Specificity of DC-SIGN for mannose- and fucose-containing glycans

Ellis van Liempt, Christine M C Bank, Padmaja Mehta, Juan Jesús Garciá-Vallejo, Ziad S Kawar, Rudolf Geyer, Richard A Alvarez, Richard D Cummings, Yvette van Kooyk, Irma van Die

Research output: Contribution to journalArticleAcademicpeer-review

224 Citations (Scopus)

Abstract

The dendritic cell specific C-type lectin dendritic cell specific ICAM-3 grabbing non-integrin (DC-SIGN) binds to "self" glycan ligands found on human cells and to "foreign" glycans of bacterial or parasitic pathogens. Here, we investigated the binding properties of DC-SIGN to a large array of potential ligands in a glycan array format. Our data indicate that DC-SIGN binds with K(d)<2muM to a neoglycoconjugate in which Galbeta1-4(Fucalpha1-3)GlcNAc (Le(x)) trisaccharides are expressed multivalently. A lower selective binding was observed to oligomannose-type N-glycans, diantennary N-glycans expressing Le(x) and GalNAcbeta1-4(Fucalpha1-3)GlcNAc (LacdiNAc-fucose), whereas no binding was observed to N-glycans expressing core-fucose linked either alpha1-6 or alpha1-3 to the Asn-linked GlcNAc of N-glycans. These results demonstrate that DC-SIGN is selective in its recognition of specific types of fucosylated glycans and subsets of oligomannose- and complex-type N-glycans.

Original languageEnglish
Pages (from-to)6123-31
Number of pages9
JournalFEBS letters
Volume580
Issue number26
DOIs
Publication statusPublished - 13 Nov 2006

Keywords

  • Cell Adhesion Molecules/metabolism
  • Fucose
  • Humans
  • Lectins, C-Type/metabolism
  • Ligands
  • Mannose
  • Polysaccharides/chemistry
  • Protein Array Analysis
  • Protein Binding
  • Receptors, Cell Surface/metabolism

Cite this