ArticleThe EMBO journal2002
Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- An In Vitro Screen Identifies H1 Influenza Hemagglutinin Substitutions That Alter mRNA-LNP Vaccine Responses Against the Stalk Domain.Vaccines · 2026Article
- Stimulus-Responsive Polymeric Carriers for Gene Delivery: Balancing Endosomal Escape with Nucleic Acid Release.Pharmaceutical research · 2026Review
- Mechanistic insights into the small-molecule inhibition of influenza A virus entry.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Influenza A virus RNA localisation and the interceding trafficking pathways of the host cell.PLoS pathogens · 2025Review
- Article
- The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023Article
- Restriction of Influenza A Virus by SERINC5.mBio · 2022Article
- Reversible structural changes in the influenza hemagglutinin precursor at membrane fusion pH.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Stability of HA2 Prefusion Structure and pH-Induced Conformational Changes in the HA2 Domain of H3N2 Hemagglutinin.Biochemistry · 2021Article
- Review
- Review
- pH-Dependent Mechanisms of Influenza Infection Mediated by Hemagglutinin.Frontiers in molecular biosciences · 2021Review
- Structural intermediates in the low pH-induced transition of influenza hemagglutinin.PLoS pathogens · 2020Article
- Structural monitoring of a transient intermediate in the hemagglutinin fusion machinery on influenza virions.Science advances · 2020Article
- Review
- Identification of a pH sensor in Influenza hemagglutinin using X-ray crystallography.Journal of structural biology · 2020Article
- Influenza Hemagglutinin and Neuraminidase: Yin⁻Yang Proteins Coevolving to Thwart Immunity.Viruses · 2019Review
- Developments in single-molecule and single-particle fluorescence-based approaches for studying viral envelope glycoprotein dynamics and membrane fusion.Advances in virus research · 2019Article
- Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers.Cell · 2018Article
- pH regulation in early endosomes and interferon-inducible transmembrane proteins control avian retrovirus fusion.The Journal of biological chemistry · 2017Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The refolding of the prototypic fusogenic protein hemagglutinin (HA) at the pH of fusion is considered to be a concerted and irreversible discharge of a loaded spring, with no distinct intermediates between the initial and final conformations. Here, we show that HA refolding involves reversible conformations with a lifetime of minutes. After reneutralization, low pH-activated HA returns from the conformations wherein both the fusion peptide and the kinked loop of the HA2 subunit are exposed, but the HA1 subunits have not yet dissociated, to a structure indistinguishable from the initial one in functional, biochemical and immunological characteristics. The rate of the transition from reversible conformations to irreversible refolding depends on the pH and on the presence of target membrane. Importantly, recovery of the initial conformation is blocked by the interactions between adjacent HA trimers. The existence of the identified reversible stage of refolding can be crucial for allowing multiple copies of HA to synchronize their release of conformational energy, as required for fusion.
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