Antibody receptors steal the sweet spotlight

J Biol Chem. 2018 Mar 9;293(10):3490-3491. doi: 10.1074/jbc.H118.001955.

Abstract

Immunoglobulin G (IgG) antibodies function, in part, through ligation of cell-surface Fc receptors such as FcγRIIIA (also known as CD16A). IgG glycosylation is known to impact antibody function, but the role of FcγRIIIA glycans, if any, is unclear. Patel et al. now reveal that these glycans do impact protein conformation and IgG affinity and display cell-specific glycosylation patterns, leading to a potential model in which the affinity and possibly function of Fc receptors is dictated by the cell type and its surface glycome.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Glycosylation
  • Humans
  • Immunoglobulin Fc Fragments / metabolism*
  • Immunoglobulin G / metabolism*
  • Killer Cells, Natural / cytology
  • Killer Cells, Natural / immunology
  • Killer Cells, Natural / metabolism*
  • Kinetics
  • Ligands
  • Models, Molecular*
  • Protein Conformation
  • Protein Processing, Post-Translational*
  • Receptors, IgG / agonists*
  • Receptors, IgG / chemistry
  • Receptors, IgG / metabolism

Substances

  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Ligands
  • Receptors, IgG