Impact of differential glycosylation on IgG activity

Adv Exp Med Biol. 2011:780:113-24. doi: 10.1007/978-1-4419-5632-3_10.

Abstract

Immunoglobulin G (IgG) molecules are glycoproteins with dual functionality. While participating in the destruction of virally infected cells or healthy tissues during autoimmune disease, IgG antibodies are also used as a therapeutic agent to suppress IgG-triggered autoimmune disease and inflammation. Research of recent years has put the IgG-associated sugar moiety in the spotlight for regulating these opposing activities. This review will focus on how certain IgG glycovariants impact different IgG-dependent effector functions and how this knowledge might be used to further improve the therapeutic effectiveness of this class of molecules.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylglucosamine / chemistry
  • Acetylglucosamine / immunology
  • Animals
  • Autoimmune Diseases / immunology
  • Autoimmune Diseases / therapy
  • Carbohydrate Sequence
  • Fucose / chemistry
  • Fucose / immunology
  • Galactose / chemistry
  • Galactose / immunology
  • Glycosylation
  • Humans
  • Immunoglobulin Fc Fragments / immunology*
  • Immunoglobulin Fc Fragments / therapeutic use
  • Immunoglobulin G* / immunology
  • Immunoglobulin G* / therapeutic use
  • Immunoglobulin Isotypes / chemistry
  • Immunoglobulin Isotypes / immunology*
  • Inflammation / immunology
  • Inflammation / therapy
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Receptors, IgG / immunology*
  • Sialic Acids / chemistry
  • Sialic Acids / immunology
  • Virus Diseases / immunology
  • Virus Diseases / therapy
  • Virus Diseases / virology

Substances

  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Immunoglobulin Isotypes
  • Receptors, IgG
  • Sialic Acids
  • Fucose
  • Acetylglucosamine
  • Galactose