ArticleThe Journal of experimental medicine1996
Localization of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Calpha2 and Calpha3 in human IgA1.
Article in The Journal of experimental medicine, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
What it found
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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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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.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 98 citations in OpenAlex.
- Anti-Desmocollin Autoantibodies in Autoimmune Blistering Diseases.Frontiers in immunology · 2021Pooled it
- Antibody Fc-chimerism and effector functions: When IgG takes advantage of IgA.Frontiers in immunology · 2023Review
- Fc Engineering Strategies to Advance IgA Antibodies as Therapeutic Agents.Antibodies (Basel, Switzerland) · 2020Review
- IgA: Structure, Function, and Developability.Antibodies (Basel, Switzerland) · 2019Review
- FcαRI binding at the IgA1 CProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Peptide mimetics of immunoglobulin A (IgA) and FcαRI block IgA-induced human neutrophil activation and migration.European journal of immunology · 2017Article
- TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity.Immunological reviews · 2015Review
- Translocalized IgA mediates neutralization and stimulates innate immunity inside infected cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Antigen binding to secretory immunoglobulin A results in decreased sensitivity to intestinal proteases and increased binding to cellular Fc receptors.The Journal of biological chemistry · 2010Article
- Structural requirements for the interaction of human IgM and IgA with the human Fcalpha/mu receptor.European journal of immunology · 2009Article
- Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- IgA and IgA-specific receptors in human disease: structural and functional insights into pathogenesis and therapeutic potential.Springer seminars in immunopathology · 2006Article
- Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques.Immunology · 2005Article
- Article
- Limited role of charge matching in the interaction of human immunoglobulin A with the immunoglobulin A Fc receptor (Fc alpha RI) CD89.Immunology · 2003Article
- Structural and functional consequences of cleavage of human secretory and human serum immunoglobulin A1 by proteinases from Proteus mirabilis and Neisseria meningitidis.Infection and immunity · 2003Article
- Amino acid sequence requirements in the hinge of human immunoglobulin A1 (IgA1) for cleavage by streptococcal IgA1 proteases.Infection and immunity · 2003Article
- Cleavage of a recombinant human immunoglobulin A2 (IgA2)-IgA1 hybrid antibody by certain bacterial IgA1 proteases.Infection and immunity · 2000Article
- Immunoglobulin-binding sites of human FcalphaRI (CD89) and bovine Fcgamma2R are located in their membrane-distal extracellular domains.The Journal of experimental medicine · 1999Article
- A human immunoglobulin (Ig)A calpha3 domain motif directs polymeric Ig receptor-mediated secretion.The Journal of experimental medicine · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Immunoglobulin (Ig) A serves as the first line of humoral defense at all mucosal surfaces and is present in large quantities of blood. In playing its role in humoral immunity, IgA interacts with a variety of effector molecules present both in serum and on the surfaces of immune and inflammatory cells. To study these interactions, we previously established expression of human IgA1 in insect cells using recombinant baculoviruses and showed that the expressed antibody is a structurally and functionally intact polypeptide useful for examining the molecular properties of IgA. Indeed, since the C alpha 2 N-linked glycosylation site lies near the Fab-distal pole of C alpha 2, the inability of a mutant IgA1 lacking C alpha 2 N-glycosylation to bind its cognate receptor suggested that the monocyte Fc alpha receptor (mFcalphaR) recognizes IgA at a hinge-distal site encompassing the boundary between the C alpha 2 and C alpha 3 domains. In this report, we utilize both domain-swapped IgA/IgG and point-mutated IgA chimeras to verify the above hypothesis. Using an antigen-specific rosetting assay and a mFc alpha R-expressing cell line, we show that (a) C alpha 2 and C alpha 3 together are necessary and sufficient for binding; (b) neither the IgA hinge nor the tailpiece is necessary for binding; (c) mutations away from the interdomain boundary do not affect binding; and (d) mutations located near the three-dimensional boundary between C alpha 2 and C alpha 3 completely disrupt binding. Taken together, these results localize the mFc alpha R recognition site on IgA to the boundary region between the second and third constant domains--a site analogous to that recognized by Staphylococcus aureus protein A on IgG. The use of this hinge-distal site is, to date, unique among Fc receptors of the Ig superfamily.
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