ArticleEuropean journal of immunology2009
Structural requirements for the interaction of human IgM and IgA with the human Fcalpha/mu receptor.
Article in European journal of immunology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 49 citations in OpenAlex.
- Serum under-O-glycosylated IgA1 level is not correlated with glomerular IgA deposition based upon heterogeneity in the composition of immune complexes in IgA nephropathy.BMC nephrology · 2014Trial
- Intestinal immunoglobulins under microbial dysbiosis: implications in opioid-induced microbial dysbiosis.Frontiers in microbiology · 2025Review
- Plasmodium falciparum has evolved multiple mechanisms to hijack human immunoglobulin M.Nature communications · 2023Article
- The IgA of hares (Frontiers in immunology · 2023Article
- Identification of the Fc-alpha/mu receptor in Xenopus provides insight into the emergence of the poly-Ig receptor (pIgR) and mucosal Ig transport.European journal of immunology · 2021Article
- Fc Receptor Variants and Disease: A Crucial Factor to Consider in the Antibody Therapeutics in Clinic.International journal of molecular sciences · 2021Review
- Structure, Function, and Therapeutic Use of IgM Antibodies.Antibodies (Basel, Switzerland) · 2020Review
- Mapping of the binding site for FcμR in human IgM-Fc.Biochimica et biophysica acta. Proteins and proteomics · 2020Article
- IgA: Structure, Function, and Developability.Antibodies (Basel, Switzerland) · 2019Review
- Genetic Diversity ofAnimals : an open access journal from MDPI · 2019Article
- Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor.Scientific reports · 2017Article
- Agglutinating mouse IgG3 compares favourably with IgMs in typing of the blood group B antigen: Functionality and stability studies.Scientific reports · 2016Article
- TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity.Immunological reviews · 2015Review
- Human IgG4: a structural perspective.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
- Article
- Structural basis for Fc gammaRIIa recognition of human IgG and formation of inflammatory signaling complexes.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- Article
- Aggregation of Streptococcus pneumoniae by a pneumococcal capsular polysaccharide-specific human monoclonal IgM correlates with antibody efficacy in vivo.Clinical and vaccine immunology : CVI · 2010Article
- IgM, Fc mu Rs, and malarial immune evasion.Journal of immunology (Baltimore, Md. : 1950) · 2010Review
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 4 countries.
Funding
Abstract
Here we unravel the structural features of human IgM and IgA that govern their interaction with the human Fcalpha/mu receptor (hFcalpha/muR). Ligand polymerization status was crucial for the interaction, because hFcalpha/muR binding did not occur with monomeric Ab of either class. hFcalpha/muR bound IgM with an affinity in the nanomolar range, whereas the affinity for dimeric IgA (dIgA) was tenfold lower. Panels of mutant IgM and dIgA were used to identify regions critical for hFcalpha/muR binding. IgM binding required contributions from both Cmu3 and Cmu4 Fc domains, whereas for dIgA, an exposed loop in the Calpha3 domain was crucial. This loop, comprising residues Pro440-Phe443, lies at the Fc domain interface and has been implicated in the binding of host receptors FcalphaRI and polymeric Ig receptor (pIgR), as well as IgA-binding proteins produced by certain pathogenic bacteria. Substitutions within the Pro440-Phe443 loop resulted in loss of hFcalpha/muR binding. Furthermore, secretory component (SC, the extracellular portion of pIgR) and bacterial IgA-binding proteins were shown to inhibit the dIgA-hFcalpha/muR interaction. Therefore, we have identified a motif in the IgA-Fc inter-domain region critical for hFcalpha/muR interaction, and highlighted the multi-functional nature of a key site for protein-protein interaction at the IgA Fc domain interface.
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Registered trials
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