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IgG Glyco-Engineering to Improve IVIg Potency.

Christine W Bruggeman1, Gillian Dekkers2, Remco Visser2

  • 1Sanquin Research and Landsteiner Laboratory, Department of Blood Cell Research, Academic Medical Center, University of Amsterdam, Amsterdam, Netherlands.

Frontiers in Immunology
|November 9, 2018
PubMed
Summary
This summary is machine-generated.

Intravenous immunoglobulins (IVIg) modulate autoimmune diseases by altering IgG glycan structures. Glyco-engineering revealed bisecting GlcNAc and galactosylation significantly impact Fc-gamma receptor interactions, improving IVIg efficacy.

Keywords:
Fc glycanFcγRsIVIgIgGglyco-engineering

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Area of Science:

  • Immunology
  • Glycobiology
  • Pharmacology

Background:

  • Intravenous immunoglobulins (IVIg) are crucial for treating autoimmune and inflammatory conditions.
  • IVIg functions by preventing phagocytosis of antibody-coated cells via Fc-gamma receptor (FcγR) blockade.
  • The N-glycan on IgG's Fc-tail significantly influences its interaction with FcγRs.

Purpose of the Study:

  • To investigate the impact of specific IgG glycan structures on FcγR-mediated phagocytosis.
  • To explore glyco-engineering strategies for enhancing the immunomodulatory efficacy of IVIg.

Main Methods:

  • Generated monoclonal IgG antibodies with defined Fc-tail glycoforms via glyco-engineering.
  • Assessed the opsonizing and FcγR-blocking capacities of these glycovariants.
  • Utilized a phagocytosis assay involving IgG-opsonized erythrocytes and human monocyte-derived macrophages.

Main Results:

  • IgG glycovariants showed differential inhibition of erythrocyte uptake, despite no effect on opsonization.
  • The presence of bisecting N-acetyl glucosamine (GlcNAc) and terminal galactosylation significantly impacted FcγR binding and phagocytosis inhibition.
  • Core fucosylation had a less pronounced effect compared to bisecting GlcNAc and galactosylation.

Conclusions:

  • Targeted glycan modifications, particularly bisecting GlcNAc and galactosylation, can enhance the efficacy of IVIg therapy.
  • Modulating IgG glycosylation offers a promising strategy for improving immunomodulatory treatments.
  • Fc-tail glycan engineering presents a novel approach to optimize IVIg's therapeutic potential in autoimmune diseases.