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Updated: Mar 15, 2026
Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI
Published on: November 1, 2014
Cloning and Characterization of the IgA Fc Receptor from Swine
Yumei Chen1,2, Yunchao Liu1, Gaiping Zhang1,3
1Henan Provincial Key Laboratory of Animal Immunology, Henan Academy of Agricultural Sciences, Zhengzhou 450002, P.R. China.
Abstract:
The myeloid-specific IgA Fc receptor (FcαR) is a cell surface molecule on immunocytes that provides a fundamental connection between humoral and cellular immunity. In this study, the full-length cDNA sequence of swine FcαRI (swFcαRI) was isolated and characterized and found to contain a 792-base-pair open reading frame, encoding a 264-amino-acid transmembrane glycoprotein with a predicted molecular mass of 29.4 kDa. The swFcαRI shares high amino acid sequence homology (>50%) with its counterparts from cattle, seal, and horse. Rosetting analysis confirmed that COS-7 cells transfected with an swFcαRI expression plasmid was able to combine with chicken erythrocytes sensitized with porcine IgA, but not IgG.
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