The Fc region of immunoglobulin E (IgE) comprising the Cε3 and Cε4 domains (residues 329–547) is sufficient for binding to the high-affinity IgE Fc receptor (FcεRIα). Three potential N-linked glycosylation sites are present within the Cε3 domain. To determine the effect of the glycosylation sites on IgE Fc synthesis and on FcεRIα binding, site-directed mutagenesis was performed. Mutant IgE Fc constructs were expressed in COS cells and analyzed for protein synthesis and secretion, and FcεRIα binding activity. We find that only N371 and N394 are glycosylated, and that the residues surrounding the glycosylation site at N394 are required for FcεRIα binding activity.

Keywords:
Immunoglobulin F (IgF), Fc domain, I high affinity IgE receptor (FcεRI), Mast cells, Glycosylation
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© 1995 S. Karger AG, Basel
1995
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