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The clinical significance of allergen-specific IgG4 in allergic diseases

Qin, Lu, Tang, Lan-Fang, Cheng, Lei, Wang, Hui-Ying·2022·Frontiers in Immunology
DOI 10.3389/fimmu.2022.1032909PMC PMC9648126
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Abstract

IgG4 is a subclass of IgG antibody with a unique molecular feature of (Fragment antigen- binding) Fab-arm exchange, allowing bi specific antigen binding in a mono -valent manner. With low binding affinity to C1q and Fcγreceptors, IgG4 is incapable of forming immune complexes and activating the complement pathway, exhibiting a non-inflammatory feature. IgG4 is produced similarly to IgE and is considered a modified reaction to IgE class-switching response under certain conditions. It could also counteract IgE-activated inflammation. However, the clinical significance of IgG4 in allergic diseases is complex and controversial. Three viewpoints have been suggested to describe the role of IgG4. IgG4 can act as a tolerance–inducer to play a protective role under repeated and rapid incremental dosing of allergen exposure in allergen immunotherapy (AIT), supported by allergies in cat raisers and venom desensitization in beekeepers. Another viewpoint accepted by mainstream specialists and guidelines of Food Allergy and Management in different countries points out that food-specific IgG4 is a bystander in food allergy and should not be used as a diagnostic tool in clinical work. However, eosinophilic esophagitis (EoE) investigation revealed a direct clinical relevance between physiopathology and serum IgG4 in cow milk and wheat. These factors indicate that allergen-specific IgG4 plays a multifaceted role in allergic diseases that is protective or pathogenic depending on different allergens or exposure conditions.

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Figure 1 Structure of IgG4 antibody and Fab-arm exchange. (A) Inter- and intra-chain disulfide bonds give structure to IgG4. (B) Antibodies separate into ‘half-molecules’, each comprising one heavy and one light chain. Half-molecules recombine to form bi-specific antibodies.
Figure 1 Structure of IgG4 antibody and Fab-arm exchange. (A) Inter- and intra-chain disulfide bonds give structure to IgG4. (B) Antibodies separate into ‘half-molecules’, each comprising one heavy and one light chain. Half-molecules recombine to form bi-specific antibodies.CC BY · PubMed Central
Figure 2 The role of allergen-specific IgG4 in allergen exposure. (A) Acute allergen exposure may lead to IgE-mediated histamine-induced hypersensitivity reactions by high-affinity receptor FcϵRI. (B) Chronic allergen exposure may induce IgG4 formation and allergen binding by IgG4, thereby binds to the inhibitory receptor FcγRIIb which prevents hypersensitivity reactions and induces allergen tolerance.
Figure 2 The role of allergen-specific IgG4 in allergen exposure. (A) Acute allergen exposure may lead to IgE-mediated histamine-induced hypersensitivity reactions by high-affinity receptor FcϵRI. (B) Chronic allergen exposure may induce IgG4 formation and allergen binding by IgG4, thereby binds to the inhibitory receptor FcγRIIb which prevents hypersensitivity reactions and induces allergen tolerance.CC BY · PubMed Central

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Metadata

Authors
Qin, L., Tang, L.-F., Cheng, L., & Wang, H.-Y.
Venue
Frontiers in Immunology
Publisher
Frontiers Media SA
Published
2022-10-25
Volume
13
ISSN
1664-3224
DOI
10.3389/fimmu.2022.1032909
PMC
PMC9648126
Cited by
71
References
1
Licence
creativecommons.org/licenses/by/4.0/ (vor)
Funders
  • National Natural Science Foundation of China
  • Zhejiang Provincial Program for the Cultivation of High-Level Innovative Health Talents

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CoChat. (2026). Citation check: The clinical significance of allergen-specific IgG4 in allergic diseases. https://app.cochat.ai/papers/10.3389/fimmu.2022.1032909
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Qin, L., Tang, L.-F., Cheng, L., & Wang, H.-Y. (2022). The clinical significance of allergen-specific IgG4 in allergic diseases. Frontiers in Immunology. https://doi.org/10.3389/fimmu.2022.1032909