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Glycobiology, Volume 30, Issue 4, April 2020, Pages 226–240, https://doi.org/10.1093/glycob/cwz048
The content of this slide may be subject to copyright: please see the slide notes for details.
Fig. 1 Schematic representation of the glycosylation sites of IgG,
IgA, IgD, IgE and IgM. The IgG glycosylation ...

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Figure.pptx

  • 1. Glycobiology, Volume 30, Issue 4, April 2020, Pages 226–240, https://doi.org/10.1093/glycob/cwz048 The content of this slide may be subject to copyright: please see the slide notes for details. Fig. 1 Schematic representation of the glycosylation sites of IgG, IgA, IgD, IgE and IgM. The IgG glycosylation ...

Editor's Notes

  1. Fig. 1 Schematic representation of the glycosylation sites of IgG, IgA, IgD, IgE and IgM. The IgG glycosylation sites are indicated by their amino acid number according to literature, e.g. Arnold et al. 2007 and Plomp et al. 2015, while the other isotypes follow UniProt numbering (for an overview of Ig glycosylation site nomenclature, see Plomp et al. 2016). Each Ig monomer is composed of two heavy chains (dark gray) and two light chains (light gray), connected by disulfide bonds. The chains are further subdivided as constant (C) and variable (V) domains. Polyclonal immunoglobulins may carry additional occupied glycosylation sites in their (hyper) variable regions in the Fab domain, which are not indicated in this figure. *IgA2 is shown in its dimeric form and in complex with the joining chain (JC; red) and the secretory component (SC; blue; present only for secretory IgA), both linked via disulfide bonds. Although not shown here, also IgA1 can form dimers, while IgM generally forms pentamers, both in combination with one joining chain. #N92 on IgA2 is only incorporated in an N-glycosylation consensus sequence in the IgAn and IgA2m(2) allotypes; N92 in IgA2m(1) is not glycosylated (Plomp et al. 2018; Chandler et al. 2019). $Although N264 of IgE is part of an N-glycosylation consensus sequence (NHS), this site was reported to be non-glycosylated when studied at the glycopeptide level (Plomp et al. 2014; Wu et al. 2016). ¥There are nine potential O-glycosylation sites present in the hinge region of IgD (S109, S10, T113, S121, T126, T127, T131, T131 and T135) for which different occupancies have been reported (Takayasu et al. 1982; Mellis and Baenziger 1983). §IgM N440 was reported to have a 30–40% site occupancy when derived from human plasma (Chandler et al. 2019). The green–blue–yellow structures at the glycosylation sites represent the presence of mainly complex type N-glycans, while the green–blue structures represent the presence of mainly high-mannose type N-glycans. The yellow–pink structures indicate the presence of O-glycosylation. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press.This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com