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Review
. 2022 Aug:77:102231.
doi: 10.1016/j.coi.2022.102231. Epub 2022 Jul 4.

Harnessing IgG Fc glycosylation for clinical benefit

Affiliations
Review

Harnessing IgG Fc glycosylation for clinical benefit

Eva J Archer et al. Curr Opin Immunol. 2022 Aug.

Abstract

The effector activity of IgG antibodies is regulated at several levels, including IgG subclass, modifications of the Fc glycan, and the distribution of Type I and II Fcγ receptors (FcγR) on effector cells. Here, we explore how Fc glycosylation, particularly sialylation and fucosylation, tunes cellular responses to immune complexes. We review the current understanding of the pathways and mechanisms underlying this biology, address FcγR in antigen presentation, and discuss aspects of the clinical understanding of Fc glycans in therapies and disease.

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Conflict of interest statement

Conflict of interest statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Figures

Figure 1
Figure 1
Cartoon representation of the complex, biantennary, N-linked Fc glycan.
Figure 2
Figure 2
Type I and Type II FcγRs. The Type I FcγRs are members of the immunoglobulin super family. The Type II FcγRs are members of the C-type lectin family.

References

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