Identification of Amino Acid Residues in Human IgM Fc Receptor (FcµR) Critical for IgM Binding.

ABSTRACT: Both non-immune "natural" and antigen-induced "immune" IgM are important for protection against infections and for regulation of immune responses to self-antigens. The roles of its Fc receptor (FcµR) in these IgM effector functions have begun to be explored. In the present study, by taking advantage of the difference in IgM-ligand binding of FcµRs of human (constitutive binding) and mouse (transient binding), we replaced non-conserved amino acid residues of human FcµR with mouse equivalents before establishment of cell lines stably expressing mutant or wild-type (WT) receptors. The resultant eight-different mutant FcµR-bearing cells were compared with WT receptor-bearing cells for cell-surface expression and IgM-binding by flow cytometric assessments using receptor-specific mAbs and IgM pa

SUBMITTER: Skopnik CM 

PROVIDER: S-EPMC7873564 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature