ArticleNature2011
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 632 papers, 2 of them syntheses that pooled it.
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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
632 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- A potential antibody repertoire diversification mechanism through tyrosine sulfation for biotherapeutics engineering and production.Frontiers in immunology · 2022Pooled it
- Employing Broadly Neutralizing Antibodies as a Human Immunodeficiency Virus Prophylactic & Therapeutic Application.Frontiers in immunology · 2021Pooled it
- Adeno-associated virus vectored immunoprophylaxis to prevent HIV in healthy adults: a phase 1 randomised controlled trial.The lancet. HIV · 2019Trial
- Targeting of conserved spike epitopes enables broad antibody neutralisation of diverse bat sarbecoviruses.PLoS biology · 2026Article
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- Structure and Dynamics of the HIV-1 Envelope Protein on the Virion Envelope.Journal of the American Chemical Society · 2026Article
- Engineering Protein-Based HIV Entry Inhibitors: Advances, Challenges, and Translational Strategies.Biomolecules · 2026Review
- Rapid and robust immune response boosting with potent, next-generation adjuvant in viral vector-primed primates.Journal of virology · 2026Article
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- Endocytic motif on HIV-1 Env regulates cleavage status and antibody neutralization of cell-free and cell-to-cell infection.Journal of virology · 2026Article
- Structural Insights Into ManAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- Genotypic challenges in implementing broadly neutralizing antibody-based long-acting HIV-1 therapies.Communications medicine · 2026Review
- Deep mining of the human antibody repertoire identifies frequent and genetically diverse CDRH3 topologies targetable by vaccination.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- N-Glycans modulate tilting of HIV-1 envelope glycoprotein.Nature communications · 2026Article
- Germline-targeting HIV immunogen induces cross-neutralizing antibodies in outbred macaques.Immunity · 2026Article
- Decoding the glycan shield: Immune recognition and response to the HIV-1 envelope trimer.The Journal of biological chemistry · 2026Review
- Early clonal dominance at priming sets the trajectory for broad HIV serum neutralization.bioRxiv : the preprint server for biology · 2026Article
- Env-antibody coevolution identifies B cell priming as the principal bottleneck to HIV V2 apex broadly neutralizing antibody development.Science immunology · 2026Article
- Immunomodulation by glycosylation: bridging glycobiology to adaptive immunity and therapeutic innovation.Frontiers in immunology · 2026Review
572 more citing papers are in PubMed but not listed here.
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47 authors.
Funding
Abstract
Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody neutralization, and are themselves protected by extraordinary sequence diversity and N-linked glycosylation. Human antibodies such as PG9 nonetheless engage V1/V2 and neutralize 80% of HIV-1 isolates. Here we report the structure of V1/V2 in complex with PG9. V1/V2 forms a four-stranded β-sheet domain, in which sequence diversity and glycosylation are largely segregated to strand-connecting loops. PG9 recognition involves electrostatic, sequence-independent and glycan interactions: the latter account for over half the interactive surface but are of sufficiently weak affinity to avoid autoreactivity. The structures of V1/V2-directed antibodies CH04 and PGT145 indicate that they share a common mode of glycan penetration by extended anionic loops. In addition to structurally defining V1/V2, the results thus identify a paradigm of antibody recognition for highly glycosylated antigens, which-with PG9-involves a site of vulnerability comprising just two glycans and a strand.
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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.