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. 2016 Nov 25;18(1):274.
doi: 10.1186/s13075-016-1172-1.

Fab glycosylation of immunoglobulin G does not associate with improvement of rheumatoid arthritis during pregnancy

Albert Bondt  1   2 , Manfred Wuhrer  2 , T Martijn Kuijper  1 , Johanna M W Hazes  1 , Radboud J E M Dolhain  3
Affiliations

Fab glycosylation of immunoglobulin G does not associate with improvement of rheumatoid arthritis during pregnancy

Albert Bondt et al. Arthritis Res Ther. .

Abstract

Background: Changes in immunoglobulin G (IgG) constant domain (Fc) glycosylation are associated with changes in rheumatoid arthritis (RA) disease activity in response to pregnancy. Here, we sought to determine whether the same holds true for variable domain (Fab) glycosylation.

Methods: IgGs were captured from RA and control sera obtained before (RA only), during and after pregnancy, followed by Fc and Fab separation, glycan release, and mass spectrometric detection. In parallel, glycans from intact IgG were analysed. The data was used to calculate glycosylation traits, and to estimate the level of Fab glycosylation.

Results: The overall level of Fab glycosylation was increased in RA patients compared to controls, while no differences in Fab glycosylation patterns were found. For the Fc and intact IgG (Total) previously observed differences in galactosylation and bisection were confirmed. Furthermore, increased galactosylation of Fc and Total were associated with lower disease activity and autoantibody positivity. In addition, the change in Fc galactosylation associated with the change in disease activity during pregnancy and after delivery, while this was not the case for Fab.

Conclusions: In contrast to changes in Fc glycosylation, changes in Fab glycosylation are not associated with improvement of RA during pregnancy and arthritis flare after delivery.

Keywords: Disease activity; Inflammation; Pregnancy; Rheumatoid arthritis.

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Figures

Fig. 1
Fig. 1
Schematic representation of immunoglobulin G. Indicated is what is generally considered as the Fc and Fab or F(ab’)2 portion. The glycans of both Fc and Fab consist of the same building blocks, although the most abundant glycans may differ vastly in their appearance. This figure was originally published in Bondt et al, Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes. Mol Cell Proteomics. 2014; 13:3029–3039. © the American Society for Biochemistry and Molecular Biology, and slightly adapted for the current manuscript
Fig. 2
Fig. 2
Fc and Fab galactosylation and sialylation in RA and healthy controls. The percentages of galactosylation (yellow circle) and sialylation (purple diamond) on the Fc show a clear increase during pregnancy (from pre-conception to the 3rd trimester; RA only) and decrease after delivery (from 3rd trim to 26 weeks postpartum), as well as differences between cases and controls. No differences between cases and controls, and only minor pregnancy-associated changes were observed for the Fab glycosylation. Abbreviations: pre-conc pre-conception, trim trimester, wkpp weeks postpartum
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