ArticleScientific reports2015
Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- A New Model for the Transmembrane Heterocomplex of Hemagglutinin HA and Ionic Channel M2 Proteins in Influenza A Virus.Doklady. Biochemistry and biophysics · 2026Article
- CW ESR spectroscopy and protein spin labeling in membrane biology.Physical biology · 2025Review
- Q-Band Double Quantum Coherence ESR for Sensitive Nitroxide-Based Distance Measurements.The journal of physical chemistry. B · 2025Article
- Flavoproteins as native and genetically encoded spin probes for in cell ESR spectroscopy.Nature communications · 2025Article
- Highly versatile small virus-encoded proteins in cellular membranes: A structural perspective on how proteins' inherent conformational plasticity couples with host membranes' properties to control cellular processes.Journal of structural biology: X · 2025Article
- Molecular biophysics and inhibition mechanism of influenza virus A M2 viroporin by adamantane-based drugs - Challenges in designing antiviral agents.Journal of structural biology: X · 2025Article
- Conformations of influenza A M2 protein in DOPC/DOPS and E. coli native lipids and proteins.Biophysical journal · 2024Article
- Review
- Differences in Oligomerization of the SARS-CoV-2 Envelope Protein, Poliovirus VP4, and HIV Vpu.Biochemistry · 2024Article
- A comparative study of influenza A M2 protein conformations in DOPC/DOPS liposomes and in nativebioRxiv : the preprint server for biology · 2024Article
- Influenza A Virus Infection Alters Lipid Packing and Surface Electrostatic Potential of the Host Plasma Membrane.Viruses · 2023Article
- Differences in Oligomerization of the SARS-CoV-2 Envelope Protein, Poliovirus VP4, and HIV Vpu.bioRxiv : the preprint server for biology · 2023Article
- A structure and knowledge-based combinatorial approach to engineering universal scFv antibodies against influenza M2 protein.Journal of biomedical science · 2023Article
- Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation.Nature communications · 2023Article
- Conformation of influenza AM2 membrane protein in nanodiscs and liposomes.Biochimica et biophysica acta. Biomembranes · 2023Article
- Insights into the oligomeric structure of the HIV-1 Vpu protein.Journal of structural biology · 2023Article
- Influenza A M2 recruits M1 to the plasma membrane: A fluorescence fluctuation microscopy study.Biophysical journal · 2021Article
- Vectorial insertion of a β-helical peptide into membrane: a theoretical study on polytheonamide B.Biophysical journal · 2021Article
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
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Authors and funding
4 authors.
Funding
Abstract
M2 from influenza A virus functions as an oligomeric proton channel essential for the viral cycle, hence it is a high-priority pharmacological target whose structure and functions require better understanding. We studied the mechanism of M2 transmembrane domain (M2TMD) assembly in lipid membranes by the powerful biophysical technique of double electron-electron resonance (DEER) spectroscopy. By varying the M2TMD-to-lipid molar ratio over a wide range from 1:18,800 to 1:160, we found that M2TMD exists as monomers, dimers, and tetramers whose relative populations shift to tetramers with the increase of peptide-to-lipid (P/L) molar ratio. Our results strongly support the tandem mechanism of M2 assembly that is monomers-to-dimer then dimers-to-tetramer, since tight dimers are abundant at small P/L's, and thereafter they assemble as dimers of dimers in weaker tetramers. The stepwise mechanism found for a single-pass membrane protein oligomeric assembly should contribute to the knowledge of the association steps in membrane protein folding.
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