ArticleProceedings of the National Academy of Sciences of the United States of America2009
A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 110 citations in OpenAlex.
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Investigating the Design of ssPalmO-Derived Lipid Nanoparticles for mRNA Delivery Applications Using Molecular Dynamics Simulations.ACS omega · 2025Article
- Exploring the influence of anionic lipids in the host cell membrane on viral fusion.Biochemical Society transactions · 2024Review
- Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infection.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Lipid Selectivity of Membrane Action of the Fragments of Fusion Peptides of Marburg and Ebola Viruses.International journal of molecular sciences · 2024Article
- Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing.International journal of molecular sciences · 2023Review
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Article
- Physico-Chemical Mechanisms of the Functioning of Membrane-Active Proteins of Enveloped Viruses.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022Article
- Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021Review
- Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope.Scientific reports · 2021Article
- Insights into the mechanism of membrane fusion induced by the plant defense element, plant-specific insert.The Journal of biological chemistry · 2020Article
- 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
- Ectodomain Pulling Combines with Fusion Peptide Inserting to Provide Cooperative Fusion for Influenza Virus and HIV.International journal of molecular sciences · 2020Article
- Continuum Models of Membrane Fusion: Evolution of the Theory.International journal of molecular sciences · 2020Review
- Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers.The Journal of biological chemistry · 2019Article
- Membrane Composition Modulates Fusion by Altering Membrane Properties and Fusion Peptide Structure.The Journal of membrane biology · 2019Review
- Integrated solid-state NMR and molecular dynamics modeling determines membrane insertion of human β-defensin analog.Communications biology · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Fusion between the membrane of HIV and the membrane of a host cell is a crucial step in HIV infection and is catalyzed by the binding of the fusion peptide domain (HFP) of the HIV gp41 protein to the host cell membrane. The HFP by itself induces vesicle fusion and is a useful model system to understand the fusion peptide/host cell membrane interaction. This article reports an experimental correlation between the membrane locations of different HFP constructs and their fusogenicities. The constructs were the HFP monomer with Val-2 to Glu-2 mutation (HFPmn_mut), wild type HFP monomer (HFPmn), and wild type HFP trimer (HFPtr). All constructs have predominant beta sheet structure in membranes with physiologically relevant cholesterol content. HFPmn_mut does not fuse vesicles, HFPmn has moderate fusion rate, and HFPtr has the putative oligomerization state of HIV gp41 and a very rapid fusion rate. The HFP membrane locations were probed with solid-state NMR measurements of distances between labeled carbonyl ((13)CO) nuclei in the HFP backbone and lipid nuclei in the surface or interior regions of the membrane bilayer. HFPmn_mut is located at the membrane surface, HFPmn is inserted into a single membrane leaflet, and HFPtr is the most deeply inserted construct with contact with the center of the membrane. These results show a clear positive correlation between the insertion depths and the fusion activities of the HFP constructs. Other disease-causing enveloped viruses contain fusion peptides and this correlation may be a general structure-function model for these peptides.
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