ArticleNature2014
Structure and immune recognition of trimeric pre-fusion HIV-1 Env.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 569 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
569 citing papers in PubMed.
- Use of 3M-052-AF with Alum adjuvant in HIV trimer vaccine induces human autologous neutralizing antibodies.The Journal of experimental medicine · 2024Trial
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- Structure and Dynamics of the HIV-1 Envelope Protein on the Virion Envelope.Journal of the American Chemical Society · 2026Article
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- Progress and prospects in HIV/AIDS pathogenicity research using rhesus macaque models: from SHIV model development to neutralizing antibody induction.The Journal of veterinary medical science · 2026Review
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- Investigating the role of a conserved hydrophobic pocket of gp41 in the anti-HIV activity of fusion inhibitors.Protein science : a publication of the Protein Society · 2026Article
- Recent advances in HIV-1 envelope-based vaccine designs for guiding broadly neutralizing antibody response.Journal of virology · 2026Review
- I53-50: Engineered icosahedral protein cage for modular vaccine nanoplatform.Journal of microbiology (Seoul, Korea) · 2026Review
- N-Glycans modulate tilting of HIV-1 envelope glycoprotein.Nature communications · 2026Article
- Decoding the glycan shield: Immune recognition and response to the HIV-1 envelope trimer.The Journal of biological chemistry · 2026Review
- Differential contributions of human oligosaccharyltransferase complexes OST-A and OST-B to HIV-1 envelope glycoprotein glycosylation.Journal of virology · 2026Article
- Identification of a potent V3 glycan site broadly neutralizing antibody targeting an N332Nature immunology · 2026Article
- Virus glycoprotein nanodisc platform for vaccine analytics.Nature communications · 2026Article
- HIV Membrane-Proximal External Region Scaffolded Immunogen as Killed Whole-Cell Genome-Reduced Vaccines.Viruses · 2026Article
- A Mammalian Surface Display Platform to Optimize the Antigenicity of Viral Proteins for Vaccine Design.bioRxiv : the preprint server for biology · 2026Article
- Structure of HIV-1 Env glycoprotein on virions reveals an alternative fusion subunit organization and native membrane coupling.bioRxiv : the preprint server for biology · 2026Article
- Galectin-8 binds HIV envelope glycoproteins with high affinity and promotes viral infectivity.Frontiers in cellular and infection microbiology · 2026Article
- [Molecular imprinting strategies and advances targeting biomembranes].Se pu = Chinese journal of chromatography · 2026Review
- Germline-Targeting Strategies to Induce bNAbs against HIV-1.Current HIV research · 2026Review
509 more citing papers are in PubMed but not listed here.
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Authors and funding
27 authors.
Funding
Abstract
The human immunodeficiency virus type 1 (HIV-1) envelope (Env) spike, comprising three gp120 and three gp41 subunits, is a conformational machine that facilitates HIV-1 entry by rearranging from a mature unliganded state, through receptor-bound intermediates, to a post-fusion state. As the sole viral antigen on the HIV-1 virion surface, Env is both the target of neutralizing antibodies and a focus of vaccine efforts. Here we report the structure at 3.5 Å resolution for an HIV-1 Env trimer captured in a mature closed state by antibodies PGT122 and 35O22. This structure reveals the pre-fusion conformation of gp41, indicates rearrangements needed for fusion activation, and defines parameters of immune evasion and immune recognition. Pre-fusion gp41 encircles amino- and carboxy-terminal strands of gp120 with four helices that form a membrane-proximal collar, fastened by insertion of a fusion peptide-proximal methionine into a gp41-tryptophan clasp. Spike rearrangements required for entry involve opening the clasp and expelling the termini. N-linked glycosylation and sequence-variable regions cover the pre-fusion closed spike; we used chronic cohorts to map the prevalence and location of effective HIV-1-neutralizing responses, which were distinguished by their recognition of N-linked glycan and tolerance for epitope-sequence variation.
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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.