Dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN)

Dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN, CD209) is a type II transmembrane C-type lectin receptor predominantly expressed on dendritic cells and some macrophages[3][1][2]. It recognizes high-mannose-type N-glycans and fucose-containing glycans on pathogens, facilitating their binding, uptake, and subsequent initiation of the immune response[5][3][1]. DC-SIGN binds to the intercellular adhesion molecule-3 (ICAM-3) on T cells, mediating adhesion and enhancing dendritic cell interactions with other immune cells[3]. As a pattern recognition receptor, it is crucial for the transmission and infection of a wide range of pathogens, including HIV, Hepatitis C virus, and Dengue virus, often by acting as an entry or attachment factor[3][6][8][1]. DC-SIGN is being explored as a target in vaccine development, especially for cancer immunotherapy and anti-infective strategies, due to its central role in controlling dendritic cell function and pathogen uptake[3][1]. The molecular structure includes a cytoplasmic tail, transmembrane segment, neck region with tandem repeats, and a carbohydrate recognition domain critical for ligand binding and tetramerization[1][5][7].

Other names

CD209DC-SIGNCluster of Differentiation 209

Inhibition of virus binding and entry (antagonism of pathogen recognition), Blockade of immune cell adhesion/activation, Modulation of dendritic cell function