ArticleCell discovery2019
Light chain modulates heavy chain conformation to change protection profile of monoclonal antibodies against influenza A viruses.
Article in Cell discovery, 2019. 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
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Comparison of Igκ and Igλ binding toward influenza virus hemagglutinin and SARS-CoV-2 Spike protein during primary viral infections in humans, mice, and pigs.Comparative immunology, microbiology and infectious diseases · 2026Article
- Heavy-chain immune repertoire sequencing enables language-model prediction of antigen-specific antibodies.Research square · 2026Article
- Selection and characterization of a broadly neutralizing class of HCV anti-E2 VH1-69 antibodies.PLoS pathogens · 2025Article
- Opportunities and challenges for T cell-based influenza vaccines.Nature reviews. Immunology · 2024Review
- Biosafety and immunology: An interdisciplinary field for health priority.Biosafety and health · 2024Review
- Antibodies utilizing VL6-57 light chains target a convergent cryptic epitope on SARS-CoV-2 spike protein and potentially drive the genesis of Omicron variants.Nature communications · 2024Article
- The Discovery and Characterization of a Potent DPP-IV Inhibitory Peptide from Oysters for the Treatment of Type 2 Diabetes Based on Computational and Experimental Studies.Marine drugs · 2024Article
- In vivo mRNA expression of a multi-mechanistic mAb combination protects against Staphylococcus aureus infection.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- Recombination Events Among SARS-CoV-2 Omicron Subvariants: Impact on Spike Interaction With ACE2 Receptor and Neutralizing Antibodies.Evolutionary bioinformatics online · 2024Article
- Bat humoral immunity and its role in viral pathogenesis, transmission, and zoonosis.Frontiers in immunology · 2024Review
- Canine interleukin-31 binds directly to OSMRβ with higher binding affinity than to IL-31RA.3 Biotech · 2023Article
- Article
- Structural basis for a human broadly neutralizing influenza A hemagglutinin stem-specific antibody including H17/18 subtypes.Nature communications · 2022Article
- Avian influenza A (H7N9) virus: from low pathogenic to highly pathogenic.Frontiers of medicine · 2021Review
- Potent sialic acid inhibitors that target influenza A virus hemagglutinin.Scientific reports · 2021Article
- Convergent antibody evolution and clonotype expansion following influenza virus vaccination.PloS one · 2021Article
- Identification of Structurally Related Antibodies in Antibody Sequence Databases Using Rosetta-Derived Position-Specific Scoring.Structure (London, England : 1993) · 2020Article
- Article
Corrections and comments
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Authors and funding
22 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The isolation of human monoclonal antibodies with broadly neutralizing breadth can provide a promising countermeasure for influenza A viruses infection. Most broadly neutralizing antibodies against influenza A viruses bind to the conserved stem region or the receptor-binding cavity of hemagglutinin and the interaction is dominated by the heavy chain. The light chain, however, contributes few or no direct contacts to the antigen. Here we report an H3-clade neutralizing human monoclonal antibody, AF4H1K1, which recognizes the hemagglutinin glycoproteins of all group 2 influenza A viruses. This human monoclonal antibody has been obtained through the screening by pairing different heavy and light chains from an H7N9-infected patient based on the next-generation sequencing technology. Further structural studies revealed that light chains modulate the neutralizing spectrum by affecting the local conformation of heavy chains, instead of direct interaction with the antigen. These findings provide important clues to understand the molecular basis of light chains in antigen recognition and to explore the strategies in particular of the use of light chain modification to develop broadly protective monoclonal antibodies against influenza A viruses and other emerging viruses.
Identifiers
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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.