Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23

Ilkow, V.F.; Davies, Anna M.; Dhaliwal, B.; Beavil, Andrew J.; Sutton, Brian J.; McDonnell, James M.

doi:10.1002/2211-5463.13214

Cited by 2 publications

(2 citation statements)

References 61 publications

(135 reference statements)

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“…The crystal structures of murine and bovine derCD23 were recently determined. In contrast to human derCD23, bovine and murine deCD23 molecules bind Ca 2+ at both the principal and auxiliary binding sites (50,51). Interestingly, in human derCD23 residue Asp258 forms part of the defunct auxiliary binding site.…”

Section: Calcium Modulates the Ige/cd23 Interactionmentioning

confidence: 95%

IgE, IgE Receptors and Anti-IgE Biologics: Protein Structures and Mechanisms of Action

McDonnell

Dhaliwal

Sutton

et al. 2023

Annu. Rev. Immunol.

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The evolution of IgE in mammals added an extra layer of immune protection at body surfaces to provide a rapid and local response against antigens from the environment. The IgE immune response employs potent expulsive and inflammatory forces against local antigen provocation, at the risk of damaging host tissues and causing allergic disease. Two well-known IgE receptors, the high-affinity FcεRI and low-affinity CD23, mediate the activities of IgE. Unlike other known antibody receptors, CD23 also regulates IgE expression, maintaining IgE homeostasis. This mechanism evolved by adapting the function of the complement receptor CD21. Recent insights into the dynamic character of IgE structure, its resultant capacity for allosteric modulation, and the potential for ligand-induced dissociation have revealed previously unappreciated mechanisms for regulation of IgE and IgE complexes. We describe recent research, highlighting structural studies of the IgE network of proteins to analyze the uniquely versatile activities of IgE and anti-IgE biologics. Expected final online publication date for the Annual Review of Immunology, Volume 41 is April 2023. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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Section: Calcium Modulates the Ige/cd23 Interactionmentioning

confidence: 95%

IgE, IgE Receptors and Anti-IgE Biologics: Protein Structures and Mechanisms of Action

McDonnell

Dhaliwal

Sutton

et al. 2023

Annu. Rev. Immunol.

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“…However, the stalk region might also be directly involved in IgE binding ( 84 ). One reason for the glycan-independent binding in humans may be that human CD23 does not bind Ca 2+ in the classical C-type lectin site, which appears to make it unable to interact with carbohydrates ( 2 , 85 ). However, the presence of Ca 2+ may still influence the binding to IgE because Ca 2+ affects the structure of CD23 and hence enhances the binding ( 86 ).…”

Section: Fcεrii (Cd23): a C-type Lectin Receptormentioning

confidence: 99%

On the complexity of IgE: The role of structural flexibility and glycosylation for binding its receptors

2023

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It is well established that immunoglobulin E (IgE) plays a crucial role in atopy by binding to two types of Fcε receptors (FcεRI and FcεRII, also known as CD23). The cross-linking of FcεRI-bound IgE on effector cells, such as basophils and mast cells, initiates the allergic response. Conversely, the binding of IgE to CD23 modulates IgE serum levels and antigen presentation. In addition to binding to FcεRs, IgE can also interact with other receptors, such as certain galectins and, in mice, some FcγRs. The binding strength of IgE to its receptors is affected by its valency and glycosylation. While FcεRI shows reduced binding to IgE immune complexes (IgE-ICs), the binding to CD23 is enhanced. There is no evidence that galectins bind IgE-ICs. On the other hand, IgE glycosylation plays a crucial role in the binding to FcεRI and galectins, whereas the binding to CD23 seems to be independent of glycosylation. In this review, we will focus on receptors that bind to IgE and examine how the glycosylation and complexation of IgE impact their binding.

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Reviving lost binding sites: Exploring calcium‐binding site transitions between human and murine CD23

Abstract: CTLD, C-type lectin-like domain; derCD23, a soluble fragment of CD23 cleaved by the house dust mite protease Der p 1; Fcε3-4, sub-fragment of IgE-Fc consisting of the dimer of Cε3 and Cε4 domains, MBL, mannose-binding lectin; PDB, Protein Data Bank.

Cited by 2 publications

References 61 publications

IgE, IgE Receptors and Anti-IgE Biologics: Protein Structures and Mechanisms of Action

IgE, IgE Receptors and Anti-IgE Biologics: Protein Structures and Mechanisms of Action

On the complexity of IgE: The role of structural flexibility and glycosylation for binding its receptors

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