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Updated: Jan 29, 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
Species-specificity in the interaction of IgE with FcεRI between humans and rats
The interaction of immunoglobulin E (IgE) to its high-affinity receptor (FcεRI) plays a key role in triggering allergic reactions. However, it is still controversial whether species specificity influences the binding ability between humans and rodents. Recombinant hFcεRIα / RBL-2H3 and hFcεRIα / MGC-803 cells were prepared and sensitized with hIgE/anti-hIgE antibody or DNP-IgE/DNP-BSA, respectively. Species-specificity was investigated using immuno-fluorescent analysis, β-hexosaminidase release rate assay, intracellular calcium concentration assay and apoptosis assay, and the results showed that there is species-specificity in IgE/FcεRI in humans and rats, and no cross-recognition between IgE and FcεRI in two species. These results should provide the experimental evidence for further research on the pathogenesis and the drug development of allergic diseases.
The interaction of immunoglobulin E (IgE) to its high-affinity receptor (FcεRI) plays a key role in triggering allergic reactions. However, it is still controversial whether species specificity influences the binding ability between humans and rodents. Recombinant hFcεRIα / RBL-2H3 and hFcεRIα / MGC-803 cells were prepared and sensitized with hIgE/anti-hIgE antibody or DNP-IgE/DNP-BSA, respectively. Species-specificity was investigated using immuno-fluorescent analysis, β-hexosaminidase release rate assay, intracellular calcium concentration assay and apoptosis assay, and the results showed that there is species-specificity in IgE/FcεRI in humans and rats, and no cross-recognition between IgE and FcεRI in two species. These results should provide the experimental evidence for further research on the pathogenesis and the drug development of allergic diseases.
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