ArticleBiophysical journal2004
Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- 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
- Peptide-based delivery of therapeutics in cancer treatment.Materials today. Bio · 2022Review
- Conformational plasticity underlies membrane fusion induced by an HIV sequence juxtaposed to the lipid envelope.Scientific reports · 2021Article
- Article
- Review
- Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.Biochemistry · 2018Article
- Identification of the Fusion Peptide-Containing Region in Betacoronavirus Spike Glycoproteins.Journal of virology · 2016Article
- 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
- Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state.Journal of molecular biology · 2014Article
- 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
- Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMR.Journal of molecular biology · 2013Article
- Computer-Aided Approaches for Targeting HIVgp41.Biology · 2012Article
- HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion.European biophysics journal : EBJ · 2011Article
- Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide.Biochemistry · 2010Article
- Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations.Journal of molecular biology · 2010Article
- Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide.Biochimica et biophysica acta · 2010Article
- Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation.Biochemistry · 2009Article
- Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.Biochemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The human immunodeficiency virus type 1 (HIV-1) fusion peptide serves as a useful model system for understanding viral/target cell fusion, at least to the lipid mixing stage. Previous solid-state NMR studies have shown that the peptide adopts an oligomeric beta-strand structure when associated with a lipid and cholesterol mixture close to that of membranes of host cells of the virus. In this study, this structure was further investigated using four different peptide constructs. In aqueous buffer solution, two of the constructs were primarily monomeric whereas the other two constructs had significant populations of oligomers/aggregates. NMR measurements for all membrane-associated peptide constructs were consistent with oligomeric beta-strand structure. Thus, constructs that are monomeric in solution can be converted to oligomers as a result of membrane association. In addition, samples prepared by very different methods had very similar NMR spectra, which indicates that the beta-strand structure is an equilibrium rather than a kinetically trapped structure. Lipid mixing assays were performed to assess the fusogenicities of the different constructs, and there was not a linear correlation between the solution oligomeric state and fusogenicity. However, the functional assays do suggest that small oligomers may be more fusogenic than either monomers or large aggregates.
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