit in protein complex structures.Acta crystallographica. Section F, Structural biology communications · 2018Review
- Article
- Rules of co-occurring mutations characterize the antigenic evolution of human influenza A/H3N2, A/H1N1 and B viruses.BMC medical genomics · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Diverged ~4000 years ago, influenza B virus has several important differences from influenza A virus, including lower receptor-binding affinity and highly restricted host range. Based on our prior structural studies, we hypothesized that a single-residue difference in the receptor-binding site of hemagglutinin (HA), Phe-95 in influenza B virus versus Tyr-98 in influenza A/H1-H15, is possibly a key determinant for the low receptor-binding affinity. Here we demonstrate that the mutation Phe95→Tyr in influenza B virus HA restores all three hydrogen bonds made by Tyr-98 in influenza A/H1-15 HA and has the potential to enhance receptor binding. However, the full realization of this potential is influenced by the local environment into which the mutation is introduced. The binding and replication of the recombinant viruses correlate well with the receptor-binding capabilities of HA. These results are discussed in relation to the roles of Phe-95 in receptor binding and pathogenicity of influenza B virus.
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