C-type lectin domain family 6 member A (Dectin-2) (CLEC6A)

C-type lectin domain family 6 member A (Dectin-2, CLEC6A) is a type II transmembrane receptor primarily expressed on dendritic cells, macrophages, and inflammatory monocytes[1][2][3][4]. It is a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily[3]. The extracellular carbohydrate recognition domain binds to α-mannans, commonly found on fungal cell walls such as *Candida albicans* and other pathogens (e.g., *Cryptococcus neoformans*, *Aspergillus fumigatus*, *Mycobacterium tuberculosis*)[2][3][4][5]. Upon ligand binding, CLEC6A associates with the FcRγ chain, recruiting Syk kinase and activating the CARD9-Bcl10-Malt1 complex, which triggers NF-κB signaling, leading to production of proinflammatory cytokines (e.g., IL-1β, IL-23) and polarization of adaptive immune responses toward Th17 and Th1 phenotypes[1][4]. This signaling axis is essential for antifungal immunity, coordinating inflammatory responses, promoting antigen presentation, and supporting clearance of fungal infections. CLEC6A is also implicated in immune responses to allergens and certain helminth antigens[1][3][4]. No small-molecule drugs or biologics are currently identified as directly targeting CLEC6A. There are also no widely recognized biomarkers or established safety concerns for therapeutic targeting of this molecule.

Other names

C-type lectin domain containing 6ACLECSF10C-type lectin superfamily member 10DC-associated C-type lectin 2Dectin-2hDECTIN-2CLEC4Ndendritic cell-associated C-type lectin 2dectin 2