ArticleProceedings of the National Academy of Sciences of the United States of America2012
pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- An EGFR-Targeted Fusogenic Tandem Peptide for siRNA Delivery in Glioblastoma.Pharmaceutics · 2026Article
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Implementation of Replica-Averaged Restraints from Nuclear Magnetic Resonance Measurement with UNRES Coarse Grained Model of Polypeptide Chains.Molecules (Basel, Switzerland) · 2025Article
- Resurrection of the Helical Hairpin Hypothesis for Understanding Coronavirus Fusion.The Journal of membrane biology · 2025Review
- Molecular Structure Refinement of a ß-Heptapeptide Based on Residual Dipolar Couplings: The Challenge of Extracting Structural Information from Measured RDCs.The journal of physical chemistry. B · 2025Article
- Implementation of Time-Averaged Restraints with UNRES Coarse-Grained Model of Polypeptide Chains.Journal of chemical theory and computation · 2025Article
- Representing structures of the multiple conformational states of proteins.Current opinion in structural biology · 2023Review
- Viral Membrane Fusion: A Dance Between Proteins and Lipids.Annual review of virology · 2023Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- 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
- Membrane-Bound Configuration and Lipid Perturbing Effects of Hemagglutinin Subunit 2 N-Terminus Investigated by Computer Simulations.Frontiers in molecular biosciences · 2022Article
- Generating Ensembles of Dynamic Misfolding Proteins.Frontiers in neuroscience · 2022Review
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies.FEBS open bio · 2021Review
- Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion.Science advances · 2021Article
- Hemagglutinin Structure and Activities.Cold Spring Harbor perspectives in medicine · 2021Review
- RapidBiochemistry · 2021Article
- Transient Excursions to Membrane Core as Determinants of Influenza Virus Fusion Peptide Activity.International journal of molecular sciences · 2021Article
- Allosteric Mechanisms of Nonadditive Substituent Contributions to Protein-Ligand Binding.Biophysical journal · 2020Article
- Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
4 authors.
Funding
Abstract
The highly conserved first 23 residues of the influenza hemagglutinin HA2 subunit constitute the fusion domain, which plays a pivotal role in fusing viral and host-cell membranes. At neutral pH, this peptide adopts a tight helical hairpin wedge structure, stabilized by aliphatic hydrogen bonding and charge-dipole interactions. We demonstrate that at low pH, where the fusion process is triggered, the native peptide transiently visits activated states that are very similar to those sampled by a G8A mutant. This mutant retains a small fraction of helical hairpin conformation, in rapid equilibrium with at least two open structures. The exchange rate between the closed and open conformations of the wild-type fusion peptide is ~40 kHz, with a total open-state population of ~20%. Transitions to these activated states are likely to play a crucial role in formation of the fusion pore, an essential structure required in the final stage of membrane fusion.
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