C-type lectin domain family 7 member A (Dectin-1) (Dectin-1)

C-type lectin domain family 7 member A (Dectin-1) is a type II transmembrane pattern recognition receptor primarily expressed on myeloid lineage cells such as macrophages, dendritic cells, neutrophils, monocytes, and some T cell subsets[3][5]. Encoded by the CLEC7A gene in humans[7], it features an extracellular carbohydrate-recognition domain that binds β-(1→3)/(1→6)-glucans found mainly on fungal cell walls but also recognizes certain endogenous ligands and N-glycan structures on tumor cells[5]. Upon ligand binding—independent of calcium—its intracellular tail containing a hemITAM motif initiates downstream signaling through Syk kinase and CARD9 adaptor proteins. This triggers robust innate immune responses including cytokine release (e.g., TNFα, IL-6), chemokine production for leukocyte recruitment,[4] autophagy-dependent unconventional protein secretion,[4] promotion of regulatory T cell responses,[6] anti-mycobacterial activity,[1] and orchestration of natural killer cell-mediated anti-tumor effects.[2][3] Dectin-1 plays critical roles in antifungal defense but is also implicated in cancer immunosurveillance and inflammatory diseases. Its broad expression across innate immune cells makes it central to early pathogen detection as well as shaping subsequent adaptive immunity.[3]

Other names

CLEC7Aβ-glucan receptorBeta-glucan receptorC-type lectin domain family 7 member A

Drugs or ligands that bind Dectin-1 typically act as agonists, triggering the hemITAM-Syk-CARD9 signaling cascade. This leads to activation of NF-κB and other transcription factors, resulting in cytokine production, enhanced phagocytosis, respiratory burst activity, and modulation of adaptive immunity[1][3].