Characterization of the Ligand Binding Site of the Bovine IgA Fc Receptor (bFcαR)

Morton, H. Craig; Pleass, Richard J.; Woof, Jenny M.; Brandtzæg, Per

doi:10.1074/jbc.m407807200

Cited by 5 publications

(10 citation statements)

References 27 publications

(35 reference statements)

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“…Interestingly, when we mutated conserved residues in the F‐G loop which, by comparison with huCD89, were implicated in boIgA binding, the interaction with boIgA‐coated beads was not abolished in our rosetting assay. Therefore, our data suggested that residues of the B‐C loop, and in particular Y35, contribute more to the IgA binding site than F‐G loop residues 18 …”

Section: Discussionmentioning

confidence: 69%

“…To analyse the surface expression and ligand‐binding properties of eqCD89, we constructed an HA‐tagged variant. We have previously observed that binding of an anti‐HA mAb to an HA‐tagged variant of boCD89 did not affect the IgA binding 18 . Therefore, COS‐1 cells transfected with the HA‐eqCD89 expression vector were first stained with an anti‐HA mAb, followed by an FITC‐labelled secondary reagent.…”

Section: Resultsmentioning

confidence: 99%

“…The tyrosine residue at position 35 (Y35) is critical for this interaction to occur. Y35 is conserved in boCD89, and we have recently shown this residue to be important for IgA binding by the receptor 18 . However, eqCD89 has phenylalanine at the corresponding position (F35).…”

Section: Resultsmentioning

confidence: 99%

“…Recently, we mapped the boIgA binding site in boCD89 and showed that the conserved tyrosine residue at position 35 (Y35) in the B‐C loop is critical 18 . Y35 has likewise been shown to be essential for huCD89–huIgA binding 21 .…”

Section: Discussionmentioning

confidence: 99%

“…We have previously observed that binding of an anti-HA mAb to an HA-tagged variant of boCD89 did not affect the IgA binding. 18 Therefore, COS-1 cells transfected with the HA-eqCD89 expression vector were first stained with an anti-HA mAb, followed by an FITC-labelled secondary reagent. Then the cells with the highest expression of HA-eqCD89 were purified by cell sorting prior to rosetting with immunoglobulin-coated beads.…”

Section: Confirmation That Eqcd89 Is An Eqiga Fcrmentioning

confidence: 99%

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Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques

et al. 2005

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SummaryImmunoglobulin A (IgA) is the major antibody class present in external secretions of mammals. At the vulnerable mucosal surfaces, IgA provides a crucial first-line defence by neutralizing pathogens. Primates also have a substantial level of IgA in serum and although not well understood, the biological role of this IgA depends, at least partly, on its ability to interact with specific receptors (FcaRs) on the surface of leucocytes. The human FcaR, CD89, was the first IgA Fc receptor to be identified and binding of IgA-coated particles to CD89 triggers numerous cellular effector functions, including phagocytosis, antibody-dependent cellular cytotoxicity, and release of inflammatory mediators, all of which may play an important role in both systemic and mucosal immunity. For many years humans were the only species known to express CD89, however, it has recently been cloned from cows and rats. Here, we describe the identification of the CD89 gene in three additional species: horses, chimpanzees, and Rhesus macaques. Equine CD89 was identified at the cDNA level, whereas the chimpanzee and Rhesus macaque genes were identified from the available draft genomic sequence. Interestingly, when compared with humans and other primates, horses, cows and rats have a relatively low concentration of serum IgA, so the role of CD89 in these species is of particular interest. The identification and characterization of CD89 in different species will contribute to a greater understanding of the biological role of IgA and CD89 in mucosal and systemic immunity throughout evolution.

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Section: Discussionmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Confirmation That Eqcd89 Is An Eqiga Fcrmentioning

confidence: 99%

See 3 more Smart Citations

Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques

et al. 2005

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Identification of the linear epitope for Fc‐binding on the bovine IgG2 Fc receptor (boFcγ2R) using synthetic peptides

et al. 2006

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To identify the linear epitope for Fc-binding on the bovine IgG2 Fc receptor (boFcc2R), peptides derived from the membrane-distal extracellular domain (EC1) of boFcc2R corresponding to the homologous region of human FcaRI were synthesized. Binding of bovine IgG2 to the different peptides was tested by Dot-blot assay, and the peptide showing maximal binding was further modified by truncation and mutation. The minimum effective peptide 82 FIGV 85 located in the putative F-G loop of the EC1 domain was found to bind bovine IgG2 specifically and inhibit the binding of bovine IgG2 to the receptor. The Phe 82 , Ile 83 and Val 85 residues within the linear epitope were shown to be critical for IgG2-binding. Such functional epitope peptide should be very useful for understanding the IgG-Fcc interaction and development of FcR-targeting drugs.

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IgA Fc receptors in cattle and horses

Morton

2005

Veterinary Immunology and Immunopathology

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Characterization of the Ligand Binding Site of the Bovine IgA Fc Receptor (bFcαR)

Cited by 5 publications

References 27 publications

Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques

Cloning and characterization of equine CD89 and identification of the CD89 gene in chimpanzees and rhesus macaques

Identification of the linear epitope for Fc‐binding on the bovine IgG2 Fc receptor (boFcγ2R) using synthetic peptides

IgA Fc receptors in cattle and horses

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