Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcɛRI.
Abstract: The binding of immunoglobulin E (IgE) to its high-affinity receptor (FcɛRI) is the central protein interaction in IgE-mediated allergic reactions. The cross-linking of the IgE/FcɛRI complex, through cognate allergens, on the surface of mast cells and basophil cells results in mediator release, and thus leads to the symptoms of type I hypersensitivity responses in mammals. To develop a baseline value for subsequent equine anti-allergy drug and vaccine research, the interaction of equine IgE with its high-affinity FcɛRI receptor was investigated following the cloning and expression of equine IgE with specificity for NIP-HSA (4-hydroxy-5-iodo-3-nitrophenylacetic acid conjugated to human serum albumin). Receptor recognition and effector functions were assessed in Rat Basophil Leukemia (RBL-2H3.1) cells transfected with the α chain of equine and canine FcɛRI. Results obtained showed that the equine FcɛRI receptor recognizes both equine and canine IgE and supports similar β-hexosaminidase release levels from RBL cells transfected with equine FcɛRI, peaking at 36.68% at 100ngml(-1) antigen and 32.00% at 100ngml(-1) antigen respectively. Furthermore, the binding kinetics of the equine IgE to the equine FcɛRI receptor and the canine IgE to the same receptor was measured to be KA=6.33×10(9)M(-1) and KA=1.84×10(9)M(-1) respectively. This research established basic reagents and vitro assay systems to underpin the development of rational therapeutic intervention strategies to combat equine allergic manifestations.
Copyright © 2013 Elsevier B.V. All rights reserved.
Publication Date: 2013-02-11 PubMed ID: 23485176DOI: 10.1016/j.vetimm.2013.01.008Google Scholar: Lookup
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- Journal Article
Summary
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This is a study that investigates the interaction between the horse’s Immunoglobulin E (IgE) and its high-affinity receptor (FcɛRI). The research lays the groundwork for future development of anti-allergy medications and vaccines for horses.
Objective of the Research
- The central purpose of this study was to understand the interaction of Immunoglobulin E (IgE) with its high-affinity receptor, FcɛRI, in horses. This interaction forms the bedrock of IgE-mediated allergic reactions. A deep understanding of this reaction can form the basis for subsequent equine anti-allergy drug and vaccine research.
Methodology
- Researchers cloned and expressed equine IgE with specificity for NIP-HSA, a compound known to cause allergic reactions.
- The interaction of this IgE with its high-affinity FcɛRI receptor was then assessed by measuring receptor recognition and effector functions in Rat Basophil Leukemia (RBL-2H3.1) cells. The RBL cells were transfected with the α chain of equine and canine FcɛRI. The transfected RBL cells serve as a simplified model system to mimic the allergic reactions that could happen in real biological systems.
Findings
- The study demonstrated that the equine FcɛRI receptor recognizes both equine and canine IgE, suggesting an interspecies consistency in allergic reactions at the molecular level.
- Further, the transfected RBL cells exhibited similar β-hexosaminidase release levels when they interacted with equine FcɛRI. β-Hexosaminidase release is an indicator of allergic reaction or hypersensitivity; thus, the similar release levels imply that the allergenic response was generated as expected.
- The study also established the binding kinetics of the equine IgE to the equine FcɛRI receptor, providing a quantifiable basis for future studies.
Implications
- The findings give insights into the IgE-related allergic reactions in horses, facilitating the development of effective anti-allergy medications and vaccines for equines.
- Moreover, the successful vitro assay systems developed can be used as reference models in related research, expediting the overall progress in resolving equine allergic manifestations.
Cite This Article
APA
Sabban S, Ye H, Helm B.
(2013).
Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcɛRI.
Vet Immunol Immunopathol, 153(1-2), 10-16.
https://doi.org/10.1016/j.vetimm.2013.01.008 Publication
Researcher Affiliations
- The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, UK. sari.sabban@gmail.com
MeSH Terms
- Animals
- Cell Line, Tumor
- Dogs
- Horses / immunology
- Immunoglobulin E / metabolism
- Rats
- Receptors, IgE / metabolism
- Surface Plasmon Resonance
- beta-N-Acetylhexosaminidases / metabolism
Citations
This article has been cited 5 times.- Lauritano D, Mastrangelo F, D'Ovidio C, Ronconi G, Caraffa A, Gallenga CE, Frydas I, Kritas SK, Trimarchi M, Carinci F, Conti P. Activation of Mast Cells by Neuropeptides: The Role of Pro-Inflammatory and Anti-Inflammatory Cytokines. Int J Mol Sci 2023 Mar 2;24(5).
- Prakash PS, Barwary NJS, Weber MHW, Wan D, Conejeros I, Pereira Moreira B, Alharbi WS, van Hellemond JJ, Akinwale J, Falcone FH. The Humanised NPY-mRFP RBL Reporter Cell Line Is a Fast and Inexpensive Tool for Detection of Allergen-Specific IgE in Human Sera. Diagnostics (Basel) 2022 Aug 25;12(9).
- Prakash PS, Weber MHW, van Hellemond JJ, Falcone FH. Are humanized IgE reporter systems potential game changers in serological diagnosis of human parasitic infection?. Parasitol Res 2022 Apr;121(4):1137-1144.
- Ali EA, Kalli M, Wan D, Nakamura R, Onion D, Alanine DGW, Alcocer MJC, Falcone FH. Characterization of human FcεRIα chain expression and gene copy number in humanized rat basophilic leukaemia (RBL) reporter cell lines. PLoS One 2019;14(8):e0221034.
- Sabban S, Ye H, Helm B. Development of an in vitro model system for studying the interaction of Equus caballus IgE with its high-affinity receptor FcεRI. J Vis Exp 2014 Nov 1;(93):e52222.
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