C-type lectin domain family 4 member D (CLEC4D)

C-type lectin domain family 4 member D (CLEC4D) is a calcium-dependent, type II transmembrane receptor predominantly expressed on myeloid lineage cells, including neutrophils and monocytes[1][2][5]. It functions as a pattern recognition receptor (PRR) in the innate immune system, recognizing both damage-associated (DAMPs) and pathogen-associated (PAMPs) molecular patterns, such as alpha-mannans on fungal pathogens (notably, Candida albicans) and mycobacterial glycolipids like trehalose-6,6'-dimycolate[1][8]. Upon ligand binding, CLEC4D triggers cellular signaling via Syk kinase, leading to phagocytosis, cytokine release, respiratory burst, and the maturation of antigen-presenting cells, thereby promoting adaptive immune responses such as Th1 and Th17 polarization[1][2]. CLEC4D also forms functional complexes with other lectin family members (e.g., CLEC6A/Dectin-2) and is implicated in defense against fungal and some bacterial infections[1]. There are currently no approved or experimental drugs known to target CLEC4D directly; its role is primarily in host defense and immunomodulation[1][8].

Other names

Dectin-3Macrophage C-type lectinMCLCLECSF8CD368MpclC-type lectin superfamily member 8C-type lectin-like receptor 6Dendritic cell-associated C-type lectin 3

Recognition of microbial glycolipids or carbohydrates triggers downstream signaling via SYK kinase; Promotes cytokine production and immune cell activation