ArticleJournal of virology2005
A peptide pertaining to the loop segment of human immunodeficiency virus gp41 binds and interacts with model biomembranes: implications for the fusion mechanism.
Article in Journal of virology, 2005. 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.
- Peptide Triazole Thiol Irreversibly Inactivates Metastable HIV-1 Env by Accessing Conformational Triggers Intrinsic to Virus-Cell Entry.Microorganisms · 2021Article
- Statistical correlation of nonconservative substitutions of HIV gp41 variable amino acid residues with the R5X4 HIV-1 phenotype.Virology journal · 2016Article
- An immunomodulating motif of the HIV-1 fusion protein is chirality-independent: implications for its mode of action.The Journal of biological chemistry · 2013Article
- Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core.The Journal of biological chemistry · 2013Article
- Amphipathic properties of HIV-1 gp41 fusion inhibitors.Current topics in medicinal chemistry · 2011Review
- Biochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor design.Current topics in medicinal chemistry · 2011Review
- Targeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapy.Current topics in medicinal chemistry · 2011Review
- Article
- Interaction of a peptide corresponding to the loop domain of the S2 SARS-CoV virus protein with model membranes.Molecular membrane biology · 2009Article
- Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.Biochemistry · 2009Article
- Membrane insertion of the three main membranotropic sequences from SARS-CoV S2 glycoprotein.Biochimica et biophysica acta · 2008Article
- Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity.Peptides · 2008Article
- Surface exposure of the HIV-1 env cytoplasmic tail LLP2 domain during the membrane fusion process: interaction with gp41 fusion core.The Journal of biological chemistry · 2008Article
- Interaction of the most membranotropic region of the HCV E2 envelope glycoprotein with membranes. Biophysical characterization.Biophysical journal · 2008Article
- Hepatitis C virus core protein binding to lipid membranes: the role of domains 1 and 2.Journal of viral hepatitis · 2008Article
- Peptide mimic of the HIV envelope gp120-gp41 interface.Journal of molecular biology · 2008Article
- Conformational flexibility and strand arrangements of the membrane-associated HIV fusion peptide trimer probed by solid-state NMR spectroscopy.Biochemistry · 2006Article
- Identification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: implications for the viral fusion mechanism.Journal of virology · 2005Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human immunodeficiency virus gp41 envelope protein mediates the entry of the virus into the target cell by promoting membrane fusion. In order to gain new insights into the viral fusion mechanism, we studied a 35-residue peptide pertaining to the loop domain of gp41, both in solution and membrane bound, by using infrared and fluorescence spectroscopy. We show here that the peptide, which has a membrane-interacting surface, binds and interacts with phospholipid model membranes and tends to aggregate in the presence of a membranous medium and induce the leakage of vesicle contents. The results reported in this work, i.e., the destabilization and fusion of negatively charged model membranes, suggest an essential role of the loop domain in the membrane fusion process induced by gp41.
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