ArticleScientific reports2017
Membrane remodeling by the M2 amphipathic helix drives influenza virus membrane scission.
Article in Scientific reports, 2017. 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.
- Roles of the M2 protein of influenza A virus.Virus genes · 2026Review
- Molecular mechanism of CtBP1-S/BARS-driven membrane fission and its cellular control by metabolic ligands.Science advances · 2026Article
- Natural and evolved membrane-associated accessory proteins differentially engage SNARE machinery for AAV egress.Journal of virology · 2026Article
- Amphipathic helical peptide-Nile red probes for fluorescence probing of the lipid packing defects and their surrounding membranes on exosomes.Scientific reports · 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
- Influenza A virus RNA localisation and the interceding trafficking pathways of the host cell.PLoS pathogens · 2025Review
- Viral Membrane-Targeting Amphipathic Helical Peptide-Based Fluorogenic Probes for the Analysis of Infectious Titers of Enveloped Viruses.Analytical chemistry · 2025Article
- The Role of Cholesterol in M2 Clustering and Viral Budding Explained.Journal of chemical theory and computation · 2025Article
- SARS-CoV-2 Assembly: Gaining Infectivity and Beyond.Viruses · 2024Review
- Membrane Activity and Viroporin Assembly for the SARS-CoV-2 E Protein Are Regulated by Cholesterol.Biomolecules · 2024Article
- Conformations of influenza A M2 protein in DOPC/DOPS and E. coli native lipids and proteins.Biophysical journal · 2024Article
- Membrane curvature sensing and symmetry breaking of the M2 proton channel from Influenza A.eLife · 2024Article
- A comparative study of influenza A M2 protein conformations in DOPC/DOPS liposomes and in nativebioRxiv : the preprint server for biology · 2024Article
- The role of an amphiphilic helix and transmembrane region in the efficient acylation of the M2 protein from influenza virus.Scientific reports · 2023Article
- SARS-CoV-2 E protein: Pathogenesis and potential therapeutic development.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023Review
- Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cholesterol and M2 Rendezvous in Budding and Scission of Influenza A Virus.Sub-cellular biochemistry · 2023Article
- Generation of nanoscopic membrane curvature for membrane trafficking.Nature reviews. Molecular cell biology · 2023Review
- Strength in numbers: effect of protein crowding on the shape of cell membranes.Biochemical Society transactions · 2022Review
- Structural and functional role of Domain I for the insecticidal activity of the Vip3Aa protein from Bacillus thuringiensis.Microbial biotechnology · 2022Article
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6 authors.
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Abstract
Membrane scission is a crucial step in all budding processes, from endocytosis to viral budding. Many proteins have been associated with scission, though the underlying molecular details of how scission is accomplished often remain unknown. Here, we investigate the process of M2-mediated membrane scission during the budding of influenza viruses. Residues 50-61 of the viral M2 protein bind membrane and form an amphipathic α-helix (AH). Membrane binding requires hydrophobic interactions with the lipid tails but not charged interactions with the lipid headgroups. Upon binding, the M2AH induces membrane curvature and lipid ordering, constricting and destabilizing the membrane neck, causing scission. We further show that AHs in the cellular proteins Arf1 and Epsin1 behave in a similar manner. Together, they represent a class of membrane-induced AH domains that alter membrane curvature and fluidity, mediating the scission of constricted membrane necks in multiple biological pathways.
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