ArticleCommunications biology2026
Multimerization of secretory IgA enhances antiviral activity by aggregating influenza A virus particles.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
12 authors.
Funding
Abstract
Secretory immunoglobulin A (sIgA), the first line of defense against mucosal epithelial infections, is a multimer. Although multimeric sIgA shows higher antiviral activity than monomeric IgA, the mechanism underlying this enhancement and the functional differences among IgA subclasses remain unclear. Here, we generated recombinant monomeric and multimeric IgA1 and IgA2m2 antibodies from clone F045-092, which targets the head domain of influenza A virus (IAV) hemagglutinin (HA) and inhibits viral entry, and compared their functional properties. Monomeric IgA1 inhibited viral entry but not viral release. Multimerization of IgA1 enhanced viral entry inhibition and conferred the additional function of inhibiting viral release. In contrast, monomeric IgA2m2 inhibited both viral entry and release and its multimerization enhanced these inhibitory effects. Importantly, treatment of IAV particles with multimeric sIgA or monomeric IgA2m2 induced viral aggregation via IgA-mediated tethering of neighboring virus particles, as visualized via cryo-electron tomography. Analysis of F(ab')
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