Background
Immunoglobulin E (IgE) is an antibody found only in mammals and is synthesized by plasma cells. The monomer of IgE consists of two heavy chains (ε chains) and two light chains, in which the ε chain contains four constant domains of Ig samples (Cε1-Cε4). IgE is considered to be an important part of the immune response against certain parasitic infections, including Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica. IgE also plays an important role in type I hypersensitivity, which is manifested in various allergic diseases, such as allergic asthma, most types of sinusitis, allergic rhinitis, food allergy, and certain types of chronic urticaria and atopic dermatitis. In addition, it also plays a key role in allergen responses, such as drug anaphylaxis, bee bites and antigen preparations for desensitization immunotherapy.
Figure 1. IgE is a heavily glycosylated molecule, with 7 documented N-glycan sites
(Source: Chauhan J, et al. 2020)
IgE initiates IgE-mediated metabolic responses by binding to Fc receptors on the surface of mast cells and basophils. Fc receptors have also been found on human eosinophils, Immunoglobulin E upregulates Fc receptor expression, and antigen binding to already Fc-bound IgE on mast cells leads to cross-linking of bound Ig E and aggregation of latent Fc, resulting in degranulation (release of mediators) and secretion of several types of type 2 cytokines, such as IL(IL)-3 and stem cell factor (SCF), both of which contribute to mast cell survival and accumulation in tissues, and IL-4, IL-5, IL-13, and IL-33, which in turn activate group 2-intrinsic lymphoid cells (ILC2 or natural helper cells). IgE, which can specifically recognize allergens, has a unique long-term interaction with its Fc receptors, so basophils and mast cells that can mediate inflammation will be "activated" and ready to release chemicals such as histamine, leukotriene, and some interleukin.
Allergies are usually diagnosed by reviewing a patient's medical history and finding positive results for allergen-specific IgE during skin or blood tests. Specific IgE test is a confirmed allergy test, but there is no evidence that indiscriminate IgE test or immunoglobulin G (IgG) test can support the diagnosis of allergy.
Alternative Names
Immunoglobulin E positive control
References
- 1. Chauhan J, et al. IgE Antibodies against Cancer: Efficacy and Safety. Antibodies (Basel). 2020 Oct 16;9(4):55.
- 2. Shade KT, et al. IgE Glycosylation in Health and Disease. Curr Top Microbiol Immunol. 2019;423:77-93.
References
IgE Antibodies against Cancer: Efficacy and Safety
Antibodies (Basel)
Authors: Chauhan J, McCraw AJ, Nakamura M, Osborn G, Sow HS, Cox VF, Stavraka C, Josephs DH, Spicer JF, Karagiannis SN, Bax HJ.
Abstract
Immunoglobulin E (IgE) antibodies are well known for their role in allergic diseases and for contributions to antiparasitic immune responses. Properties of this antibody class that mediate powerful effector functions may be redirected for the treatment of solid tumours. This has led to the rise of a new class of therapeutic antibodies to complement the armamentarium of approved tumour targeting antibodies, which to date are all IgG class. The perceived risk of type I hypersensitivity reactions following administration of IgE has necessitated particular consideration in the development of these therapeutic agents. Here, we bring together the properties of IgE antibodies pivotal to the hypothesis for superior antitumour activity compared to IgG, observations of in vitro and in vivo efficacy and mechanisms of action, and a focus on the safety considerations for this novel class of therapeutic agent. These include in vitro studies of potential hypersensitivity, selection of and observations from appropriate in vivo animal models and possible implications of the high degree of glycosylation of IgE. We also discuss the use of ex vivo predictive and monitoring clinical tools, as well as the risk mitigation steps employed in, and the preliminary outcomes from, the first-in-human clinical trial of a candidate anticancer IgE therapeutic.
Aiming to IgE: Drug development in allergic diseases
Int Immunopharmacol
Authors: Ling XJ, Wei JF, Zhu Y
Abstract
The incidence of allergic disease significantly increases in recent decades, causing it become a major public health problem all over the world. The common allergic diseases such as allergic dermatitis, allergy rhinitis, allergic asthma and food allergy are mediated, at least in part, by immunoglobulin E (IgE), and so IgE acts as a central role in allergic diseases. IgE can interact with its high-affinity receptor (FcεRⅠ) which is primarily expressed on tissue-resident mast cells and circulating basophils, initiating intracellular signal transduction and then causing the activation and degranulation of mast cells and basophils. On the other hand, IgE interaction with its low-affinity receptor (CD23), can regulate various IgE-mediated immune responses including IgE-allergen complex presentation, IgE synthesis, the growth and differentiation of both B and T cells, and the secretion of pro-inflammatory mediators. With the deeper mechanism research for allergic diseases, new therapeutic strategies for interfering IgE are developed and receive a great attention. In this review, we summarize a current profile of therapeutic strategies for interfering IgE in allergic diseases. Besides, we suggest that targeting memory B cells (including long-lived plasma cells and (or) IgE+ memory B cells) may help to completely control allergic diseases, and highlight that the development of drugs synergistically aiming to multiple targets can be a better choice for improving treatment efficacy which results from allergic diseases as the systemic disorders caused by an impaired immune system.
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