Immunoglobulin E (IgE)- Definition, Structure and Functions

Immunoglobulin E (IgE) Definition

Immunoglobulin E (IgE) is one of the 5 classes of immunoglobulins, which is defined by the presence of epsilon (ε) heavy chain. It is present in circulation at very low concentrations of less than 1 µg/mL which is approximately 300-fold lower than that of IgG. Although least abundant, it is in many respects the most potent of the various antibody classes found in mammals. It has a half-life of about 2 days in serum. IgE is produced by IgE plasma cells which are present in mucosal areas, especially in the respiratory tract, where the secreted IgE mediates allergic reactions, and the gastrointestinal tract, where it may mediate expulsion of parasitic worm infestations. Although the physiologic role of IgE is not well characterized it is associated mainly with allergic reactions and thought to be involved in defense against parasites, specifically helminths.

Immunoglobulin E (IgE)- Structure and Functions
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Structure of IgE

  • IgE is a glycoprotein produced as a monomeric antibody with two identical heavy chains of the epsilon (ε) class, and two identical Ig light chains. The epsilon (ε) heavy chain has a high (12%) carbohydrate content.
  • The structure has two identical antigen-binding areas consisting of both light and heavy chains and valency of 2.
  • Heavy and light chains have variable regions on their most N terminal ends.
  • Heavy and light chains are subdivided into variable and constant regions. In addition to the disulfide bonds linking the chains together, there are intrachain disulfide links that divide each chain into areas called domains.
  • The light chains have two domains, one variable and one constant.
  • The heavy chains have five domains, one variable, and four constant-region domains. It is unique in having the additional constant region (CH4).
  • CH4 region restricts IgE binding to high-affinity receptors (Fcε-RI) on basophils and mast cells, which contain preformed granules of heparin and histamine.
  • A hinge region is absent.

Functions of IgE

The function of IgE is distinct from other immunoglobulins in that it induces activation of mast cells and basophils through the cell-surface receptor Fc epsilon RI which are high-affinity receptors of The Fc region of IgE.

  • Allergic reactions are predominantly associated with IgE. Antigen reintroduced into a previously sensitized individual binds to antigen-specific IgE on mast cells and triggers the release of the pharmacologically active agents (e.g., histamine) involved in immediate hypersensitivity syndromes such as hay fever and asthma.
  • IgE’s other main functions include providing immunity to parasites such as helminths like Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica. IgE is utilized during immune defense against certain protozoan parasites such as Plasmodium falciparum.
  • IgE also has an essential role in type I hypersensitivity, which manifests in various allergic diseases, such as allergic asthma, most types of sinusitis, allergic rhinitis, food allergies, and specific types of chronic urticaria and atopic dermatitis.
  • IgE also plays a pivotal role in responses to allergens, such as anaphylactic drugs, bee stings, and antigen preparations used in desensitization immunotherapy.
  • High IgE levels indicate that the body is overreacting to allergens leading to an allergic reaction. It can also be a sign that the body is fighting off an infection from a parasite or with some immune system conditions.

References

  1. Amarasekera, M. (2011). Immunoglobulin E in health and disease. Asia Pacific Allergy, 1(1), 12–15. http://doi.org/10.5415/apallergy.2011.1.1.12
  2. https://www.sciencedirect.com/science/article/pii/B9780323069472100094
  3. https://www.mayomedicallaboratories.com/test-catalog/Clinical+and+Interpretive/8159
  4. Lydyard, P.M., Whelan,A.,& Fanger,M.W. (2005).Immunology (2 ed.).London: BIOS Scientific Publishers.
  5. Owen, J. A., Punt, J., & Stranford, S. A. (2013). Kuby Immunology (7 ed.). New York: W.H. Freeman and Company.

About Author

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Sagar Aryal, PhD

Dr. Sagar Aryal is a microbiologist, researcher, and science communicator from Nepal. He is also co-founder and Research Head of the Department of Natural Products at the Kathmandu Research Institute for Biological Sciences (KRIBS), where he leads research on natural product discovery and microbial biodiversity. Dr. Aryal earned his Ph.D. in Microbiology from Tribhuvan University, Kathmandu, Nepal, in 2025, supported by a DAAD Research Grant and a University Grants Commission (UGC) Nepal Ph.D. Fellowship. His research interests include Actinomycetes, Myxobacteria, microbial taxonomy, and natural products, particularly the discovery of bioactive compounds with potential pharmaceutical applications. He isolated and identified Nocardia nepalensis, a novel bacterial species from Nepal, contributing to understanding microbial diversity in the region. Dr. Aryal has published more than 16 research articles in international journals and contributed three book chapters to established academic publications. He has presented scientific research findings and developed international research collaborations through visits to more than 18 countries across Asia, Europe, North America, and Oceania. From 2023 to 2025, he served as the American Society for Microbiology (ASM) Young Ambassador to Nepal. Since December 2025, he has served as an Editorial Board Member of Scientific Reports, a Nature Portfolio journal. In recognition of his scientific contributions, Dr. Aryal received the NAST Science and Technology Youth Award 2025 from the Nepal Academy of Science and Technology. He previously received the Frs. Locke and Stiller Research Award (LSRA) for the 2017-2018 cycle from St. Xavier's College, Kathmandu, and a Nepal Academy of Science and Technology (NAST) Research Grant for 2017-2018. Alongside his scientific career, Dr. Aryal has more than 15 years of experience in blogging, content writing, and search engine optimization (SEO).