Abstract
Immunoglobulin G (IgG) molecules are glycoproteins with dual functionality. While participating in the destruction of virally infected cells or healthy tissues during autoimmune disease, IgG antibodies are also used as a therapeutic agent to suppress IgG-triggered autoimmune disease and inflammation. Research of recent years has put the IgG-associated sugar moiety in the spotlight for regulating these opposing activities. This review will focus on how certain IgG glycovariants impact different IgG-dependent effector functions and how this knowledge might be used to further improve the therapeutic effectiveness of this class of molecules.
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Acknowledgements
This work was supported by grants from the German Research Foundation (SFB 643, FOR832, GK1660, SPP1468) and the Bavarian Genome Research Network (BayGene) to F.N. We apologize to all colleagues whose important work could not be cited directly due to limitation in space. These references can be found in the review articles referred to in this manuscript.
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Lux, A., Nimmerjahn, F. (2011). Impact of Differential Glycosylation on IgG Activity. In: Pulendran, B., Katsikis, P., Schoenberger, S. (eds) Crossroads between Innate and Adaptive Immunity III. Advances in Experimental Medicine and Biology, vol 780. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-5632-3_10
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DOI: https://doi.org/10.1007/978-1-4419-5632-3_10
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