Fc-Glycosylation in Human IgG1 and IgG3 Is Similar for Both Total and Anti-Red-Blood Cell Anti-K Antibodies
Myrthe E. Sonneveld; Myrthe E. Sonneveld; Carolien A. M. Koeleman; H. Rosina Plomp; Manfred Wuhrer; C. Ellen van der Schoot; C. Ellen van der Schoot; Gestur Vidarsson · 2018 · Frontiers in Immunology
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Abstract
After albumin, immunoglobulin G (IgG) are the most abundant proteins in human serum, with IgG1 and IgG3 being the most abundant subclasses directed against protein antigens. The quality of the IgG-Fc-glycosylation has important functional consequences, which have been found to be skewed toward low fucosylation in some antigen-specific immune responses. This increases the affinity to IgG1-Fc-receptor (FcγR)IIIa/b and thereby directly affects downstream effector functions and disease severity. To date, antigen-specific IgG-glycosylation have not been analyzed for IgG3. Here, we analyzed 30 pregn
Abstract by Myrthe E. Sonneveld; Myrthe E. Sonneveld; Carolien A. M. Koeleman; H. Rosina Plomp; Manfred Wuhrer; C. Ellen van der Schoot; C. Ellen van der Schoot; Gestur Vidarsson, Frontiers in Immunology (2018) — licensed CC BY 4.0.
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Metadata source: DOAJ · DOI 10.3389/fimmu.2018.00129