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- Title
DC-SIGN binds ICAM-3 isolated from peripheral human leukocytes through Lewis x residues.
- Authors
Valentina Bogoevska; Peter Nollau; Lothar Lucka; Detlef Grunow; Birgit Klampe; Liisa M. Uotila; Alexandra Samsen; Carl G. Gahmberg; Christoph Wagener
- Abstract
Intercellular adhesion molecule-3 (ICAM-3) binds to the αLβ2 integrin and mediates the contact between T cells and antigen-presenting cells. It has been suggested that dendritic cell-specific ICAM-3 grabbing nonintegrin (DC-SIGN), a C-type lectin of macrophages and DCs, is an additional ligand of ICAM-3. So far, the glycan structure mediating the interaction of native ICAM-3 with DC-SIGN is undefined. Here, we demonstrate that native ICAM-3 from human peripheral leukocytes binds recombinant DC-SIGN, is recognized by monoclonal Lewis x antibodies, and specifically interacts with DC-SIGN on immature DCs. The presence of Lewis x residues on ICAM-3 was confirmed by matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy. Investigations on different peripheral blood cell populations revealed that only ICAM-3 from granulocytes bound DC-SIGN. Cotransfection studies demonstrated that fucosyltransferase (FUT) IX and, to a significantly lesser extent, FUT IV, but not FUTs III and VII, mediate the synthesis of Lewis x residues on ICAM-3. These findings indicate that FUT IX is the main FUT mediating the synthesis of Lewis x residues of ICAM-3 in cells of the myeloid lineage, and that these residues bind DC-SIGN. The results suggest that ICAM-3 assists in the interaction of granulocytes with DC-SIGN of DCs.
- Publication
Glycobiology, 2007, Vol 17, Issue 3, p324
- ISSN
0959-6658
- Publication type
Academic Journal
- DOI
10.1093/glycob/cwl073