ArticleBiochemistry2005
Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 59 citations in OpenAlex.
- HIV-Induced Apoptosis: Host Defense and Viral Strategy.Biology · 2025Review
- Profiling HIV1-host protein-protein interaction networks in patient-derived exosome proteins: impact on pathophysiology and innate immune pathways.Virology journal · 2025Article
- Computational epitope mapping of class I fusion proteins using low complexity supervised learning methods.PLoS computational biology · 2022Article
- Molecular mechanism of HIV-1 resistance to sifuvirtide, a clinical trial-approved membrane fusion inhibitor.The Journal of biological chemistry · 2018Article
- Article
- Structure-activity relationship studies of indole-based compounds as small molecule HIV-1 fusion inhibitors targeting glycoprotein 41.Journal of medicinal chemistry · 2014Article
- Immunization with hybrid proteins containing the membrane proximal external region of HIV-1.AIDS research and human retroviruses · 2014Article
- Molecular architecture of the uncleaved HIV-1 envelope glycoprotein trimer.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Anti-tumor and anti-viral activities of Galanthus nivalis agglutinin (GNA)-related lectins.Glycoconjugate journal · 2013Review
- Designing a soluble near full-length HIV-1 gp41 trimer.The Journal of biological chemistry · 2013Article
- Sub-inhibitory concentrations of human α-defensin potentiate neutralizing antibodies against HIV-1 gp41 pre-hairpin intermediates in the presence of serum.PLoS pathogens · 2013Article
- HIV entry and envelope glycoprotein-mediated fusion.The Journal of biological chemistry · 2012Review
- The M-T hook structure is critical for design of HIV-1 fusion inhibitors.The Journal of biological chemistry · 2012Article
- Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer.Nature structural & molecular biology · 2012Article
- HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.Biochemistry · 2012Article
- Targeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapy.Current topics in medicinal chemistry · 2011Review
- Maturation-induced cloaking of neutralization epitopes on HIV-1 particles.PLoS pathogens · 2011Article
- A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascade.Journal of virology · 2010Article
- Fab crystallization and preliminary X-ray analysis of NC-1, an anti-HIV-1 antibody that recognizes the six-helix bundle core of gp41.Acta crystallographica. Section F, Structural biology and crystallization communications · 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
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
HIV-1 envelope glycoprotein-mediated fusion is driven by the concerted coalescence of the HIV-1 gp41 N- and C-helical regions, which results in the formation of 6-helix bundles. These two regions are considered prime targets for peptides and antibodies that inhibit HIV-1 entry. However, the parameters that govern this inhibition have yet to be elucidated. We address this issue by monitoring the temporal sequence of conformational states of HIV-1 gp41 during the course of HIV-1-mediated cell-cell fusion by quantitative video microscopy using reagents that bind to N- and C-helical regions, respectively. Env-expressing cells were primed by incubation with target cells at different times at 37 degrees C followed by washing. The reactivity of triggered gp41 to the NC-1 monoclonal antibody, which we demonstrate here to bind to N-helical gp41 trimers, increased rapidly to a maximal level in the primed state but decreased once stable fusion junctions had formed. In contrast, reactivity with 5-helix, which binds to the C-helical region of gp41, increased continuously as a function of time following the priming. The peptide N36(Mut(e,g)) reduced NC-1 monoclonal antibody binding and enhanced 5-helix binding, consistent with the notion that this molecule promotes dissociation of gp41 trimers. This inactivation pathway may be important for the design of entry inhibitors and vaccine candidates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.