ArticleThe Journal of biological chemistry2015
The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- 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
- Integrating Cryo-Electron Microscopy and Molecular Dynamics Simulations to Investigate Membrane Binding of Influenza Virus Fusion Peptides.Journal of the American Chemical Society · 2025Article
- A Salt Bridge and Disulfide Bond within the Lassa Virus Fusion Domain Are Required for the Initiation of Membrane Fusion.ACS omega · 2024Article
- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
- Two modes of fusogenic action for influenza virus fusion peptide.PLoS computational biology · 2023Article
- Article
- Mechanism of Membrane Fusion: Interplay of Lipid and Peptide.The Journal of membrane biology · 2022Review
- IFITM protein regulation and functions: Far beyond the fight against viruses.Frontiers in immunology · 2022Review
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Human respiratory viral infections: Current status and future prospects of nanotechnology-based approaches for prophylaxis and treatment.Life sciences · 2021Review
- Transient Excursions to Membrane Core as Determinants of Influenza Virus Fusion Peptide Activity.International journal of molecular sciences · 2021Article
- Continuum Models of Membrane Fusion: Evolution of the Theory.International journal of molecular sciences · 2020Review
- Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Inhibition of influenza virus activity by the bovine seminal plasma protein PDC-109.European biophysics journal : EBJ · 2019Article
- Super resolution NOESY spectra of proteins.Journal of biomolecular NMR · 2019Article
- FerA is a Membrane-Associating Four-Helix Bundle Domain in the Ferlin Family of Membrane-Fusion Proteins.Scientific reports · 2018Article
- SARS-CoV fusion peptides induce membrane surface ordering and curvature.Scientific reports · 2016Article
- Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis.Journal of the American Chemical Society · 2015Article
- Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Frontiers in molecular biosciences · 2015Article
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3 authors.
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Abstract
The highly conserved N-terminal 23 residues of the hemagglutinin glycoprotein, known as the fusion peptide domain (HAfp23), is vital to the membrane fusion and infection mechanism of the influenza virus. HAfp23 has a helical hairpin structure consisting of two tightly packed amphiphilic helices that rest on the membrane surface. We demonstrate that HAfp23 is a new class of amphipathic helix that functions by leveraging the negative curvature induced by two tightly packed helices on membranes. The helical hairpin structure has an inverted wedge shape characteristic of negative curvature lipids, with a bulky hydrophobic region and a relatively small hydrophilic head region. The F3G mutation reduces this inverted wedge shape by reducing the volume of its hydrophobic base. We show that despite maintaining identical backbone structures and dynamics as the wild type HAfp23, the F3G mutant has an attenuated fusion activity that is correlated to its reduced ability to induce negative membrane curvature. The inverted wedge shape of HAfp23 is likely to play a crucial role in the initial stages of membrane fusion by stabilizing negative curvature in the fusion stalk.
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