CLEC7A

CLEC7A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2BPD, 2BPE, 2BPH, 2CL8
Identifiers
Aliases	CLEC7A , BGR, CANDF4, CLECSF12, DECTIN1, CD369, SCARE2, C-type lectin domain family 7 member A, C-type lectin domain containing 7A
External IDs	OMIM: 606264 MGI: 1861431 HomoloGene: 49606 GeneCards: CLEC7A
Gene location (Human)
Chr.	Chromosome 12 (human)
End	10,130,258 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	129,449,742 bp
RNA expression pattern
	Top expressed in
	monocyte; ; blood; ; periodontal fiber; ; right lung; ; appendix; ; spleen; ; upper lobe of left lung; ; bone marrow; ; bone marrow cells; ; palpebral conjunctiva;
	Top expressed in
	right lung lobe; ; blood; ; bone marrow; ; left lung; ; mucous cell of stomach; ; subcutaneous adipose tissue; ; spleen; ; thymus; ; carotid body; ; white adipose tissue;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	MHC protein binding ; pattern recognition receptor activity ; metal ion binding ; protein binding ; carbohydrate binding ;
Cellular component	cytoplasm ; integral component of membrane ; intracellular membrane-bounded organelle ; membrane ; plasma membrane ; nucleoplasm ;
Biological process	cell recognition ; immune system process ; carbohydrate mediated signaling ; phagocytosis, recognition ; inflammatory response ; T cell activation ; defense response to protozoan ; pattern recognition receptor signaling pathway ; innate immune response ; positive regulation of protein-containing complex assembly ; positive regulation of interleukin-1 beta production ; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process ; positive regulation of phagocytosis ; positive regulation of killing of cells of other organism ; positive regulation of cytokine production involved in inflammatory response ;
	Sources:Amigo / QuickGO
Orthologs
	64581
	56644
	ENSG00000172243
	ENSMUSG00000079293
	Q9BXN2
	V9GXI5
NM_022570 ; NM_197947 ; NM_197948 ; NM_197949 ; NM_197950 ;
	NM_197951 ; NM_197952 ; NM_197953 ; NM_197954
	NM_020008 ; NM_001309637
NP_072092 ; NP_922938 ; NP_922939 ; NP_922940 ; NP_922941 ;
	NP_922945
	NP_001296566 ; NP_064392
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 05, 2024

C-type lectin domain family 7 member A or Dectin-1 is a protein that in humans is encoded by the CLEC7A gene.^[5] CLEC7A is a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. The encoded glycoprotein is a small type II membrane receptor with an extracellular C-type lectin-like domain fold and a cytoplasmic domain with a partial immunoreceptor tyrosine-based activation motif. It functions as a pattern-recognition receptor for a variety of β-1,3-linked and β-1,6-linked glucans from fungi and plants, and in this way plays a role in innate immune response. Expression is found on myeloid dendritic cells, monocytes, macrophages and B cells. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. This gene is closely linked to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region.^[5]

Structure

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.^[6]^[7]

CLEC7A is expressed by macrophages, neutrophils and dendritic cells.^[8] Expression has also been studied on other immune cells including eosinophils and B cells.^[9]

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.^[6] As a member of this receptor family, dectin-1 recognizes β-glucans and carbohydrates found in fungal cell walls, some bacteria and plants, but may also recognize other unidentified molecules (endogenous ligand on T-cells and ligand on mycobacteria).^[6] Ligand binding induces intracellular signalling via the ITAM-like motif. CLEC7A can induce both Syk dependent or Syk independent pathways. Dimerization of dectin-1 upon ligand binding leads to tyrosine phosphorylation by Src family kinases and recruitment of Syk. Upon Syk recruitment is PKC-δ activated, which subsequently phosphorylates CARD9 that triggers recruitment of BCL10 and MALT1, leading to a CARD-CC/BCL10/MALT1 (CBM) signaling complex.^[10] 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 ^[9] and chemokines such as TNF, IL-23, IL-6, IL-2. Other responses include: respiratory burst, production of arachidonic acid metabolites, dendritic cell maturation, and phagocytosis of the ligand.^[11]

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 T_h17.^[11]

Histoplasma capsulatum can evade recognition of β-glucan via CLEC7A on phagocytic cells by secreting an enzyme that removes exposed β-glucans or by masking the β-glucan with α-glucan.^[12]

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.^[11]

Related Research Articles

Pattern recognition receptors (PRRs) play a crucial role in the proper function of the innate immune system. PRRs are germline-encoded host sensors, which detect molecules typical for the pathogens. They are proteins expressed mainly by cells of the innate immune system, such as dendritic cells, macrophages, monocytes, neutrophils, as well as by epithelial cells, to identify two classes of molecules: pathogen-associated molecular patterns (PAMPs), which are associated with microbial pathogens, and damage-associated molecular patterns (DAMPs), which are associated with components of host's cells that are released during cell damage or death. They are also called primitive pattern recognition receptors because they evolved before other parts of the immune system, particularly before adaptive immunity. PRRs also mediate the initiation of antigen-specific adaptive immune response and release of inflammatory cytokines.

DC-SIGN also known as CD209 is a protein which in humans is encoded by the CD209 gene.

Collectins (collagen-containing C-type lectins) are a part of the innate immune system. They form a family of collagenous Ca²⁺-dependent defense lectins, which are found in animals. Collectins are soluble pattern recognition receptors (PRRs). Their function is to bind to oligosaccharide structure or lipids that are on the surface of microorganisms. Like other PRRs they bind pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs) of oligosaccharide origin. Binding of collectins to microorganisms may trigger elimination of microorganisms by aggregation, complement activation, opsonization, activation of phagocytosis, or inhibition of microbial growth. Other functions of collectins are modulation of inflammatory, allergic responses, adaptive immune system and clearance of apoptotic cells.

