Dectin-2

Dectin-2 acts as a calcium-dependent lectin and pattern recognition receptor (PRR) within the innate immune system, exhibiting specific recognition and binding to alpha-mannans on C. albicans hyphae. Upon binding of C. albicans alpha-mannans, this receptor complex initiates the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, thereby activating SYK, CARD9, and NF-kappa-B. This cascade of events drives the maturation of antigen-presenting cells and influences antigen-specific priming of T-cells, favoring the development of effector T-helper 1 and T-helper 17 cell subtypes. In addition to its role in antifungal defense, Dectin-2 recognizes allergens from house dust mites and fungi in a mannose-dependent manner, promoting cysteinyl leukotriene production. Moreover, it plays a role in altering adaptive immune responses by recognizing soluble elements from the eggs of Schistosoma mansoni. Associated with FCER1G, Dectin-2 forms a heterodimer with CLEC4D, establishing a pattern recognition receptor against fungal infections. The multifaceted functions of Dectin-2 underscore its importance in immune surveillance and response mechanisms.