Harnessing IgG Fc glycosylation for clinical benefit

Curr Opin Immunol. 2022 Aug:77:102231. doi: 10.1016/j.coi.2022.102231. Epub 2022 Jul 4.

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.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigen-Antibody Complex / metabolism
  • Glycosylation
  • Humans
  • Immunoglobulin Fc Fragments
  • Immunoglobulin G* / metabolism
  • Polysaccharides
  • Receptors, IgG*

Substances

  • Antigen-Antibody Complex
  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Polysaccharides
  • Receptors, IgG