Molecular characteristics of IgA and IgM Fc binding to the Fc alpha/mu R

スポンサーリンク

概要

• 論文の詳細を見る

• Fc alpha/mu receptor (Fc alpha/mu R), 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 Fc alpha/mu R, the molecular and structural characteristics of the ligand-receptor interactions have been undetermined. Here, we developed twelve monoclonal antibodies (mAbs) against murine Fc alpha/mu R by. P se blocking immunizing mice deficient in Fc alpha/mu R gene. Eight mAbs totally or partially blocked IgA and IgM bindings to Fc alpha/mu R. The mAbs bound to a peptide derived from the Ig-like domain of murine Fc alpha/mu R, which is conserved not only in human and rat Fc alpha/mu R 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 Fc alpha/mu R as well as poly-IgR.

• ACADEMIC PRESS INC ELSEVIER SCIENCEの論文

著者

• Shibuya Kazuko

  Department Of Immunology Institute Of Basic Medical Sciences And Center For Tara Graduate School Of

関連論文

• Quinupristin/dalfopristin and voriconazole controlled Staphylococcus epidermidis pneumonia and chronic necrotizing aspergillosis in a patient with severe lung degradation consequent to multiple treatments for Hodgkin's lymphoma
• Requirement of the tyrosines at residues 258 and 270 of MAIR-I in inhibitory effect on degranulation from basophilic leukemia RBL-2H3
• Requirement of the serine at residue 329 for lipid raft recruitment of DNAM-1 (CD226)
• LFA-1 decreases the antigen dose for T cell activation in vivo
• LFA-1-dependent lipid raft recruitment of DNAM-1 (CD226) in CD4^+ T cell
• Molecular characteristics of IgA and IgM Fc binding to the Fc alpha/mu R
• Functional characterization of DNAM-1 (CD226) interaction with its ligands PVR (CD155) and nectin-2 (PRR-2/CD112)

スポンサーリンク