ArticleBiophysical journal2012
NMR determination of protein partitioning into membrane domains with different curvatures and application to the influenza M2 peptide.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025Article
- Cholesterol and M2 Rendezvous in Budding and Scission of Influenza A Virus.Sub-cellular biochemistry · 2023Article
- Article
- Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes fromBiochimica et biophysica acta. Biomembranes · 2021Article
- Biomolecular complex viewed by dynamic nuclear polarization solid-state NMR spectroscopy.Biochemical Society transactions · 2020Review
- Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism.Nature structural & molecular biology · 2020Article
- Origin and Evolution of H1N1/pdm2009: A Codon Usage Perspective.Frontiers in microbiology · 2020Article
- Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR.Journal of structural biology · 2019Article
- Integrated solid-state NMR and molecular dynamics modeling determines membrane insertion of human β-defensin analog.Communications biology · 2019Article
- 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
- Structure and Dynamics of Membrane Proteins from Solid-State NMR.Annual review of biophysics · 2018Review
- Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR.Journal of the American Chemical Society · 2018Article
- Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Geodesic curvature driven surface microdomain formation.Journal of computational physics · 2017Article
- Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.Journal of molecular biology · 2017Article
- MASBiophysical journal · 2016Article
- Protein-lipid interactions critical to replication of the influenza A virus.FEBS letters · 2016Review
- Distinct Membrane Disruption Pathways Are Induced by 40-Residue β-Amyloid Peptides.The Journal of biological chemistry · 2016Article
- Spherical nanoparticle supported lipid bilayers for the structural study of membrane geometry-sensitive molecules.Journal of the American Chemical Society · 2015Article
- Structural Changes and Proapoptotic Peroxidase Activity of Cardiolipin-Bound Mitochondrial Cytochrome c.Biophysical journal · 2015Article
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3 authors.
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Abstract
The M2 protein of the influenza A virus acts both as a drug-sensitive proton channel and mediates virus budding through membrane scission. The segment responsible for causing membrane curvature is an amphipathic helix in the cytoplasmic domain of the protein. Here, we use (31)P and (13)C solid-state NMR to examine M2-induced membrane curvature. M2(22-46), which includes only the transmembrane (TM) helix, and M2(21-61), which contains an additional amphipathic helix, are studied. (31)P chemical shift lineshapes indicate that M2(21-61) causes a high-curvature isotropic phase to both cholesterol-rich virus-mimetic membranes and 1,2-dimyristoyl-sn-glycero-3-phosphocholine bilayers, whereas M2(22-46) has minimal effect. The lamellar and isotropic domains have distinct (31)P isotropic chemical shifts, indicating perturbation of the lipid headgroup conformation by the amphipathic helix. (31)P- and (13)C-detected (1)H T(2) relaxation and two-dimensional peptide-lipid correlation spectra show that M2(21-61) preferentially binds to the high-curvature domain. (31)P linewidths indicate that the isotropic vesicles induced by M2(21-61) are 10-35 nm in diameter, and the virus-mimetic vesicles are smaller than the 1,2-dimyristoyl-sn-glycero-3-phosphocholine vesicles. A strong correlation is found between high membrane curvature and weak drug-binding ability of the TM helix. Thus, the M2 amphipathic helix causes membrane curvature, which in turn perturbs the TM helix conformation, abolishing drug binding. These NMR experiments are applicable to other curvature-inducing membrane proteins such as fusion proteins and antimicrobial peptides.
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