ArticleNature communications2019
Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodies.Nature reviews. Microbiology · 2025Review
- Microscopic insight into HIV fusion peptide-mediated dehydration and packing regulation in membranes.Biophysical journal · 2025Article
- Viral glycoprotein-mediated entry and antibody-mediated immunity in HIV-1 and SARS-CoV-2 infection.Frontiers in immunology · 2025Review
- Insertion and Anchoring of HIV-1 Fusion Peptide into Complex Membrane Mimicking Human T-cell.bioRxiv : the preprint server for biology · 2024Article
- Identification of residues in Lassa virus glycoprotein 1 involved in receptor switch.Virologica Sinica · 2024Article
- Priming antibody responses to the fusion peptide in rhesus macaques.NPJ vaccines · 2024Article
- Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site.Nature communications · 2023Article
- Alterations in gp120 glycans or the gp41 fusion peptide-proximal region modulate the stability of the human immunodeficiency virus (HIV-1) envelope glycoprotein pretriggered conformation.Journal of virology · 2023Article
- Structural basis for respiratory syncytial virus and human metapneumovirus neutralization.Current opinion in virology · 2023Review
- Conformational antigenic heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.Retrovirology · 2023Article
- Conformational antigenic heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.Research square · 2023Article
- Peptide Triazole Inhibitors of HIV-1: Hijackers of Env Metastability.Current protein & peptide science · 2023Review
- Structural dynamics reveal isolate-specific differences at neutralization epitopes on HIV Env.iScience · 2022Article
- Antibody elicited by HIV-1 immunogen vaccination in macaques displaces Env fusion peptide and destroys a neutralizing epitope.NPJ vaccines · 2021Article
- Article
- Peptide Triazole Thiol Irreversibly Inactivates Metastable HIV-1 Env by Accessing Conformational Triggers Intrinsic to Virus-Cell Entry.Microorganisms · 2021Article
- Article
- Virus-Like Particle Based Vaccines Elicit Neutralizing Antibodies against the HIV-1 Fusion Peptide.Vaccines · 2020Article
- Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements.Nature communications · 2020Article
- Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody.Nature structural & molecular biology · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The N-terminal fusion peptide (FP) of the human immunodeficiency virus (HIV)-1 envelope glycoprotein (Env) gp41 subunit plays a critical role in cell entry. However, capturing the structural flexibility in the unbound FP is challenging in the native Env trimer. Here, FP conformational isomerism is observed in two crystal structures of a soluble clade B transmitted/founder virus B41 SOSIP.664 Env with broadly neutralizing antibodies (bNAbs) PGT124 and 35O22 to aid in crystallization and that are not specific for binding to the FP. Large rearrangements in the FP and fusion peptide proximal region occur around M530, which remains anchored in the tryptophan clasp (gp41 W623, W628, W631) in the B41 Env prefusion state. Further, we redesigned the FP at position 518 to reinstate the bNAb VRC34.01 epitope. These findings provide further structural evidence for the dynamic nature of the FP and how a bNAb epitope can be restored during vaccine design.
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