ArticleNature communications2017
In vitro evolution of an influenza broadly neutralizing antibody is modulated by hemagglutinin receptor specificity.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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
47 citing papers in PubMed, 73 citations in OpenAlex.
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- High-throughput synthesis and specificity characterization of natively paired influenza hemagglutinin antibodies with oPoolScience translational medicine · 2025Article
- An explainable language model for antibody specificity prediction using curated influenza hemagglutinin antibodies.Immunity · 2024Article
- A library-on-library screen reveals the breadth expansion landscape of a broadly neutralizing betacoronavirus antibody.bioRxiv : the preprint server for biology · 2024Article
- Effects of selection stringency on the outcomes of directed evolution.bioRxiv : the preprint server for biology · 2024Article
- Article
- Stringent and complex sequence constraints of an IGHV1-69 broadly neutralizing antibody to influenza HA stem.Cell reports · 2023Article
- An explainable language model for antibody specificity prediction using curated influenza hemagglutinin antibodies.bioRxiv : the preprint server for biology · 2023Article
- Improved HIV-1 neutralization breadth and potency of V2-apex antibodies by in silico design.Cell reports · 2023Article
- Genotype-phenotype landscapes for immune-pathogen coevolution.Trends in immunology · 2023Review
- Structural characterisation of hemagglutinin from seven Influenza A H1N1 strains reveal diversity in the C05 antibody recognition site.Scientific reports · 2023Article
- Mechanisms that promote the evolution of cross-reactive antibodies upon vaccination with designed influenza immunogens.Cell reports · 2023Article
- Article
- Potential of conserved antigenic sites in development of universal SARS-like coronavirus vaccines.Frontiers in immunology · 2022Article
- Primary antibody response after influenza virus infection is first dominated by low-mutated HA-stem antibodies followed by higher-mutated HA-head antibodies.Frontiers in immunology · 2022Article
- Identification of Hemagglutinin Mutations Caused by Neuraminidase Antibody Pressure.Microbiology spectrum · 2021Article
- Binding affinity landscapes constrain the evolution of broadly neutralizing anti-influenza antibodies.eLife · 2021Article
- Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain.Nature communications · 2021Article
- Article
- Modeling Immunity with Rosetta: Methods for Antibody and Antigen Design.Biochemistry · 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
7 authors at 1 institution in 1 country.
Funding
Abstract
The relatively recent discovery and characterization of human broadly neutralizing antibodies (bnAbs) against influenza virus provide valuable insights into antiviral and vaccine development. However, the factors that influence the evolution of high-affinity bnAbs remain elusive. We therefore explore the functional sequence space of bnAb C05, which targets the receptor-binding site (RBS) of influenza haemagglutinin (HA) via a long CDR H3. We combine saturation mutagenesis with yeast display to enrich for C05 variants of CDR H3 that bind to H1 and H3 HAs. The C05 variants evolve up to 20-fold higher affinity but increase specificity to each HA subtype used in the selection. Structural analysis reveals that the fine specificity is strongly influenced by a highly conserved substitution that regulates receptor binding in different subtypes. Overall, this study suggests that subtle natural variations in the HA RBS between subtypes and species may differentially influence the evolution of high-affinity bnAbs.
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.