ArticleNature communications2023
Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
18 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Priming of Multiple HIV Neutralizing B Cell Precursors in Humans.medRxiv : the preprint server for health sciences · 2026Article
- Anti-malaria antibody engineering broadens recognition motifs and reveals new homotypic interactions that enhance protective breadth.Nature communications · 2026Article
- Egyptian rousette bat humoral immunity to H9 influenza hemagglutinin.bioRxiv : the preprint server for biology · 2026Article
- Genotypic challenges in implementing broadly neutralizing antibody-based long-acting HIV-1 therapies.Communications medicine · 2026Review
- Harnessing Nature's Algorithm: From Test Tubes to Autonomous In Vivo Evolution.Biotechnology journal · 2026Review
- The adaptive immune receptors in a big data world.ImmunoHorizons · 2026Review
- Contemporary HIV-1 envelope pseudovirus panels for detecting and assessing B cell lineages with broadly neutralizing antibody potential.PLoS pathogens · 2026Article
- Contemporary HIV-1 envelope pseudovirus panels for detecting and assessing B cell lineages with broadly neutralizing antibody potential.bioRxiv : the preprint server for biology · 2025Article
- Article
- Anti-Malaria Antibody Engineering Broadens Recognition Motifs and Reveals New Homotypic Interactions that Enhance Protective Breadth.bioRxiv : the preprint server for biology · 2025Article
- Optimizing a human monoclonal antibody for better neutralization of SARS-CoV-2.Nature communications · 2025Article
- Breaking Barriers to an HIV-1 Cure: Innovations in Gene Editing, Immune Modulation, and Reservoir Eradication.Life (Basel, Switzerland) · 2025Review
- A facile yeast-display approach for antibody mask discovery.Protein engineering, design & selection : PEDS · 2025Article
- Beyond Single Clones: High-Throughput Sequencing in Antibody Discovery.Cold Spring Harbor protocols · 2025Article
- A library-on-library screen reveals the breadth expansion landscape of a broadly neutralizing betacoronavirus antibody.bioRxiv : the preprint server for biology · 2024Article
- Cryo-electron microscopy in the study of virus entry and infection.Frontiers in molecular biosciences · 2024Review
- Vaccine-elicited and naturally elicited antibodies differ in their recognition of the HIV-1 fusion peptide.Frontiers in immunology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
26 authors at 3 institutions in 1 country.
Funding
Abstract
The HIV-1 fusion peptide (FP) represents a promising vaccine target, but global FP sequence diversity among circulating strains has limited anti-FP antibodies to ~60% neutralization breadth. Here we evolve the FP-targeting antibody VRC34.01 in vitro to enhance FP-neutralization using site saturation mutagenesis and yeast display. Successive rounds of directed evolution by iterative selection of antibodies for binding to resistant HIV-1 strains establish a variant, VRC34.01_mm28, as a best-in-class antibody with 10-fold enhanced potency compared to the template antibody and ~80% breadth on a cross-clade 208-strain neutralization panel. Structural analyses demonstrate that the improved paratope expands the FP binding groove to accommodate diverse FP sequences of different lengths while also recognizing the HIV-1 Env backbone. These data reveal critical antibody features for enhanced neutralization breadth and potency against the FP site of vulnerability and accelerate clinical development of broad HIV-1 FP-targeting vaccines and therapeutics.
Indexed as
Identifiers
What OpenQuestion holds
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.