TY - JOUR
T1 - IgE, IgE Receptors and Anti-IgE Biologics: Protein Structures and Mechanisms of Action
AU - McDonnell, James
AU - Sutton, Brian
AU - Gould, Hannah
N1 - Funding Information:
The authors acknowledge support by Asthma UK (AUK-09/029), the Biotechnology and Biological Sciences Research Council UK (BB/P000436, BB/K501815), the Medical Research Council UK (G0501494, G1100090), and theWellcome Trust (076343).
Publisher Copyright:
© 2023 Annual Reviews Inc.. All rights reserved.
PY - 2023/4/26
Y1 - 2023/4/26
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85159247009&partnerID=8YFLogxK
U2 - doi: 10.1146/annurev-immunol-061020-053712
DO - doi: 10.1146/annurev-immunol-061020-053712
M3 - Review article
SN - 0732-0582
VL - 41
SP - 255
EP - 275
JO - Annual Review of Immunology
JF - Annual Review of Immunology
ER -