ArticleJournal of virology2009
Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 109 citations in OpenAlex.
- In silico analysis of pH stabilising mutations of hemagglutinin of influenza A virus H5N1 clade 2.3.4.4b.Npj viruses · 2026Review
- An In Vitro Screen Identifies H1 Influenza Hemagglutinin Substitutions That Alter mRNA-LNP Vaccine Responses Against the Stalk Domain.Vaccines · 2026Article
- Identification of thermostability-enhancing mutations in H9N2 avian influenza virus hemagglutinin.Journal of virology · 2026Article
- Zooming into Disease at the Nanoscale: High-Speed Atomic Force Microscopy in Biomedical Discovery.ACS nano · 2026Review
- Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus.Viruses · 2025Article
- Host switching mutations in H5N1 influenza hemagglutinin suppress site-specific activation dynamics.Nature communications · 2025Article
- Divergent Avian Influenza H10 Viruses from Sympatric Waterbird Species in Italy: Zoonotic Potential Assessment by Molecular Markers.Microorganisms · 2025Article
- Host Switching Mutations in H5N1 Influenza Hemagglutinin Suppress Site-specific Activation Dynamics.bioRxiv : the preprint server for biology · 2025Article
- Molecular Dynamics Investigation of the Influenza Hemagglutinin Conformational Changes in Acidic pH.The journal of physical chemistry. B · 2024Article
- The host tropism of current zoonotic H7N9 viruses depends mainly on an acid-labile hemagglutinin with a single amino acid mutation in the stalk region.PLoS pathogens · 2024Article
- Article
- Rapid evolution of A(H5N1) influenza viruses after intercontinental spread to North America.Nature communications · 2023Article
- Article
- Swine H1N1 Influenza Virus Variants with Enhanced Polymerase Activity and HA Stability Promote Airborne Transmission in Ferrets.Journal of virology · 2022Article
- Characterization of changes in the hemagglutinin that accompanied the emergence of H3N2/1968 pandemic influenza viruses.PLoS pathogens · 2021Article
- Relationship between hemagglutinin stability and influenza virus persistence after exposure to low pH or supraphysiological heating.PLoS pathogens · 2021Article
- Review
- pH-Dependent Mechanisms of Influenza Infection Mediated by Hemagglutinin.Frontiers in molecular biosciences · 2021Review
- Genetic and antigenic characterization of influenza A/H5N1 viruses isolated from patients in Indonesia, 2008-2015.Virus genes · 2020Article
- Characterizing Emerging Canine H3 Influenza Viruses.PLoS pathogens · 2020Article
17 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The receptor specificity and cleavability of the hemagglutinin (HA) protein have been shown to regulate influenza A virus transmissibility and pathogenicity, but little is known about how its pH of activation contributes to these important biological properties. To identify amino acid residues that regulate the acid stability of the HA protein of H5N1 influenza viruses, we performed a mutational analysis of the HA protein of the moderately pathogenic A/chicken/Vietnam/C58/04 (H5N1) virus. Nineteen HA proteins containing point mutations in the HA2 coiled-coil domain or in an HA1 histidine or basic patch were generated. Wild-type and mutant HA plasmids were transiently transfected in cell culture and analyzed for total protein expression, surface expression, cleavage efficiency, pH of fusion, and pH of conformational change. Four mutations to residues in the fusion peptide pocket, Y23H and H24Q in the HA1 subunit and E105K and N114K in the HA2 subunit, and a K58I mutation in the HA2 coiled-coil domain significantly altered the pH of activation of the H5 HA protein. In some cases, the magnitude and direction of changes of individual mutations in the H5 HA protein differed considerably from similar mutations in other influenza A virus HA subtypes. Introduction of Y23H, H24Q, K58I, and N114K mutations into recombinant viruses resulted in virus-expressed HA proteins with similar shifts in the pH of fusion. Overall, the data show that residues comprising the fusion peptide pocket are important in triggering pH-dependent activation of the H5 HA protein.
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