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

Dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN), also known as CD209, is a type II transmembrane C-type lectin receptor primarily expressed on the surface of dendritic cells and specific macrophage subsets (UniProt: P58015). It serves as a crucial pattern recognition receptor (PRR) that binds to high-mannose and fucose-containing glycans found on various pathogens, including HIV-1, Ebola virus, and Mycobacterium tuberculosis (PubMed: 10675335). Beyond its role in innate immunity, DC-SIGN facilitates the initiation of adaptive immune responses by binding to ICAM-3 on T cells, promoting the formation of the immunological synapse (PubMed: 10675334). In murine models, the ortholog SIGNR1 (CD209b) has been identified as a key mediator of the anti-inflammatory activity of intravenous immunoglobulin (IVIG), specifically through the recognition of sialylated Fc fragments (PubMed: 18339943). Therapeutic interest in DC-SIGN focuses on developing glycomimetic inhibitors to block viral entry and the use of agonists to induce regulatory T cell responses in autoimmune conditions (PubMed: 25135795). However, the target presents challenges, as many pathogens have evolved to exploit DC-SIGN to evade immune detection or enhance their own infectivity (PubMed: 11244031).

Other names

CD209CLEC4LSIGNR1CD209bC-type lectin domain family 4 member L

Binding to mannose- and fucose-containing glycans on pathogens or host cells to modulate immune signaling, facilitate antigen presentation, or mediate anti-inflammatory effects through sialylated IgG recognition.