ArticleEuropean biophysics journal : EBJ2011
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.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- Multistate Method to Efficiently Account for Tautomerism and Protonation in Alchemical Free-Energy Calculations.Journal of chemical theory and computation · 2024Article
- Article
- Insights into the mechanism of membrane fusion induced by the plant defense element, plant-specific insert.The Journal of biological chemistry · 2020Article
- Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers.The Journal of biological chemistry · 2019Article
- HIV-1 gp41 transmembrane oligomerization monitored by FRET and FCS.FEBS letters · 2018Article
- Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.Biochemistry · 2018Article
- Article
- Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide make significant contributions to fusion of membrane vesicles.Protein expression and purification · 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
- Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding.Journal of biomolecular NMR · 2015Article
- Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.Biochemistry · 2015Article
- 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
- Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Protonation and pK changes in protein-ligand binding.Quarterly reviews of biophysics · 2013Review
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The HIV gp41 protein catalyzes fusion between HIV and target cell membranes. The fusion states of the gp41 ectodomain include early coiled-coil (CC) structure and final six-helix bundle (SHB) structure. The ectodomain has an additional N-terminal apolar fusion peptide (FP) sequence which binds to target cell membranes and plays a critical role in fusion. One approach to understanding gp41 function is study of vesicle fusion induced by constructs that encompass various regions of gp41. There are apparent conflicting literature reports of either rapid or no fusion of negatively charged vesicles by SHB constructs. These reports motivated the present study, which particularly focused on effects of pH because the earlier high and no fusion results were at pH 3.0 and 7.2, respectively. Constructs include "Hairpin," which has SHB structure but lacks the FP, "FP-Hairpin" with FP + SHB, and "N70," which contains the FP and part of the CC but does not have SHB structure. Aqueous solubility, membrane binding, and vesicle fusion function were measured at a series of pHs and much of the pH dependences of these properties were explained by protein charge. At pH 3.5, all constructs were positively charged, bound negatively charged vesicles, and induced rapid fusion. At pH 7.0, N70 remained positively charged and induced rapid fusion, whereas Hairpin and FP-Hairpin were negatively charged and induced no fusion. Because viral entry occurs near pH 7 rather than pH 3, our results are consistent with fusogenic function of early CC gp41 and with fusion arrest by final SHB gp41.
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