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Related Experiment Video

Updated: Jan 22, 2026

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Human DC-SIGN and CD23 do not interact with human IgG.

A Robin Temming1, Gillian Dekkers1, Fleur S van de Bovenkamp2

  • 1Department Experimental Immunohematology, Sanquin Research and Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.

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|July 12, 2019
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Summary

Intravenous immunoglobulin (IVIg) therapies

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Area of Science:

  • Immunology
  • Glycobiology
  • Pharmacology

Background:

  • Intravenous immunoglobulin (IVIg) therapies are used for various inflammatory and autoimmune conditions, but their precise mechanisms remain unclear.
  • Sialylated IgG, a fraction within IVIg, shows enhanced therapeutic activity in mouse models.
  • Fc-sialylation of IgG may alter its binding properties, potentially mediating immunomodulatory effects through interactions with C-type lectins like DC-SIGN and CD23.

Purpose of the Study:

  • To investigate whether human CD23 and DC-SIGN directly bind to human IgG, irrespective of its glycosylation status.
  • To determine if Fc- or Fab-glycosylation of IgG influences its interaction with CD23 and DC-SIGN.
  • To clarify the role of these C-type lectins in the immunomodulatory mechanisms of IVIg.

Main Methods:

  • Utilized flow cytometry (FACS) to assess cellular binding.
  • Employed a novel cellular Surface Plasmon Resonance imaging (cSPRi) approach to monitor low-affinity, high-avidity interactions.
  • Tested binding of sialylated and non-sialylated human IgG (with variations in glycosylation) to cells expressing human CD23 and DC-SIGN.

Main Results:

  • Cells expressing native CD23 and DC-SIGN bound their natural ligands (IgE and ICAM-3, respectively).
  • No binding of human IgG to CD23 or DC-SIGN was observed, regardless of Fc- or Fab-glycan sialylation, fucosylation, or bisection.
  • The study found no evidence supporting CD23 or DC-SIGN as direct receptors for human IgG.

Conclusions:

  • Human CD23 and DC-SIGN do not appear to be direct receptors for human IgG, challenging proposed mechanisms of IVIg therapy.
  • The findings do not exclude indirect roles for IgG glycosylation or C-type lectins in modulating IVIg efficacy.
  • Further research is needed to fully elucidate the complex mechanisms underlying IVIg's anti-inflammatory effects.