Dendritic cell-associated C-type lectin-1 (Dectin-1)

Dendritic cell-associated C-type lectin-1 (Dectin-1) is a type II transmembrane C-type lectin receptor (CLR) encoded by the CLEC7A gene. It is primarily expressed on myeloid lineage immune cells—including macrophages, monocytes, neutrophils, and dendritic cells—and is also found at lower levels in some lymphoid cells. Dectin-1 functions as a pattern recognition receptor (PRR), recognizing β-1,3 and β-1,6 glucans present mainly in fungal cell walls and select bacterial species. Upon recognizing its ligands, Dectin-1 induces signaling via its hemITAM motif in the cytoplasmic tail. This signaling can activate both canonical (Syk kinase, CARD9/Bcl10/MALT1, NF-κB) and non-canonical (Raf-1) pathways, resulting in cytokine production, the respiratory burst, phagocytosis, and the promotion of adaptive immunity. Dectin-1 plays a fundamental role in anti-fungal immunity, contributes to the concept of innate immune memory ("trained immunity"), and is a key modulator at the interface of innate and adaptive immune responses. Dectin-1 is under exploration as a therapeutic target for immune modulation and as a vaccine adjuvant, but no approved drugs specifically target this receptor as of now. Overactivation or dysregulation of Dectin-1 can potentially contribute to immune-mediated tissue injury, making precise modulation a safety consideration.

Other names

β-glucan receptorCLEC7ADectin-1Dendritic cell-associated C-type lectin 1

Agonists (such as β-glucans, curdlan) activate Dectin-1 by binding to its carbohydrate recognition domain (CRD), triggering intracellular signaling Triggers phosphorylation of the cytoplasmic hemITAM motif, recruits and activates Syk kinase, subsequently activating downstream pathways such as CARD9/Bcl10/MALT1 and Raf-1, leading to NF-κB activation, cytokine release, and inflammatory responses Promotes phagocytosis and activation of adaptive immune responses through T cell differentiation and cytokine induction