ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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.
The trial behind it
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
54 citing papers in PubMed, 72 citations in OpenAlex.
- Article
- Engineering Protein-Based HIV Entry Inhibitors: Advances, Challenges, and Translational Strategies.Biomolecules · 2026Review
- Diverse germline-targeting HIV Env immunogens select for distinct mutations in the same knock-in mice B cell receptors.Nature communications · 2026Article
- VDJ-Insights: simplifying the annotation of genomic immunoglobulin and T cell receptor regions.Bioinformatics (Oxford, England) · 2026Article
- The Germline Targeting Vaccine Concept: Overview and Updates from HIV Pre-Clinical and Clinical Trials.Current HIV research · 2026Review
- Potent neutralization by antibodies targeting the MPXV A28 protein.Nature communications · 2025Article
- Ultra-long sequencing for contiguous haplotype resolution of the human immunoglobulin heavy-chain locus.Genome research · 2025Article
- Increased immunogen valency improves the maturation of vaccine-elicited HIV-1 VRC01-like antibodies.PLoS pathogens · 2025Article
- Towards a unifying model for B-cell receptor triggering.Nature reviews. Immunology · 2025Review
- Short CDRL1 in intermediate VRC01-like mAbs is not sufficient to overcome key glycan barriers on HIV-1 Env.Journal of virology · 2024Article
- Germline-targeting HIV vaccination induces neutralizing antibodies to the CD4 binding site.Science immunology · 2024Article
- A VRC13-like bNAb response is associated with complex escape pathways in HIV-1 envelope.Journal of virology · 2024Article
- Vaccine induction of CD4-mimicking HIV-1 broadly neutralizing antibody precursors in macaques.Cell · 2024Article
- Article
- HIV-1 CD4-binding site germline antibody-Env structures inform vaccine design.Nature communications · 2022Article
- Characterization of a vaccine-elicited human antibody with sequence homology to VRC01-class antibodies that binds the C1C2 gp120 domain.Science advances · 2022Article
- Selective Recognition of Carbohydrate Antigens by Germline Antibodies Isolated from AID Knockout Mice.Journal of the American Chemical Society · 2022Article
- Design of human immunodeficiency virus-1 neutralizing peptides targeting CD4-binding site: An integrative computational biologics approach.Frontiers in medicine · 2022Article
- Development and in vitro characterization of a humanized scFv against fungal infections.PloS one · 2022Article
- Immunoglobulin germline gene variation and its impact on human disease.Genes and immunity · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Efforts to design an effective antibody-based vaccine against HIV-1 would benefit from understanding how germ-line B-cell receptors (BCRs) recognize the HIV-1 gp120/gp41 envelope spike. Potent VRC01-like (PVL) HIV-1 antibodies derived from the VH1-2*02 germ-line allele target the conserved CD4 binding site on gp120. A bottleneck for design of immunogens capable of eliciting PVL antibodies is that VH1-2*02 germ-line BCR interactions with gp120 are uncharacterized. Here, we report the structure of a VH1-2*02 germ-line antibody alone and a germ-line heavy-chain/mature light-chain chimeric antibody complexed with HIV-1 gp120. VH1-2*02 residues make extensive contacts with the gp120 outer domain, including all PVL signature and CD4 mimicry interactions, but not critical CDRH3 contacts with the gp120 inner domain and bridging sheet that are responsible for the improved potency of NIH45-46 over closely related clonal variants, such as VRC01. Our results provide insight into initial recognition of HIV-1 by VH1-2*02 germ-line BCRs and may facilitate the design of immunogens tailored to engage and stimulate broad and potent CD4 binding site antibodies.
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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.