Harnessing IgG Fc glycosylation for clinical benefit
- PMID: 35797920
- PMCID: PMC9870045
- DOI: 10.1016/j.coi.2022.102231
Harnessing IgG Fc glycosylation for clinical benefit
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.
Copyright © 2022. Published by Elsevier Ltd.
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
References
-
- Nimmerjahn F, Ravetch JV: Divergent immunoglobulin g subclass activity through selective Fc receptor binding. Science 2005, 310:1510–1512. - PubMed
-
Demonstrated differential affinities of IgG subclasses for activating vs inhibitor Fc receptors, the activating/inhibitory ratio.
-
- Anthony RM, Nimmerjahn F: The role of differential IgG glycosylation in the interaction of antibodies with FcγRs in vivo. Curr Opin Organ Transplant 2011, 16:7–14. - PubMed
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
