Mac-1 (CD11b/CD18) as Accessory Molecule for FcαR (CD89) Binding of IgA

Spriel, Annemiek B. van; Leusen, Jeanette H.W.; Vilé, Henriette A.; Winkel, Jan G. J. van de

doi:10.4049/jimmunol.169.7.3831

Cited by 69 publications

(48 citation statements)

References 52 publications

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“…It has been shown that eosinophils may be activated by secretory IgA not only in an FcαRI-mediated way, but also independently of FcαRI [31, 32, 33]. This is in accord with the role of eosinophils in inflammatory reactions of airway tissue, where secretory IgA is abundant.…”

Section: Discussionsupporting

confidence: 66%

Are Single Nucleotide Polymorphisms of the <i>Immunoglobulin A Fc Receptor</i> Gene Associated with Allergic Asthma?

Jasek

Obojski²,

Mańczak³

et al. 2004

Int Arch Allergy Immunol

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Background: Eosinophils are important components of allergic inflammation. The immunoglobulin A (IgA) Fc receptor (FcαRI), encoded by the FCAR gene, is a possible candidate for eosinophil activation at mucosal surfaces, where IgA is abundant. Both elevated cell surface expression of FcαRI and increased avidity for IgA were described on eosinophils from allergic subjects. The aim of our study was to examine the possible association of FCAR gene polymorphisms with allergic asthma. Methods: We screened three regions of the FCAR gene: (1) the promoter region, (2) exon 3, encoding the first extracellular domain (EC1), and (3) exon 5, coding for the transmembrane and cytoplasmic domain, for new and published polymorphisms using a sensitive temperature gradient gel electrophoresis technique and compared their frequencies in 112 patients diagnosed with allergic asthma and 100 healthy controls. Results: Six polymorphisms, including two novel ones, were detected. No differences between patients and controls were found in the distribution of any of these polymorphisms. Conclusion: FcαRI polymorphism does not seem to be a risk factor in allergic asthma. Nevertheless, this is the first report on the distribution of 6 single nucleotide polymorphisms of the FCAR gene in a human population and the first study on FCAR polymorphism in allergic asthma.

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Section: Discussionsupporting

confidence: 66%

Are Single Nucleotide Polymorphisms of the <i>Immunoglobulin A Fc Receptor</i> Gene Associated with Allergic Asthma?

Jasek

Obojski²,

Mańczak³

et al. 2004

Int Arch Allergy Immunol

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“…SIgA binds Fc␣RI, but, in contrast to mIgA, is unable to trigger Fc␣RI-mediated phagocytosis and requires the presence of the integrin coreceptor Mac-1 (CD11b/CD18) to trigger a respiratory burst via Fc␣RI (58,59). The overlap of Fc␣RI and hpIgR binding sites revealed in this study may account for this difference between SIgA and mIgA.…”

Section: Discussionmentioning

confidence: 69%

Structural Requirements for the Interaction of Human IgA with the Human Polymeric Ig Receptor

Lewis

Pleass

Batten

et al. 2005

The Journal of Immunology

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Transport of polymeric IgA onto mucosal surfaces to become secretory IgA is mediated by the polymeric Ig receptor (pIgR). To study the interaction of human dimeric IgA (dIgA) (the predominant form of IgA polymer) with the human pIgR (hpIgR), we generated recombinant wild-type dIgA1 and dIgA2m(1) and various mutant dIgA1 and analyzed their interaction with a recombinant human secretory component and membrane-expressed hpIgR. We found that wild-type dIgA1 and dIgA2m(1) bound to recombinant human secretory component with similar affinity and were transcytosed by the hpIgR to the same extent. Mutation of the IgA Cα2 domain residue Cys311 to Ser reduced binding to hpIgR, possibly through disruption of noncovalent interactions between the Cα2 domain and domain 5 of the receptor. Within the Cα3 domain of IgA1, we found that combined mutation of residues Phe411, Val413, and Thr414, which lie close to residues previously implicated in hpIgR binding, abolished interaction with the receptor. Mutation of residue Lys377, located very close to this same region, perturbed receptor interaction. In addition, 4 aa (Pro440-Phe443), which lie on a loop at the domain interface and form part of the binding site for human FcαRI, appear to contribute to hpIgR binding. Lastly, use of a monomeric IgA1 mutant lacking the tailpiece revealed that the tailpiece does not occlude hpIgR-binding residues in IgA1 monomers. This directed mutagenesis approach has thus identified motifs lying principally across the upper surface of the Cα3 domain (i.e., that closest to Cα2) critical for human pIgR binding and transcytosis.

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“…63 and 64). Mac-1 has a broad specificity to sugars, including ␤-glucans (65), and has been shown to bind to recombinant SC, either as free SC or in the SIgA complex (62). The physiological roles of serum and SIgA are quite different, and these data show that the presence of the highly glycosylated SC has major effects on the biological functions of SIgA.…”

Section: N-glycans Of Sc Present Many Epitopes For Bacterial Adhesin mentioning

confidence: 99%

Secretory IgA N- and O-Glycans Provide a Link between the Innate and Adaptive Immune Systems

Royle

Roos

Harvey

et al. 2003

Journal of Biological Chemistry

303

327

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Secretory IgA (SIgA) is a multi-polypeptide complex consisting of a secretory component (SC) covalently attached to dimeric IgA containing one joining (J) chain. We present the analysis of both the N-and O-glycans on the individual peptides from this complex. Based on these data, we have constructed a molecular model of SIgA1 with all its glycans, in which the Fab arms form a T shape and the SC is wrapped around the heavy chains. The O-glycan regions on the heavy (H) chains and the SC N-glycans have adhesin-binding glycan epitopes including galactose-linked ␤1-4 and ␤1-3 to GlcNAc, fucoselinked ␣1-3 and ␣1-4 to GlcNAc and ␣1-2 to galactose, and ␣2-3 and ␣2-6-linked sialic acids. These glycan epitopes provide SIgA with further bacteria-binding sites in addition to the four Fab-binding sites, thus enabling SIgA to participate in both innate and adaptive immunity. We also show that the N-glycans on the H chains of both SIgA1 and SIgA2 present terminal GlcNAc and mannose residues that are normally masked by SC, but that can be unmasked and recognized by mannosebinding lectin, by disrupting the SC-H chain noncovalent interactions.

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Mac-1 (CD11b/CD18) as Accessory Molecule for FcαR (CD89) Binding of IgA

Cited by 69 publications

References 52 publications

Are Single Nucleotide Polymorphisms of the <i>Immunoglobulin A Fc Receptor</i> Gene Associated with Allergic Asthma?

Are Single Nucleotide Polymorphisms of the <i>Immunoglobulin A Fc Receptor</i> Gene Associated with Allergic Asthma?

Structural Requirements for the Interaction of Human IgA with the Human Polymeric Ig Receptor

Secretory IgA N- and O-Glycans Provide a Link between the Innate and Adaptive Immune Systems

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