Dendritic cell–specific intercellular adhesion molecule-3–grabbing nonintegrin (DC-SIGN)

Dendritic cell–specific intercellular adhesion molecule-3–grabbing nonintegrin (DC-SIGN or CD209) is a type II transmembrane C-type lectin receptor primarily expressed on dendritic cells and some macrophages. It consists of a short cytosolic region, a transmembrane domain, and an extracellular domain containing a neck region and a carbohydrate recognition domain (CRD), forming tetramers at the cell surface. DC-SIGN binds high-mannose and fucosylated glycoproteins on pathogens (such as HIV, hepatitis C, and schistosomes), facilitating adhesion, endocytosis, and antigen presentation. By recognizing pathogen-associated molecular patterns (PAMPs), it triggers phagocytosis and signaling for innate and adaptive immune responses. It also mediates T cell activation via binding to ICAM-3. Importantly, DC-SIGN can promote infection (notably for HIV and hepatitis C) and contribute to immune evasion, making it a potential target for therapeutic intervention (e.g., vaccines, infection modulators) and a candidate biomarker for dendritic cell function and maturation. Abnormal DC-SIGN activity has implications in infectious disease, cancer, and inflammatory diseases.

Other names

CD209Dendritic cell–specific ICAM-3–grabbing nonintegrinCluster of Differentiation 209DC-SIGN protein

Inhibitors compete with high-mannose or fucosylated glycan ligands, blocking pathogen binding and endocytosis. Glycomimetic drugs may target the carbohydrate recognition domain (CRD) to modulate immune or viral interactions.