Mechanism of action of immunoglobulin: Sialylated IgG

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

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
Pages223-230
Number of pages8
ISBN (Electronic)9784431560395
ISBN (Print)9784431560371
DOIs
Publication statusPublished - 2016 Jan 1

Keywords

  • DC-SIGN
  • Dendritic cell
  • Fc receptor
  • Lectin
  • Oligosaccharide

ASJC Scopus subject areas

  • Medicine(all)
  • Immunology and Microbiology(all)

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