Immunoglobulin E (IgE) is the immunoglobulin with the shortest half-life in serum with just 3-5 days. However, the half-life of cell bound IgE is extended to months and even years when IgE is bound to the high affinity IgE receptor (FceRI) on mast cells and basophils. This interaction is particularly relevant in allergy. The crosslinking of IgE bound to FceRI on the surface of mast cells and basophils by allergen triggers a series of intracellular signaling cascades, which culminates in the release of leukotrienes, histamine, and other mediators responsible for the symptoms observed during allergic reactions.
IgE also interacts with CD23, the low-affinity IgE receptor, which is mainly expressed on B cells. CD23 participates in IgE serum clearance as well as in a process known as facilitated allergen presentation, in which IgE-allergen complexes are captured processed and presented on the B cell surface.
Given the relevance of these interactions in allergy, several attempts have been made to modulate the binding of free IgE to its receptors such as omalizumab or ligelizumab (anti-IgE antibodies). Recent lines of research are also trying to develop engineered proteins able to disrupt FceRI-IgE binding without crosslinking the receptor for example by using ankyrin repeated proteins (DARPins). Additionally, IgE can bind to soluble receptors such as Galectin-9, the soluble isoform of Fc?RI and soluble CD23. Recently published studies are exploring the potential use of IgE-receptor complexes and soluble receptor levels as biomarkers or treatment approaches for allergy.
This Research Topic will help to integrate and expand the current understanding of IgE associations with its receptors, mainly FceRI and CD23, and the mechanism behind the modulation and/or disruption of these interactions. A better comprehension of IgE-receptor interactions can lead to the development of new therapies and identification of potential biomarkers for allergy.
Suitable themes for this Research Topic include, but are not limited to:
- Insights into FceRI-IgE and CD23-IgE molecular interaction.
- Regulation and modulation of FceRI-IgE and CD23-IgE interactions
- Signaling downstream of IgE-Fc epsilon receptors.
- Approaches to disrupt IgE binding to its receptors.
- IgE-Fc receptors as biomarkers.
- IgE-Fc receptors and their interaction with co-receptors.
All manuscript types accepted by Frontiers are welcome with an emphasis on original research articles.
Immunoglobulin E (IgE) is the immunoglobulin with the shortest half-life in serum with just 3-5 days. However, the half-life of cell bound IgE is extended to months and even years when IgE is bound to the high affinity IgE receptor (FceRI) on mast cells and basophils. This interaction is particularly relevant in allergy. The crosslinking of IgE bound to FceRI on the surface of mast cells and basophils by allergen triggers a series of intracellular signaling cascades, which culminates in the release of leukotrienes, histamine, and other mediators responsible for the symptoms observed during allergic reactions.
IgE also interacts with CD23, the low-affinity IgE receptor, which is mainly expressed on B cells. CD23 participates in IgE serum clearance as well as in a process known as facilitated allergen presentation, in which IgE-allergen complexes are captured processed and presented on the B cell surface.
Given the relevance of these interactions in allergy, several attempts have been made to modulate the binding of free IgE to its receptors such as omalizumab or ligelizumab (anti-IgE antibodies). Recent lines of research are also trying to develop engineered proteins able to disrupt FceRI-IgE binding without crosslinking the receptor for example by using ankyrin repeated proteins (DARPins). Additionally, IgE can bind to soluble receptors such as Galectin-9, the soluble isoform of Fc?RI and soluble CD23. Recently published studies are exploring the potential use of IgE-receptor complexes and soluble receptor levels as biomarkers or treatment approaches for allergy.
This Research Topic will help to integrate and expand the current understanding of IgE associations with its receptors, mainly FceRI and CD23, and the mechanism behind the modulation and/or disruption of these interactions. A better comprehension of IgE-receptor interactions can lead to the development of new therapies and identification of potential biomarkers for allergy.
Suitable themes for this Research Topic include, but are not limited to:
- Insights into FceRI-IgE and CD23-IgE molecular interaction.
- Regulation and modulation of FceRI-IgE and CD23-IgE interactions
- Signaling downstream of IgE-Fc epsilon receptors.
- Approaches to disrupt IgE binding to its receptors.
- IgE-Fc receptors as biomarkers.
- IgE-Fc receptors and their interaction with co-receptors.
All manuscript types accepted by Frontiers are welcome with an emphasis on original research articles.
