ArticleJournal of the American Chemical Society2014
Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 47 citations in OpenAlex.
- Phosphatidylinositol Interactions with the SARS-CoV-2 Envelope Protein Investigated by LipidBiochemistry · 2026Article
- The Interplay of Lipids and Peptides in Membrane Merger.Advances in experimental medicine and biology · 2026Review
- Microscopic insight into HIV fusion peptide-mediated dehydration and packing regulation in membranes.Biophysical journal · 2025Article
- Unravelling the role of key amino acid residues of the parainfluenza fusion peptide in membrane fusion.RSC chemical biology · 2025Article
- Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections.FEBS open bio · 2025Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Membrane-induced tau amyloid fibrils.Communications biology · 2023Article
- Unraveling Membrane Perturbations Caused by the Bacterial Riboregulator Hfq.International journal of molecular sciences · 2022Article
- Parainfluenza Fusion Peptide Promotes Membrane Fusion by Assembling into Oligomeric Porelike Structures.ACS chemical biology · 2022Article
- Mechanism of Membrane Fusion: Interplay of Lipid and Peptide.The Journal of membrane biology · 2022Review
- Membranotropic and biological activities of the membrane fusion peptides from SARS-CoV spike glycoprotein: The importance of the complete internal fusion peptide domain.Biochimica et biophysica acta. Biomembranes · 2021Article
- Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes fromBiochimica et biophysica acta. Biomembranes · 2021Article
- RapidBiochemistry · 2021Article
- SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on CaJournal of molecular biology · 2021Article
- Parainfluenza virus entry at the onset of infection.Advances in virus research · 2021Article
- Article
- Mechanistic insights of host cell fusion of SARS-CoV-1 and SARS-CoV-2 from atomic resolution structure and membrane dynamics.Biophysical chemistry · 2020Review
- Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.Journal of molecular biology · 2020Article
- Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers.The Journal of biological chemistry · 2019Article
- Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR.Journal of structural biology · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Viral fusion proteins catalyze the merger of the virus envelope and the target cell membrane through multiple steps of protein conformational changes. The fusion peptide domain of these proteins is important for membrane fusion, but how it causes membrane curvature and dehydration is still poorly understood. We now use solid-state NMR spectroscopy to investigate the conformation, topology, and lipid and water interactions of the fusion peptide of the PIV5 virus F protein in three lipid membranes, POPC/POPG, DOPC/DOPG, and DOPE. These membranes allow us to investigate the effects of lipid chain disorder, membrane surface charge, and intrinsic negative curvature on the fusion peptide structure. Chemical shifts and spin diffusion data indicate that the PIV5 fusion peptide is inserted into all three membranes but adopts distinct conformations: it is fully α-helical in the POPC/POPG membrane, adopts a mixed strand/helix conformation in the DOPC/DOPG membrane, and is primarily a β-strand in the DOPE membrane. (31)P NMR spectra show that the peptide retains the lamellar structure and hydration of the two anionic membranes. However, it dehydrates the DOPE membrane, destabilizes its inverted hexagonal phase, and creates an isotropic phase that is most likely a cubic phase. The ability of the β-strand conformation of the fusion peptide to generate negative Gaussian curvature and to dehydrate the membrane may be important for the formation of hemifusion intermediates in the membrane fusion pathway.
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