Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin receptor (DC-SIGN)

Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin receptor (DC-SIGN) is a C-type lectin transmembrane receptor expressed primarily on immature dendritic cells and macrophages. Its extracellular domain contains a neck region that drives tetramerization and a carbohydrate recognition domain (CRD), enabling high-affinity binding to high-mannose and fucosylated glycoproteins found on viruses, bacteria, fungi, as well as on other cells of the immune system. DC-SIGN is critical for pathogen recognition, facilitating uptake and presentation of antigens, and also plays a role in cell adhesion (ICAM-3 binding) and modulation of immune responses. DC-SIGN can enable trans-infection by capturing viral particles (such as HIV, Ebola, SARS-CoV, MERS-CoV) and passing them to permissive cells, amplifying infection. It is actively studied as a therapeutic and vaccine target, especially in infectious diseases and cancer immunotherapy

Other names

CD209Dendritic cell-specific ICAM-3-grabbing non-integrinDC-SIGNR (closely related but distinct receptor; do not confuse with DC-SIGN)

Drugs or mimetics aim to block carbohydrate recognition by the C-type lectin domain, inhibiting DC-SIGN binding to viral envelope glycoproteins (e.g., HIV gp120), to prevent pathogen uptake, viral trans-infection, or modulate immune response