ArticleImmunity2018
A Neutralizing Antibody Recognizing Primarily N-Linked Glycan Targets the Silent Face of the HIV Envelope.
Article in Immunity, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Employing Broadly Neutralizing Antibodies as a Human Immunodeficiency Virus Prophylactic & Therapeutic Application.Frontiers in immunology · 2021Pooled it
- N-Glycans modulate tilting of HIV-1 envelope glycoprotein.Nature communications · 2026Article
- Enhanced Clearance of HIV-1 Broadly Neutralizing Antibody VRC07-523-LS During Viremia: Influences on Trial Design and Analysis.Clinical and translational science · 2026Article
- The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodies.Nature reviews. Microbiology · 2025Review
- Identification of a broad and potent V3 glycan site bNAb targeting an N332bioRxiv : the preprint server for biology · 2025Article
- Article
- Beyond glycan barriers: non-cognate ligands and protein mimicry approaches to elicit broadly neutralizing antibodies for HIV-1.Journal of biomedical science · 2024Review
- Broadly neutralizing antibodies for HIV prevention: a comprehensive review and future perspectives.Clinical microbiology reviews · 2024Review
- Long trimer-immunization interval and appropriate adjuvant reduce immune responses to the soluble HIV-1-envelope trimer base.iScience · 2024Article
- Neutralizing the threat: harnessing broadly neutralizing antibodies against HIV-1 for treatment and prevention.Microbial cell (Graz, Austria) · 2024Article
- Current methods for detecting and assessing HIV-1 antibody resistance.Frontiers in immunology · 2024Review
- Broadly neutralizing antibodies targeting HIV: Progress and challenges.Clinical immunology (Orlando, Fla.) · 2023Review
- An Overview of Human Anti-HIV-1 Neutralizing Antibodies against Diverse Epitopes of HIV-1.ACS omega · 2023Review
- Article
- Complementary antibody lineages achieve neutralization breadth in an HIV-1 infected elite neutralizer.PLoS pathogens · 2022Article
- Antigenic analysis of the HIV-1 envelope trimer implies small differences between structural states 1 and 2.The Journal of biological chemistry · 2022Article
- Analysis of B Cell Receptor Repertoires Reveals Key Signatures of the Systemic B Cell Response after SARS-CoV-2 Infection.Journal of virology · 2022Article
- Cross-Neutralizing CRF01_AE-Infected Plasma from Malaysia Targets CD4-Binding Site of Human Immunodeficiency Virus Type-1 Envelope Glycoprotein.AIDS research and human retroviruses · 2022Article
- High-Throughput B Cell Epitope Determination by Next-Generation Sequencing.Frontiers in immunology · 2022Article
- Lentil lectin derived fromEmerging microbes & infections · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
35 authors.
Funding
Abstract
Virtually the entire surface of the HIV-1-envelope trimer is recognized by neutralizing antibodies, except for a highly glycosylated region at the center of the "silent face" on the gp120 subunit. From an HIV-1-infected donor, #74, we identified antibody VRC-PG05, which neutralized 27% of HIV-1 strains. The crystal structure of the antigen-binding fragment of VRC-PG05 in complex with gp120 revealed an epitope comprised primarily of N-linked glycans from N262, N295, and N448 at the silent face center. Somatic hypermutation occurred preferentially at antibody residues that interacted with these glycans, suggesting somatic development of glycan recognition. Resistance to VRC-PG05 in donor #74 involved shifting of glycan-N448 to N446 or mutation of glycan-proximal residue E293. HIV-1 neutralization can thus be achieved at the silent face center by glycan-recognizing antibody; along with other known epitopes, the VRC-PG05 epitope completes coverage by neutralizing antibody of all major exposed regions of the prefusion closed trimer.
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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.