Dectin-1 receptor (Dectin-1)

Dectin‑1, encoded by the CLEC7A gene, is a type II transmembrane protein belonging to the C-type lectin-like receptor family. It functions primarily as a pattern-recognition receptor for β-(1→3)/(1→6)-linked glucans found in fungal cell walls but can also recognize endogenous ligands. Structurally, it features an extracellular carbohydrate-recognition domain that binds glucans independently of calcium ions and an intracellular tail containing a hemITAM motif crucial for signal transduction. Upon ligand binding—such as during fungal infection—Dectin‑1 triggers phagocytosis and induces pro-inflammatory cytokines through Syk kinase-dependent pathways. It is highly expressed on myeloid cells including monocytes/macrophages, dendritic cells, neutrophils, and some lymphoid subsets. Beyond host defense against fungi, Dectin‑1 has emerging roles in anti-tumor immunity by recognizing tumor-associated glycans; it also participates in inflammatory diseases and can have both protective or pathogenic effects depending on context.[1][2][3]

Other names

β-glucan receptorCLEC7AC-type lectin domain family 7 member A

Drugs or biologicals targeting Dectin‑1 typically act by: - Agonism with β-glucan ligands to stimulate innate immune responses such as cytokine release and phagocytosis. - Modulation of downstream signaling pathways including Syk kinase activation via its hemITAM motif.