ArticleNature communications2019
A sequestered fusion peptide in the structure of an HIV-1 transmitted founder envelope trimer.
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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Conformational landscape of HIV-1 Env from closed to fully open.Nature communications · 2026Article
- Targeted bacteriophage T4 nanoparticles reverse HIV-1 latency in human T cell line models.iScience · 2025Article
- Structure-Guided Design of Novel Diarylpyrimidine-Based NNRTIs Through a Comprehensive In Silico Approach: 3D-QSAR, ADMET Evaluation, Molecular Docking, and Molecular Dynamics.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Viral glycoprotein-mediated entry and antibody-mediated immunity in HIV-1 and SARS-CoV-2 infection.Frontiers in immunology · 2025Review
- A remarkable genetic shift in a transmitted/founder virus broadens antibody responses against HIV-1.eLife · 2024Article
- Cryo-electron microscopy in the study of virus entry and infection.Frontiers in molecular biosciences · 2024Review
- Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir.Nature communications · 2023Article
- Structures and immune recognition of Env trimers from two Asia prevalent HIV-1 CRFs.Nature communications · 2023Article
- Immune reconstruction effectiveness of combination antiretroviral therapy for HIV-1 CRF01_AE cluster 1 and 2 infected individuals.Emerging microbes & infections · 2022Article
- Structural dynamics reveal isolate-specific differences at neutralization epitopes on HIV Env.iScience · 2022Article
- R848 Adjuvant Laden With Self-Assembled Nanoparticle-Based mRNA Vaccine Elicits Protective Immunity Against H5N1 in Mice.Frontiers in immunology · 2022Article
- Review
- Peptide Triazole Thiol Irreversibly Inactivates Metastable HIV-1 Env by Accessing Conformational Triggers Intrinsic to Virus-Cell Entry.Microorganisms · 2021Article
- Neutralizing Antibodies Targeting HIV-1 gp41.Viruses · 2020Review
- Probing the Structure of the HIV-1 Envelope Trimer Using Aspartate Scanning Mutagenesis.Journal of virology · 2020Article
- Common evolutionary features of the envelope glycoprotein of HIV-1 in patients belonging to a transmission chain.Scientific reports · 2020Article
- Strategies for inducing effective neutralizing antibody responses against HIV-1.Expert review of vaccines · 2019Review
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Authors and funding
14 authors.
Funding
Abstract
The envelope protein of human immunodeficiency virus-1 (HIV-1) and its fusion peptide are essential for cell entry and vaccine design. Here, we describe the 3.9-Å resolution structure of an envelope protein trimer from a very early transmitted founder virus (CRF01_AE T/F100) complexed with Fab from the broadly neutralizing antibody (bNAb) 8ANC195. The overall T/F100 trimer structure is similar to other reported "closed" state prefusion trimer structures. In contrast, the fusion peptide, which is exposed to solvent in reported closed structures, is sequestered (buried) in the hydrophobic core of the T/F100 trimer. A buried conformation has previously been observed in "open" state structures formed after CD4 receptor binding. The T/F100 trimer binds poorly to bNAbs including the fusion peptide-specific bNAbs PGT151 and VRC34.01. The T/F100 structure might represent a prefusion state, intermediate between the closed and open states. These observations are relevant to mechanisms of HIV-1 transmission and vaccine design.
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