ArticleJournal of molecular biology2013
Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMR.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Phosphatidylinositol Interactions with the SARS-CoV-2 Envelope Protein Investigated by LipidBiochemistry · 2026Article
- Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections.FEBS open bio · 2025Review
- Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement.Biophysical chemistry · 2023Article
- Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes fromBiochimica et biophysica acta. Biomembranes · 2021Article
- Parainfluenza virus entry at the onset of infection.Advances in virus research · 2021Article
- Parainfluenza virus 5 fusion protein maintains pre-fusion stability but not fusogenic activity following mutation of a transmembrane leucine/isoleucine domain.The Journal of general virology · 2020Article
- Article
- Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers.The Journal of biological chemistry · 2019Article
- Article
- Integrated solid-state NMR and molecular dynamics modeling determines membrane insertion of human β-defensin analog.Communications biology · 2019Article
- Machine learning antimicrobial peptide sequences: Some surprising variations on the theme of amphiphilic assembly.Current opinion in colloid & interface science · 2018Article
- Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 Membrane-Proximal External Region and Transmembrane Domain in Phospholipid Bilayers.Journal of the American Chemical Society · 2018Article
- Structure and Dynamics of Membrane Proteins from Solid-State NMR.Annual review of biophysics · 2018Review
- Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.Journal of molecular biology · 2018Article
- Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.Scientific reports · 2017Article
- Structure and interaction with lipid membrane models of Semliki Forest virus fusion peptide.Biochimica et biophysica acta · 2016Article
- Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis.Journal of the American Chemical Society · 2015Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- pH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.Biochimica et biophysica acta · 2015Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The entry of enveloped viruses into cells requires protein-catalyzed fusion of the viral and cell membranes. The structure-function relation of a hydrophobic fusion peptide (FP) in viral fusion proteins is still poorly understood. We report magic-angle-spinning solid-state NMR results of the membrane-bound conformation, dynamics, and lipid interactions of the FP of the F protein of the paramyxovirus, parainfluenza virus 5 (PIV5). (13)C chemical shifts indicate that the PIV5 FP structure depends on the composition of the phospholipid membrane: the peptide is α-helical in palmitoyloleoylphosphatidylglycerol-containing anionic membranes but mostly β-sheet in neutral phosphocholine membranes. Other environmental factors, including peptide concentration, cholesterol, membrane reconstitution protocol, and a Lys solubility tag, do not affect the secondary structure. The α-helical and β-sheet states exhibit distinct dynamics and lipid interactions. The β-sheet FP is immobilized, resides on the membrane surface, and causes significant membrane curvature. In contrast, the α-helical FP undergoes intermediate-timescale motion and maintains the lamellar order of the membrane. Two-dimensional (31)P-(1)H correlation spectra show clear (31)P-water cross peaks for anionic membranes containing the α-helical FP but weak or no (31)P-water cross peak for neutral membranes containing the β-sheet FP. These results suggest that the β-sheet FP may be associated with high-curvature dehydrated fusion intermediates, while the α-helical state may be associated with the extended prehairpin state and the post-fusion state. Conformational plasticity is also a pronounced feature of the influenza and human immunodeficiency virus FPs, suggesting that these Gly-rich sequences encode structural plasticity to generate and sense different membrane morphologies.
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