ArticleJournal of structural biology2020
Identification of a pH sensor in Influenza hemagglutinin using X-ray crystallography.
Article in Journal of structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Inhibition of Influenza Entry by Organosilicon Compounds.Journal of medical virology · 2025Article
- Visualizing and analyzing 3D biomolecular structures using Mol* at RCSB.org: Influenza A H5N1 virus proteome case study.Protein science : a publication of the Protein Society · 2025Article
- Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch.Nature communications · 2024Article
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift.FEMS microbiology reviews · 2024Review
- Review
- Structural Characterization ofJournal of virology · 2022Article
- Universal stabilization of the influenza hemagglutinin by structure-based redesign of the pH switch regions.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
- pH-Dependent Mechanisms of Influenza Infection Mediated by Hemagglutinin.Frontiers in molecular biosciences · 2021Review
- Structure of avian influenza hemagglutinin in complex with a small molecule entry inhibitor.Life science alliance · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemagglutnin (HA) mediates entry of influenza virus through a series of conformational changes triggered by the low pH of the endosome. The residue or combination of residues acting as pH sensors has not yet been fully elucidated. In this work, we assay pH effects on the structure of H5 HA by soaking HA crystallized at pH 6.5 in a series of buffers with lower pH, mimicking the conditions of the endosome. We find that HA1-H38, which is conserved in Group 1 HA, undergoes a striking change in side chain conformation, which we attribute to its protonation and cation-cation repulsion with conserved HA1-H18. This work suggests that x-ray crystallography can be applied for studying small-scale pH-induced conformational changes providing valuable information on the location of pH sensors in HA. Importantly, the observed change in HA1-H38 conformation is further evidence that the pH-induced conformational changes of HA are the result of a series of protonation events to conserved and non-conserved pH sensors.
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Registered trials
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