Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G.

Glycoconjugate Journal
Helga K EinarsdottirManfred Wuhrer

Abstract

Human immunoglobulin G (IgG) molecules are composed of two Fab portions and one Fc portion. The glycans attached to the Fc portions of IgG are known to modulate its biological activity as they influence interaction with both complement and various cellular Fc receptors. IgG glycosylation changes significantly with pregnancy, showing a vast increase in galactosylation and sialylation and a concomitant decrease in the incidence of bisecting GlcNAc. Maternal IgGs are actively transported to the fetus by the neonatal Fc receptor (FcRn) expressed in syncytiotrophoblasts in the placenta, providing the fetus and newborn with immunological protection. Two earlier reports described significant differences in total glycosylation between fetal and maternal IgG, suggesting a possible glycosylation-selective transport via the placenta. These results might suggest an alternative maternal transport pathway, since FcRn binding to IgG does not depend on Fc-glycosylation. These early studies were performed by releasing N-glycans from total IgG. Here, we chose for an alternative approach analyzing IgG Fc glycosylation at the glycopeptide level in an Fc-specific manner, providing glycosylation profiles for IgG1 and IgG4 as well as combined Fc glyc...Continue Reading

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Citations

Jan 30, 2014·Journal of Mammary Gland Biology and Neoplasia·Craig R Baumrucker, Rupert M Bruckmaier
Feb 6, 2014·Immunology Letters·Rick KapurGestur Vidarsson
Oct 14, 2014·Frontiers in Immunology·Matthew Aaron PettengillOfer Levy
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Nov 5, 2021·Frontiers in Immunology·Kristina Zlatina, Sebastian P Galuska

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Methods Mentioned

BETA
glycosylation
electrophoresis
galactosylation

Software Mentioned

Excel
Bruker DataAnalysis
Xtractor2D
msalign2

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