ArticleProceedings of the National Academy of Sciences of the United States of America2010
The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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Who cites it
114 citing papers in PubMed.
- Pre-existing and cross-reactive immunity to avian influenza H5N1 in humans: Implications for pandemic risk and vaccine strategies.The Journal of infection · 2026Review
- The microprotein Dafcin resembles influenza HA fusion peptide and regulates the size of storage lysosomes in the germline.bioRxiv : the preprint server for biology · 2026Article
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Resurrection of the Helical Hairpin Hypothesis for Understanding Coronavirus Fusion.The Journal of membrane biology · 2025Review
- Integrating Cryo-Electron Microscopy and Molecular Dynamics Simulations to Investigate Membrane Binding of Influenza Virus Fusion Peptides.Journal of the American Chemical Society · 2025Article
- Effects of a Polarizable Force Field on Membrane Dynamics: Surface Viscosity, Lipid Diffusion, and Peptide Induced Pore Formation.Journal of computational chemistry · 2025Article
- Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections.FEBS open bio · 2025Review
- Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infection.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular Dynamics Investigation of the Influenza Hemagglutinin Conformational Changes in Acidic pH.The journal of physical chemistry. B · 2024Article
- Spontaneous curvature generation by peptides in asymmetric bilayers.Journal of computational chemistry · 2024Article
- Review
- Molecular Mechanisms behind Conformational Transitions of the Influenza Virus Hemagglutinin Membrane Anchor.The journal of physical chemistry. B · 2023Article
- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Article
- Two modes of fusogenic action for influenza virus fusion peptide.PLoS computational biology · 2023Article
- Initiation and evolution of pores formed by influenza fusion peptides probed by lysolipid inclusion.Biophysical journal · 2023Article
- Article
- Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration.Nature communications · 2022Article
- The interaction of viral fusion peptides with lipid membranes.Biophysical journal · 2022Article
54 more citing papers are in PubMed but not listed here.
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3 authors.
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Abstract
All but five of the N-terminal 23 residues of the HA2 domain of the influenza virus glycoprotein hemagglutinin (HA) are strictly conserved across all 16 serotypes of HA genes. The structure and function of this HA2 fusion peptide (HAfp) continues to be the focus of extensive biophysical, computational, and functional analysis, but most of these analyses are of peptides that do not include the strictly conserved residues Trp(21)-Tyr(22)-Gly(23). The heteronuclear triple resonance NMR study reported here of full length HAfp of sero subtype H1, solubilized in dodecylphosphatidyl choline, reveals a remarkably tight helical hairpin structure, with its N-terminal alpha-helix (Gly(1)-Gly(12)) packed tightly against its second alpha-helix (Trp(14)-Gly(23)), with six of the seven conserved Gly residues at the interhelical interface. The seventh conserved Gly residue in position 13 adopts a positive angle, enabling the hairpin turn that links the two helices. The structure is stabilized by multiple interhelical C(alpha)H to C=O hydrogen bonds, characterized by strong interhelical H(N)-H(alpha) and H(alpha)-H(alpha) NOE contacts. Many of the previously identified mutations that make HA2 nonfusogenic are also incompatible with the tight antiparallel hairpin arrangement of the HAfp helices.(15)N relaxation analysis indicates the structure to be highly ordered on the nanosecond time scale, and NOE analysis indicates HAfp is located at the water-lipid interface, with its hydrophobic surface facing the lipid environment, and the Gly-rich side of the helix-helix interface exposed to solvent.
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