ArticleBiophysical journal2015
The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane Structure.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Sulfur-containing class of broad-spectrum antivirals improves influenza virus vaccine development.Nature communications · 2026Article
- Discovery of a novel broad-spectrum inhibitor against influenza virus A.Virology journal · 2025Article
- Novel requirements for HAP2/GCS1-mediated gamete fusion iniScience · 2024Article
- UCST-Type Soluble Immobilized Cellulase: A New Strategy for the Efficient Degradation and Improved Recycling Performance of Wastepaper Cellulose.Molecules (Basel, Switzerland) · 2024Article
- Transmembrane domain of IFITM3 is responsible for its interaction with influenza virus HAVirologica Sinica · 2022Article
- Negatively charged residues in the membrane ordering activity of SARS-CoV-1 and -2 fusion peptides.Biophysical journal · 2022Article
- Critical Negatively Charged Residues Are Important for the Activity of SARS-CoV-1 and SARS-CoV-2 Fusion Peptides.bioRxiv : the preprint server for biology · 2021Article
- Membranotropic and biological activities of the membrane fusion peptides from SARS-CoV spike glycoprotein: The importance of the complete internal fusion peptide domain.Biochimica et biophysica acta. Biomembranes · 2021Article
- Article
- SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on CaJournal of molecular biology · 2021Article
- Membrane tension may define the deadliest virus infection.Colloid and interface science communications · 2021Article
- Influenza A H1 and H3 Transmembrane Domains Interact Differently with Each Other and with Surrounding Membrane Lipids.Viruses · 2020Article
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- Submillisecond Freezing Permits Cryoprotectant-Free EPR Double Electron-Electron Resonance Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- CaJournal of virology · 2020Article
- Parainfluenza virus 5 fusion protein maintains pre-fusion stability but not fusogenic activity following mutation of a transmembrane leucine/isoleucine domain.The Journal of general virology · 2020Article
- Calcium Ions Directly Interact with the Ebola Virus Fusion Peptide To Promote Structure-Function Changes That Enhance Infection.ACS infectious diseases · 2020Article
- SARS-CoV-2, Early Entry Events.Journal of pathogens · 2020Review
- Organometallic Complex Strongly Impairs Chikungunya Virus Entry to the Host Cells.Frontiers in microbiology · 2020Article
- Local ordering and dynamics in anisotropic media by magnetic resonance: from liquid crystals to proteins.Liquid crystals · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Viral glycoproteins, such as influenza hemagglutinin (HA) and human immunodeficiency virus gp41, are anchored by a single helical segment transmembrane domain (TMD) on the viral envelope membrane. The fusion peptides (FP) of the glycoproteins insert into the host membrane and initiate membrane fusion. Our previous study showed that the FP or TMD alone perturbs membrane structure. Interaction between the influenza HA FP and TMD has previously been shown, but its role is unclear. We used PC spin labels dipalmitoylphospatidyl-tempo-choline (on the headgroup), 5PC and 14PC (5-C and 14-C positions on the acyl chain) to detect the combined effect of FP-TMD interaction by titrating HA FP to TMD-reconstituted 1,2-dimyristoyl-sn-glycero-3-phosphocholine/1,2-dimyristoyl-sn-glycero-3-phospho-(1'-rac-glycerol)/cholesterol lipid bilayers using electron spin resonance. We found that the FP-TMD increases the lipid order at all positions, which has a greater lipid ordering effect than the sum of the FP or TMD alone, and this effect reaches deeper into the membranes. Although HA-mediated membrane fusion is pH dependent, this combined effect is observed at both pH 5 and pH 7. In addition to increasing lipid order, multiple components are found for 5PC at increased concentration of FP-TMD, indicating that distinct domains are induced. However, the mutation of Gly1 in the FP and L187 in the TMD eliminates the perturbations, consistent with their fusogenic phenotypes. Electron spin resonance on spin-labeled peptides confirms these observations. We suggest that this interaction may provide a driving force in different stages of membrane fusion: initialization, transition from hemifusion stalk to transmembrane contact, and fusion pore formation.
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