ArticleThe Journal of biological chemistry2009
The nonplanar secretory IgA2 and near planar secretory IgA1 solution structures rationalize their different mucosal immune responses.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 68 citations in OpenAlex.
- Research Advances and Biological Features of IgA for Immune-Related Diseases.International journal of molecular sciences · 2026Review
- Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026Review
- 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
- Natural and induced immune responses in oral cavity and saliva.BMC immunology · 2025Review
- Nasal delivery of secretory IgA confers enhanced neutralizing activity against Omicron variants compared to its IgG counterpart.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Conversion of monoclonal IgG to dimeric and secretory IgA restores neutralizing ability and prevents infection of Omicron lineages.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cross-tissue immune cell analysis reveals tissue-specific features in humans.Science (New York, N.Y.) · 2022Article
- Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodies.Cellular and molecular life sciences : CMLS · 2021Article
- Cooperation Between Systemic IgG1 and Mucosal Dimeric IgA2 Monoclonal Anti-HIV Env Antibodies: Passive Immunization Protects Indian Rhesus Macaques Against Mucosal SHIV Challenges.Frontiers in immunology · 2021Article
- Loop Grafting between Similar Local Environments for Fc-Silent Antibodies.Journal of chemical information and modeling · 2020Article
- IgA as a potential candidate for enteric monoclonal antibody therapeutics with improved gastrointestinal stability.Vaccine · 2020Article
- Article
- Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses.Cell reports · 2018Article
- BAFF augments IgA2 and IL-10 production by TLR7/8 stimulated total peripheral blood B cells.European journal of immunology · 2018Article
- Antibody-mediated immune exclusion of HIV.Current opinion in HIV and AIDS · 2017Review
- Immunoglobulin A nephropathy: a pathophysiology view.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2016Review
- TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity.Immunological reviews · 2015Review
- Article
- Are anti-HIV IgAs good guys or bad guys?Retrovirology · 2014Review
- Regional specialization within the intestinal immune system.Nature reviews. Immunology · 2014Review
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Secretory IgA (SIgA) is the most prevalent human antibody and is central to mucosal immunity. It exists as two subclasses, SIgA1 and SIgA2, where SIgA2 has a shorter hinge joining the Fab and Fc regions. Both forms of SIgA are predominantly dimeric and contain an additional protein called the secretory component (SC) that is attached during the secretory process and is believed to protect SIgA in harsh mucosal conditions. Here we locate the five SC domains relative to dimeric IgA2 within SIgA2 using constrained scattering modeling. The x-ray and sedimentation parameters showed that SIgA2 has an extended solution structure. The constrained modeling of SIgA2 was initiated using two IgA2 monomers that were positioned according to our best fit solution structure for dimeric IgA1. SC was best located along the convex edge of the Fc-Fc region. The best fit models showed that SIgA2 is significantly nonplanar in its structure, in distinction to our previous near planar SIgA1 structure. Both the shorter IgA2 hinges and the presence of SC appear to displace the four Fab regions out of the Fc plane in SIgA2. This may explain the noncovalent binding of SC in some SIgA2 molecules. This nonplanar structure is predicted to result in specific immune properties for SIgA2 and SIgA1. It may explain differences observed between the SIgA1 and SIgA2 subclasses in terms of their interactions with antigens, susceptibility to proteases, effects on receptors, and distribution in different tissues. The different structures account for the prevalence of both forms in mucosal secretions.
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Registered trials
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