ArticlePLoS pathogens2019
IgA tetramerization improves target breadth but not peak potency of functionality of anti-influenza virus broadly neutralizing antibody.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 63 citations in OpenAlex.
- Serum IgA proteomics reveals clonal composition and neutralization of dimeric and monomeric IgA repertoires against human norovirus.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Research Advances and Biological Features of IgA for Immune-Related Diseases.International journal of molecular sciences · 2026Review
- Antibody Transcytosis and Neutralizing Activity in Respiratory Epithelial Cells.bioRxiv : the preprint server for biology · 2026Article
- Structural promiscuity in the human circulatory IgA1 clonal repertoire.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multimerization of secretory IgA enhances antiviral activity by aggregating influenza A virus particles.Communications biology · 2026Article
- Intranasal vaccination with probiotic Escherichia coli membrane vesicles displaying pneumococcal capsular polysaccharides elicits mucosal immunity.NPJ vaccines · 2025Article
- Expression of porcine-derived IgA against PEDV and use of Alg-CS gel to protect the IgA from degradation in simulated gastric fluid.Archives of virology · 2025Article
- Neutralizing Antibodies vs. Viruses: Interacting Mechanisms and Escape Tactics.Microorganisms · 2025Review
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- An intranasally administered IgM protects against antigenically distinct subtypes of influenza A viruses.Nature communications · 2025Article
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- Intranasal administration of a panreactive influenza antibody reveals Fc-independent mode of protection.Scientific reports · 2025Article
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- The role of vaccines in the COVID-19 pandemic: what have we learned?Seminars in immunopathology · 2024Review
- Infectious virus shedding duration reflects secretory IgA antibody response latency after SARS-CoV-2 infection.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function.Nature communications · 2023Article
- Structural basis for cross-group recognition of an influenza virus hemagglutinin antibody that targets postfusion stabilized epitope.PLoS pathogens · 2023Article
- A new hope? Possibilities of therapeutic IgA antibodies in the treatment of inflammatory lung diseases.Frontiers in immunology · 2023Review
- Application of spatial transcriptomics analysis using the Visium system for the mouse nasal cavity after intranasal vaccination.Frontiers in immunology · 2023Article
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Authors and funding
18 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mucosal immunoglobulins comprise mainly secretory IgA antibodies (SIgAs), which are the major contributor to pathogen-specific immune responses in mucosal tissues. These SIgAs are highly heterogeneous in terms of their quaternary structure. A recent report shows that the polymerization status of SIgA defines their functionality in the human upper respiratory mucosa. Higher order polymerization of SIgA (i.e., tetramers) leads to a marked increase in neutralizing activity against influenza viruses. However, the precise molecular mechanisms underlying the effects of SIgA polymerization remain elusive. Here, we developed a method for generating recombinant tetrameric monoclonal SIgAs. We then compared the anti-viral activities of these tetrameric SIgAs, which possessed variable regions identical to that of a broadly neutralizing anti-influenza antibody F045-092 against influenza A viruses, with that of monomeric IgG or IgA. The tetrameric SIgA showed anti-viral inhibitory activity superior to that of other forms only when the antibody exhibits low-affinity binding to the target. By contrast, SIgA tetramerization did not substantially modify anti-viral activity against targets with high-affinity binding. Taken together, the data suggest that tetramerization of SIgA improved target breadth, but not peak potency of antiviral functions of the broadly neutralizing anti-influenza antibody. This phenomenon presumably represents one of the mechanisms by which SIgAs present in human respiratory mucosa prevent infection by antigen-drifted influenza viruses. Understanding the mechanisms involved in cross neutralization of viruses by SIgAs might facilitate the development of vaccine strategies against viral infection of mucosal tissues.
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