ArticleBiophysical journal2005
Properties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusion.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 70 citations in OpenAlex.
- Hemifusomes and proteolipid nanodroplets: a critical synthesis of an emerging model for endosomal membrane remodeling.Cell communication and signaling : CCS · 2026Review
- Lipid Selectivity of Membrane Action of the Fragments of Fusion Peptides of Marburg and Ebola Viruses.International journal of molecular sciences · 2024Article
- Initiation and evolution of pores formed by influenza fusion peptides probed by lysolipid inclusion.Biophysical journal · 2023Article
- Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration.Nature communications · 2022Article
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- ViralFP: A Web Application of Viral Fusion Proteins.Frontiers in medical technology · 2021Article
- Membrane Composition Modulates Fusion by Altering Membrane Properties and Fusion Peptide Structure.The Journal of membrane biology · 2019Review
- Autophagy: The multi-purpose bridge in viral infections and host cells.Reviews in medical virology · 2018Review
- Membrane remodeling by the M2 amphipathic helix drives influenza virus membrane scission.Scientific reports · 2017Article
- Fusion of Enveloped Viruses in Endosomes.Traffic (Copenhagen, Denmark) · 2016Review
- Assessment of RNA carrier function in peptide amphiphiles derived from the HIV fusion peptide.Peptides · 2016Article
- REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.Biophysical journal · 2014Article
- Wild-type and mutant hemagglutinin fusion peptides alter bilayer structure as well as kinetics and activation thermodynamics of stalk and pore formation differently: mechanistic implications.Biophysical journal · 2013Article
- Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.The journal of physical chemistry. A · 2013Article
- Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational models.PLoS computational biology · 2013Article
- Modulation of prothrombinase assembly and activity by phosphatidylethanolamine.The Journal of biological chemistry · 2011Article
- Hemagglutinin fusion peptide mutants in model membranes: structural properties, membrane physical properties, and PEG-mediated fusion.Biophysical journal · 2011Article
- Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.European biophysics journal : EBJ · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The fusion peptides of HIV and influenza virus are crucial for viral entry into a host cell. We report the membrane-perturbing and structural properties of fusion peptides from the HA fusion protein of influenza virus and the gp41 fusion protein of HIV. Our goals were to determine: 1), how fusion peptides alter structure within the bilayers of fusogenic and nonfusogenic lipid vesicles and 2), how fusion peptide structure is related to the ability to promote fusion. Fluorescent probes revealed that neither peptide had a significant effect on bilayer packing at the water-membrane interface, but both increased acyl chain order in both fusogenic and nonfusogenic vesicles. Both also reduced free volume within the bilayer as indicated by partitioning of a lipophilic fluorophore into membranes. These membrane ordering effects were smaller for the gp41 peptide than for the HA peptide at low peptide/lipid ratio, suggesting that the two peptides assume different structures on membranes. The influenza peptide was predominantly helical, and the gp41 peptide was predominantly antiparallel beta-sheet when membrane bound, however, the depths of penetration of Trps of both peptides into neutral membranes were similar and independent of membrane composition. We previously demonstrated: 1), the abilities of both peptides to promote fusion but not initial intermediate formation during PEG-mediated fusion and 2), the ability of hexadecane to compete with this effect of the fusion peptides. Taken together, our current and past results suggest a hypothesis for a common mechanism by which these two viral fusion peptides promote fusion.
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