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Specificity of DC‐SIGN for mannose‐ and fucose‐containing glycans
Author(s) -
van Liempt Ellis,
Bank Christine M.C.,
Mehta Padmaja,
Garcı´a-Vallejo Juan Jesús,
Kawar Ziad S.,
Geyer Rudolf,
Alvarez Richard A.,
Cummings Richard D.,
Kooyk Yvette van,
van Die Irma
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.009
Subject(s) - dc sign , glycan , fucose , lectin , chemistry , c type lectin , biochemistry , mannose , fucosylation , glycoprotein , dendritic cell , microbiology and biotechnology , biology , immunology , antigen
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 < 2 μM to a neoglycoconjugate in which Galβ1‐4(Fucα1‐3)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 GalNAcβ1‐4(Fucα1‐3)GlcNAc (LacdiNAc‐fucose), whereas no binding was observed to N ‐glycans expressing core‐fucose linked either α1‐6 or α1‐3 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.