Sweet SIGNs: IgG glycosylation leads the way in IVIG-mediated resolution of inflammation

Int Immunol. 2017 Dec 30;29(11):499-509. doi: 10.1093/intimm/dxx053.

Abstract

A hallmark of many chronic inflammatory and autoimmune diseases is that there is an impaired resolution of inflammation and return to the steady state. The infusion of high doses of pooled serum IgG preparations from thousands of donors [intravenous immunoglobulin (IVIG) therapy] has been shown to induce resolution of inflammation in a variety of chronic inflammatory and autoimmune diseases, suggesting that IgG molecules can instruct the immune system to stop inflammatory processes and initiate the return to the steady state. The aim of this review is to discuss how insights into the mechanism of IVIG activity may help to understand the molecular and cellular pathways underlying resolution of inflammation. We will put a special emphasis on pathways dependent on the IgG FC domain and IgG sialylation, as several recent studies have provided new insights into how this glycosylation-dependent pathway modulates innate and adaptive immune responses through different sets of C-type or I-type lectins.

Keywords: C-type lectin; FC receptors; IgG; autoimmunity; sialic acid.

Publication types

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

MeSH terms

  • Animals
  • Autoimmune Diseases / immunology
  • Autoimmune Diseases / therapy
  • Cell Adhesion Molecules / immunology
  • Humans
  • Immunoglobulin G / immunology*
  • Immunoglobulins, Intravenous / immunology*
  • Immunoglobulins, Intravenous / therapeutic use*
  • Inflammation / immunology*
  • Inflammation / therapy*
  • Lectins, C-Type / immunology
  • Receptors, Cell Surface / immunology

Substances

  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Immunoglobulin G
  • Immunoglobulins, Intravenous
  • Lectins, C-Type
  • Receptors, Cell Surface
  • glycosylated IgG