ArticleLangmuir : the ACS journal of surfaces and colloids2016
Influenza M2 Transmembrane Domain Senses Membrane Heterogeneity and Enhances Membrane Curvature.
Article in Langmuir : the ACS journal of surfaces and colloids, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Viruses · 2026Article
- The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025Article
- Comparing Multifunctional Viral and Eukaryotic Proteins for Generating Scission Necks in Membranes.ACS nano · 2024Article
- The vaccinia chondroitin sulfate binding protein drives host membrane curvature to facilitate fusion.EMBO reports · 2024Article
- Probing the interactions of the HIV-1 matrix protein-derived polybasic region with lipid bilayers: insights from AFM imaging and force spectroscopy.European biophysics journal : EBJ · 2024Article
- Cholesterol and M2 Rendezvous in Budding and Scission of Influenza A Virus.Sub-cellular biochemistry · 2023Article
- Determining Cholesterol Binding to Membrane Proteins by CholesterolJournal of the American Chemical Society · 2018Article
- Entropic forces drive clustering and spatial localization of influenza A M2 during viral budding.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Membrane Disruption Mechanism of a Prion Peptide (106-126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy.The journal of physical chemistry. B · 2017Article
- Lateral Organization of Influenza Virus Proteins in the Budozone Region of the Plasma Membrane.Journal of virology · 2017Article
- Modulation of lipid membrane structural and mechanical properties by a peptidomimetic derived from reduced amide scaffold.Biochimica et biophysica acta. Biomembranes · 2017Article
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Authors and funding
5 authors.
Funding
Abstract
Targeting host cell membranes by M2 of influenza A virus is important for virus invasion and replication. We study the transmembrane domain of M2 (M2TM) interacting with mica-supported planar bilayers and free-standing giant unilamellar vesicles (GUVs). Using solution atomic force microscopy (AFM), we show that the size of M2TM oligomers is dependent on lipid composition. The addition of M2TM to lipid bilayers containing liquid-ordered (Lo) and liquid-disordered (Ld) phases reveals that M2TM preferentially partitions into the Ld phase; phase-dependent partitioning results in a larger rigidity of the Ld phase. We next use fluorescence microscopy to study the effects of M2TM on phase-coexisting GUVs. In particular, M2TM is found to increase GUVs' miscibility transition temperature Tmix. The augmented thermodynamic stability can be accounted for by considering an enhanced energy barrier of lipid mixing between coexisting phases. Our GUV study also shows that M2TM can elicit an array of vesicle shapes mimicking virus budding. M2TM enhanced membrane curvature is consistent with our AFM data, which show altered membrane rigidity and consequently line tension at domain edges. Together, our results highlight that in addition to conducting protons, M2TM can actively regulate membrane heterogeneity and augment membrane curvature.
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