Immunoglobulin E makes up the lowest serum concentration of all isotypes, but it is strongly potent, being associated with mediating hypersensitivity and allergic reactions, in addition to having roles in antiparasitic activity, autoimmune processes, and venom protection.
Since IgE is a monomer composed of two epsilon-heavy chains and light chains, it can only bind two antigens, but the structure of their heavy chain C-terminal regions is crucial for the binding to high-affinity cellular receptor Fc-epsilon R1 and low-affinity CD23.1
FcɛRI is expressed on mast cells, basophils, Langerhans cells, and eosinophils, with circulating IgE upregulating FcɛR expression on these cells. This expression and upregulation are what allows the highly potent IgE to be responsible for immediate hypersensitivity reactions, parasitic immunity, enhanced cytokine production, and antigen presentation. This ultimately results in cellular degranulation and the release of vasoactive and pro-inflammatory mediators.2,3
On the other hand, CD23 is mainly expressed on B-cells, T-cells, and antigen-presenting cells, and manages IgE production homeostasis, facilitated antigen presentation, and IgE transportation through airway and gut epithelial cells.2
Recently, research into anti-IgE antibodies as therapy for allergy and asthma has been increasing, with antibodies being designed to target free IgE and membrane-bound IgE. As of now, the monoclonal antibody omalizumab is the only licensed anti-IgE therapy available for clinical use in allergic asthma and chronic spontaneous urticaria. Other drugs in development include ligelizumab, which demonstrates improvements to IgE binding, production and basophil activation compared to omalizumab. Furthermore, IgE antibody MOv18 has shown potential for cancer therapy.4
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Schroeder, H. W., & Cavacini, L. (2010). Structure and Function of Immunoglobulins. The Journal of Allergy and Clinical Immunology, 125(2 0 2), S41. https://doi.org/10.1016/J.JACI.2009.09.046
Godwin, L., Sinawe, H., & Crane, J. S. (2022). Biochemistry, Immunoglobulin E. StatPearls. https://www.ncbi.nlm.nih.gov/books/NBK541058/
Gasser, P., Tarchevskaya, S. S., Guntern, P., Brigger, D., Ruppli, R., Zbären, N., Kleinboelting, S., Heusser, C., Jardetzky, T. S., & Eggel, A. (2020). The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab. Nature Communications 2020 11:1, 11(1), 1–14. https://doi.org/10.1038/s41467-019-13815-w
Spicer, J., Basu, B., Montes, A., Banerji, U., Kristeleit, R., Miller, R., Veal, G. J., Corrigan, C. J., Till, S. J., Figini, M., Canevari, S., Barton, C., Jones, P., Mellor, S., Carroll, S., Selkirk, C., Nintos, G., Kwatra, V., Funingana, I. G., … Karagiannis, S. N. (2023). Safety and anti-tumour activity of the IgE antibody MOv18 in patients with advanced solid tumours expressing folate receptor-alpha: a phase I trial. Nature Communications 2023 14:1, 14(1), 1–11. https://doi.org/10.1038/s41467-023-39679-9
Antibody specificity refers to an antibody's ability to selectively bind to a unique epitope on a target antigen while avoiding interactions with unrelated antigens. This property arises from the highly specialized antigen-binding site located in the variable region of the antibody, which determines its unique binding characteristics.
Antibody affinity refers to the strength of the binding interaction between a single antigen epitope and the paratope (binding site) of an antibody. This interaction is a fundamental measure of how well an antibody recognizes its specific antigen target.
Recombinant antibodies are produced using genetic engineering techniques, unlike traditional antibody production, where the immune system generates antibodies without direct control over their sequence. By introducing genes encoding antibody fragments into host cells, such as bacteria or mammalian cells, recombinant antibodies can be expressed, purified, and deployed for applications including research, diagnostics, and therapeutics.
Recombinant antibody expression is a biotechnological process that involves engineering and producing antibodies outside their natural context using recombinant DNA technology.
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