ArticleBMC biology2008
Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex.
Article in BMC biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 71 citations in OpenAlex.
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Probing the role of membrane in neutralizing activity of antibodies against influenza virus.Structure (London, England : 1993) · 2026Article
- Lysosome-escaping and nucleus-targeting nanomedicine for enhanced cancer catalytic internal radiotherapy.European journal of nuclear medicine and molecular imaging · 2025Article
- Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding.Protein science : a publication of the Protein Society · 2024Article
- Purification and characterization of the Lassa virus transmembrane domain.Biochemistry and biophysics reports · 2023Article
- The interaction of viral fusion peptides with lipid membranes.Biophysical journal · 2022Article
- Transmembrane domain of IFITM3 is responsible for its interaction with influenza virus HAVirologica Sinica · 2022Article
- Temporal and Gene Reassortment Analysis of Influenza C Virus Outbreaks in Hong Kong, SAR, China.Journal of virology · 2022Article
- Hydrophobic Mismatch Controls the Mode of Membrane-Mediated Interactions of Transmembrane Peptides.Membranes · 2022Article
- Stability of HA2 Prefusion Structure and pH-Induced Conformational Changes in the HA2 Domain of H3N2 Hemagglutinin.Biochemistry · 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
- Disulfide isomerase ERp57 improves the stability and immunogenicity of H3N2 influenza virus hemagglutinin.Virology journal · 2020Article
- Article
- Vesicular stomatitis virus G protein transmembrane region is crucial for the hemi-fusion to full fusion transition.Scientific reports · 2018Article
- Recombinant influenza H9N2 virus with a substitution of H3 hemagglutinin transmembrane domain showed enhanced immunogenicity in mice and chicken.Scientific reports · 2017Article
- Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Identification of the Fusion Peptide-Containing Region in Betacoronavirus Spike Glycoproteins.Journal of virology · 2016Article
- Fusion of Enveloped Viruses in Endosomes.Traffic (Copenhagen, Denmark) · 2016Review
- The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane Structure.Biophysical journal · 2015Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTo study the organization and interaction with the fusion domain (or fusion peptide, FP) of the transmembrane domain (TMD) of influenza virus envelope glycoprotein for its role in membrane fusion which is also essential in the cellular trafficking of biomolecules and sperm-egg fusion.
resultsThe fluorescence and gel electrophoresis experiments revealed a tight self-assembly of TMD in the model membrane. A weak but non-random interaction between TMD and FP in the membrane was found. In the complex, the central TMD oligomer was packed by FP in an antiparallel fashion. FP insertion into the membrane was altered by binding to TMD. An infrared study exhibited an enhanced membrane perturbation by the complex formation. A model was built to illustrate the role of TMD in the late stages of influenza virus-mediated membrane fusion reaction.
conclusionThe TMD oligomer anchors the fusion protein in the membrane with minimal destabilization to the membrane. Upon associating with FP, the complex exerts a synergistic effect on the membrane perturbation. This effect is likely to contribute to the complete membrane fusion during the late phase of fusion protein-induced fusion cascade. The results presented in the work characterize the nature of the interaction of TMD with the membrane and TMD in a complex with FP in the steps leading to pore initiation and dilation during virus-induced fusion. Our data and proposed fusion model highlight the key role of TMD-FP interaction and have implications on the fusion reaction mediated by other type I viral fusion proteins. Understanding the molecular mechanism of membrane fusion may assist in the design of anti-viral drugs.
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