CLEC7A

Dectin-1 is a transmembrane protein containing an immunoreceptor tyrosine-based activation (ITAM)-like motif in its intracellular tail (which is involved in cellular activation) and one C-type lectin-like domain (carbohydrate-recognition domain, CRD) in the extracellular region (which recognizes β-glucans and endogenous ligands on T cells). The CRD is separated from the membrane by a stalk region. CLEC7A contains putative sites of N-linked glycosylation in the stalk region. CLEC7A is expressed by macrophages, neutrophils and dendritic cells. Expression has also been studied on other immune cells including eosinophils and B cells. == Function ==

The C-type lectin receptors are class of signalling pattern recognition receptors which are involved in antifungal immunity, but also play important roles in immune responses to other pathogens such as bacteria, viruses and nematodes. This signaling complex in turn triggers downstream recruitment of TRAF6 and NF-κB activation. This transcription factor is responsible for the production of numerous inflammatory cytokines Antifungal immunity CLEC7A has been shown to recognize species of several fungal genera, including Saccharomyces, Candida, Pneumocystis, Coccidioides, Penicillium and others. Recognition of these organisms triggers many protective pathways, such as fungal uptake by phagocytosis and killing via hypochlorite generation. Activation of dectin-1 also triggers expression of many protecting antifungal cytokines and chemokines (TNF, CXCL2, IL-1β, IL-1α, CCL3, GM-CSF, G-CSF and IL-6) and the development of Th17. Co-stimulatory molecule Also operating as a co-stimulatory molecule via recognition of an endogenous ligand on T-cells, which leads to cellular activation and proliferation, CLEC7A can bind both CD4+ and CD8+ T cells. == References ==