Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (CD209) (CD209)

Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (CD209), commonly known as DC-SIGN, is a C-type lectin receptor primarily expressed on the surface of dendritic cells and certain macrophages [1, 3, 6]. It plays a dual role in the immune system, functioning both as a cell adhesion molecule that facilitates T-cell priming and as a pattern recognition receptor that identifies a wide array of pathogens, including HIV-1, Ebola virus, and Mycobacterium tuberculosis [1, 4, 8]. By binding to mannose- and fucose-containing glycans, CD209 mediates the endocytosis of these pathogens for antigen presentation, though many viruses exploit this mechanism to facilitate their own entry and dissemination [2, 5, 27]. In oncology, CD209 has emerged as a novel therapeutic target, particularly in acute myeloid leukemia (AML), where it is being explored for targeted delivery via antibody-drug conjugates (ADCs) [7, 10]. Additionally, its role as an alternative receptor for SARS-CoV-2 has highlighted its potential as a target for antiviral strategies aimed at preventing viral attachment and inflammatory complications [9, 21, 27]. Therapeutic development currently focuses on small molecule inhibitors, neutralizing antibodies, and ADCs to modulate its activity in infectious diseases, cancer, and inflammatory conditions [17, 25, 26].

Other names

DC-SIGNCLEC4LCD209 antigenC-type lectin domain family 4 member LDC-SIGN1hDC-SIGN

Inhibition of pathogen binding and entry; targeted delivery of cytotoxic agents via antibody-drug conjugates; modulation of immune signaling pathways.