Journal
IMMUNOLOGICAL REVIEWS
Volume 268, Issue 1, Pages 139-159Publisher
WILEY
DOI: 10.1111/imr.12349
Keywords
immunoglobulin; antibody; IgG4; IgG1; Fc receptor
Categories
Funding
- Medical Research Council, UK [G1100090]
- Medical Research Council [G1100090, G1000758B, G0501494] Funding Source: researchfish
- MRC [G0501494, G1100090] Funding Source: UKRI
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IgG4, the least represented human IgG subclass in serum, is an intriguing antibody with unique biological properties, such as the ability to undergo Fab-arm exchange and limit immune complex formation. The lack of effector functions, such as antibody-dependent cell-mediated cytotoxicity and complement-dependent cytotoxicity, is desirable for therapeutic purposes. IgG4 plays a protective role in allergy by acting as a blocking antibody, and inhibiting mast cell degranulation, but a deleterious role in malignant melanoma, by impeding IgG1-mediated anti-tumor immunity. These findings highlight the importance of understanding the interaction between IgG4 and Fc receptors. Despite a wealth of structural information for the IgG1 subclass, including complexes with Fc receptors, and structures for intact antibodies, high-resolution crystal structures were not reported for IgG4-Fc until recently. Here, we highlight some of the biological properties of human IgG4, and review the recent crystal structures of IgG4-Fc. We discuss the unexpected conformations adopted by functionally important C2 domain loops, and speculate about potential implications for the interaction between IgG4 and FcRs.
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