C-type lectin domain family 4 member L (CD209) (CD209)

C-type lectin domain family 4 member L, widely known as Dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN) or CD209, is a calcium-dependent type II transmembrane receptor primarily expressed on the surface of dendritic cells and specific macrophage subsets (UniProt: Q9NNX6). It plays a pivotal role in the immune system by mediating cell-cell adhesion through binding with ICAM-3 on T cells, which is essential for the initiation of primary immune responses and the formation of the immunological synapse (Geijtenbeek et al., 2000, PMID: 10688190). Additionally, DC-SIGN acts as a pattern recognition receptor (PRR) that identifies and captures a broad range of pathogens, including HIV-1, Ebola virus, Mycobacterium tuberculosis, and SARS-CoV-2, by recognizing high-mannose or fucose-containing glycans (PMID: 33833023). In the context of infectious disease, DC-SIGN is frequently exploited by viruses to facilitate host entry or to promote "trans-infection," a process where the receptor captures viral particles and transmits them to susceptible target cells like CD4+ T cells (Thépaut et al., 2020, PMID: 32582158). Beyond infections, it is involved in the immune evasion mechanisms of certain tumors and the regulation of inflammatory signaling. Consequently, DC-SIGN is a significant therapeutic target for the development of glycomimetic inhibitors and monoclonal antibodies designed to block pathogen attachment and modulate immune activation in chronic infections and oncology.

Other names

DC-SIGNCLEC4LDendritic cell-specific ICAM-3-grabbing non-integrinCD209 antigen

Competitive inhibition of the carbohydrate recognition domain (CRD) to prevent pathogen binding and entry (PMID: 32582158).