CLEC7A
CLEC7A (C-type lectin domain containing 7A), also known as Dectin-1, hDectin-1, CD369, SCARE2 and CLECSF12, is a pattern-recognition receptor for beta-1,3-linked and beta-1,6-linked glucans. It contributes to innate immune responses to fungal and bacterial cell wall components. Browse Assay Genie's current range of CLEC7A research reagents below, or read on for the biology behind the target.
CLEC7A is a lectin that works as a pattern-recognition receptor (PRR) specific for beta-1,3-linked and beta-1,6-linked glucans, which are cell wall constituents of pathogenic bacteria and fungi. After binding beta-glucan, it recruits SYK through its ITAM motif and triggers a signalling cascade that activates some CARD domain-BCL10-MALT1 (CBM) signalosomes. This leads to activation of the NF-kappa-B and MAP kinase p38 pathways, which drive expression of genes for pro-inflammatory cytokines and chemokines. CLEC7A is necessary for the TLR2-mediated inflammatory response and NF-kappa-B activation.
Functionally, CLEC7A enhances cytokine production in macrophages and dendritic cells, mediates production of reactive oxygen species and mediates phagocytosis of C. albicans conidia. It also binds T-cells in a way that does not involve their surface glycans, plays a role in T-cell activation and stimulates T-cell proliferation. After binding beta-glucans it induces phosphorylation of SCIMP.
The CLEC7A gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. The glycoprotein is a small type II membrane receptor with an extracellular C-type lectin-like domain fold and a cytoplasmic domain carrying an immunoreceptor tyrosine-based activation motif. UniProt lists it at the cell membrane and in the cytoplasm. Alternative splice variants encoding different isoforms have been characterised. The gene lies in the natural killer gene complex region, closely linked to other CTL/CTLD superfamily members. HGNC places it in the CD molecules, scavenger receptors, C-type lectin domain containing and Dectin 1 cluster groups, and the mouse ortholog is Clec7a.
CLEC7A recognises beta-1,3- and beta-1,6-glucans from fungi and bacteria, making it a central receptor for studying innate pathogen detection.
Signalling via SYK, CBM signalosomes, NF-kappa-B and p38 MAP kinase links CLEC7A to pro-inflammatory cytokine and chemokine gene expression.
CLEC7A enhances cytokine production in macrophages and dendritic cells and mediates reactive oxygen species production and phagocytosis of C. albicans conidia.
CLEC7A binds T-cells independently of their surface glycans, plays a role in T-cell activation and stimulates T-cell proliferation.
CLEC7A is a pattern-recognition receptor for beta-1,3- and beta-1,6-linked glucans. Glucan binding leads to SYK recruitment through its ITAM motif, activation of NF-kappa-B and p38 MAP kinase pathways, and production of pro-inflammatory cytokines and chemokines. It also mediates phagocytosis of C. albicans conidia and reactive oxygen species production.
CLEC7A is also called Dectin-1, hDectin-1, CD369, SCARE2 and CLECSF12. An earlier name was C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 12. Alternative splicing produces different isoforms, so check which isoform a reagent recognises.
A mouse ortholog, Clec7a, is recorded for the human gene. Human CLEC7A belongs to the C-type lectin/C-type lectin-like domain superfamily and sits in the natural killer gene complex region. Check the datasheet of any product for its validated reactivity.
Other C-type lectin domain family members and pattern-recognition receptors with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9BXN2; product specifications from Assay Genie datasheets.