Mechanism of action of immunoglobulin: Sialylated IgG

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review


Glycosylation of IgG, including sialylation of the Fc region, influences binding of IgG to receptors. In addition to the classical Fc receptor members, we now know of several sugar-binding lectins that recognize sialylated oligosaccharides of IgG. These lectins, particularly human dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN), may regulate immune reactions and are thus candidate molecules in the initiation of the sequence of IVIG-mediated anti-inflammatory events. This chapter reviews the emerging role of sialylated IgG Fc in the IVIG-mediated therapeutic effect, in particular the importance of DC-SIGN-initiated events.

Original languageEnglish
Title of host publicationKawasaki Disease
Subtitle of host publicationCurrent Understanding of the Mechanism and Evidence-Based Treatment
PublisherSpringer Japan
Number of pages8
ISBN (Electronic)9784431560395
ISBN (Print)9784431560371
Publication statusPublished - 2016 Jan 1


  • Dendritic cell
  • Fc receptor
  • Lectin
  • Oligosaccharide


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