| First Author | Cho Y | Year | 2006 |
| Journal | Biochem Biophys Res Commun | Volume | 345 |
| Issue | 1 | Pages | 474-8 |
| PubMed ID | 16681999 | Mgi Jnum | J:109018 |
| Mgi Id | MGI:3625590 | Doi | 10.1016/j.bbrc.2006.04.084 |
| Citation | Cho Y, et al. (2006) Molecular characteristics of IgA and IgM Fc binding to the Fcalpha/muR. Biochem Biophys Res Commun 345(1):474-8 |
| abstractText | Fcalpha/mu receptor (Fcalpha/muR), a novel Fc receptor for IgA and IgM, is a type I transmembrane protein with an immunoglobulin (Ig)-like domain in the extracellular portion. Although IgA and IgM bind to Fcalpha/muR, the molecular and structural characteristics of the ligand-receptor interactions have been undetermined. Here, we developed twelve monoclonal antibodies (mAbs) against murine Fcalpha/muR by immunizing mice deficient in Fcalpha/muR gene. Eight mAbs totally or partially blocked IgA and IgM bindings to Fcalpha/muR. These blocking mAbs bound to a peptide derived from the Ig-like domain of murine Fcalpha/muR, which is conserved not only in human and rat Fcalpha/muR but also in polymeric Ig receptor (poly-IgR), another Fc receptor for IgA and IgM. These results suggest that IgA and IgM bind to an epitope in the conserved amino acids in the Ig-like domain of Fcalpha/muR as well as poly-IgR. |
