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- Title
ST6Gal1 in plasma is dispensable for IgG sialylation.
- Authors
Oswald, Douglas M; Lehoux, Sylvain D; Zhou, Julie Y; Glendenning, Leandre M; Cummings, Richard D; Cobb, Brian A
- Abstract
The glycosylation of immunoglobulin G (IgG) has attracted increased attention due to the impact of N -glycan modifications at N297 on IgG function, acting primarily through modulation of Fc domain conformation and Fcγ receptor-binding affinities and signaling. However, the mechanisms regulating IgG glycosylation and especially α2,6-sialylation of its N -glycan remain poorly understood. We observed previously that IgG is normally sialylated in mice with B cells lacking the sialyltransferase ST6Gal1. This supported the hypothesis that IgG may be sialylated outside of B cells, perhaps through the action of hepatocyte-released plasma ST6Gal1. Here, we demonstrate that this model is incorrect. Animals lacking hepatocyte expressed ST6Gal1 retain normal IgG α2,6-sialylation despite the lack of detectable ST6Gal1 in plasma. Moreover, we confirmed that B cells were not a redundant source of IgG sialylation. Thus, while α2,6-sialylation is lacking in IgG from mice with germline ablation of ST6Gal1, IgG α2,6-sialylation is normal in mice lacking ST6Gal1 in either hepatocytes or B cells. These results indicate that IgG α2,6-sialylation arises after release from a B cell but is not dependent on plasma-localized ST6Gal1 activity.
- Subjects
FC receptors; LIVER cells; GERM cells; B cells; IMMUNOGLOBULIN G
- Publication
Glycobiology, 2022, Vol 32, Issue 9, p803
- ISSN
0959-6658
- Publication type
Article
- DOI
10.1093/glycob/cwac039