An immunoreceptor tyrosine-based activation motif (ITAM) is a conserved sequence of four amino acids that is repeated twice in the cytoplasmic tails of non-catalytic tyrosine-phosphorylated receptors, cell-surface proteins found mainly on immune cells. Its major role is being an integral component for the initiation of a variety of signaling pathway and subsequently the activation of immune cells, although different functions have been described, for example an osteoclast maturation.

Langerin (CD207) is a type II transmembrane protein which is encoded by the CD207 gene in humans. It was discovered by scientists Sem Saeland and Jenny Valladeau as a main part of Birbeck granules. Langerin is C-type lectin receptor on Langerhans cells (LCs) and in mice also on dermal interstitial CD103+ dendritic cells (DC) and on resident CD8+ DC in lymph nodes.

The mannose receptor is a C-type lectin primarily present on the surface of macrophages, immature dendritic cells and liver sinusoidal endothelial cells, but is also expressed on the surface of skin cells such as human dermal fibroblasts and keratinocytes. It is the first member of a family of endocytic receptors that includes Endo180 (CD280), M-type PLA2R, and DEC-205 (CD205).

NKG2 also known as CD159 is a receptor for natural killer cells. There are 7 NKG2 types: A, B, C, D, E, F and H. NKG2D is an activating receptor on the NK cell surface. NKG2A dimerizes with CD94 to make an inhibitory receptor (CD94/NKG2).

Toll-like receptor 6 is a protein that in humans is encoded by the TLR6 gene. TLR6 is a transmembrane protein, member of toll-like receptor family, which belongs to the pattern recognition receptor (PRR) family. TLR6 acts in a heterodimer form with toll-like receptor 2 (TLR2). Its ligands include multiple diacyl lipopeptides derived from gram-positive bacteria and mycoplasma and several fungal cell wall saccharides. After dimerizing with TLR2, the NF-κB intracellular signalling pathway is activated, leading to a pro-inflammatory cytokine production and activation of innate immune response. TLR6 has also been designated as CD286.

Intercellular adhesion molecule 3 (ICAM3) also known as CD50, is a protein that in humans is encoded by the ICAM3 gene. The protein is constitutively expressed on the surface of leukocytes, which are also called white blood cells and are part of the immune system. ICAM3 mediates adhesion between cells by binding to specific integrin receptors. It plays an important role in the immune cell response through its facilitation of interactions between T cells and dendritic cells, which allows for T cell activation. ICAM3 also mediates the clearance of cells undergoing apoptosis by attracting and binding macrophages, a type of cell that breaks down infected or dying cells through a process known as phagocytosis, to apoptotic cells.

CD69 is a human transmembrane C-Type lectin protein encoded by the CD69 gene. It is an early activation marker that is expressed in hematopoietic stem cells, T cells, and many other cell types in the immune system. It is also implicated in T cell differentiation as well as lymphocyte retention in lymphoid organs.

CD244 also known as 2B4 or SLAMF4 is a protein that in humans is encoded by the CD244 gene.

Killer cell lectin-like receptor subfamily B, member 1, also known as KLRB1, NKR-P1A or CD161, is a human gene.

NKG2-C type II integral membrane protein or NKG2C is a protein that in humans is encoded by the KLRC2 gene. It is also known as or cluster of differentiation 159c (CD159c).

C-type lectin domain family 12 member A is a protein that in humans is encoded by the CLEC12A gene.

The following outline is provided as an overview of and topical guide to immunology:

C-type lectin domain family 5 member A (CLEC5A), also known as C-type lectin superfamily member 5 (CLECSF5) and myeloid DAP12-associating lectin 1 (MDL-1) is a C-type lectin that in humans is encoded by the CLEC5A gene.

NKG2D is an activating receptor (transmembrane protein) belonging to the NKG2 family of C-type lectin-like receptors. NKG2D is encoded by KLRK1 (killer cell lectin like receptor K1) gene which is located in the NK-gene complex (NKC) situated on chromosome 6 in mice and chromosome 12 in humans. In mice, it is expressed by NK cells, NK1.1⁺ T cells, γδ T cells, activated CD8⁺ αβ T cells and activated macrophages. In humans, it is expressed by NK cells, γδ T cells and CD8⁺ αβ T cells. NKG2D recognizes induced-self proteins from MIC and RAET1/ULBP families which appear on the surface of stressed, malignant transformed, and infected cells.

Macrophage inducible Ca²⁺-dependent lectin receptor, (abbreviated to Mincle), is a member of the C-type lectin superfamily encoded by the gene CLEC4E. It is a pattern recognition receptor that can recognize glycolipids including mycobacterial cord factor, trehalose-6,6'-dimycolate (TDM). The mincle receptor binds a range of carbohydrate structures, predominantly containing glucose or mannose, and play an important role in recognition of bacterial glycolipids by the immune system. Upon activation by cord factor, Mincle binds the Fc receptor FcRγ and Syk. Cord factor also binds and activates the related C-type lectin MCL. Upon receptor stimulation is PKC-δ activated, which subsequently phosphorylates CARD9 that triggers recruitment of BCL10 and MALT1, leading to a CARD-CC/BCL10/MALT1 (CBM) signaling complex. This signaling complex in turn triggers downstream recruitment of TRAF6 and NF-κB activation.

Dectin-2 or C-type lectin domain containing 6A is a protein that in humans is encoded by the CLEC6A gene. Dectin-2 is a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. The encoded protein is a type II transmembrane protein with an extracellular carbohydrate recognition domain. It functions as a pattern recognition receptor recognizing α-mannans and as such plays an important role in innate immune response to fungi. Expression is found on macrophages and dendritic cells. It can also be found at low levels in Langerhans cells and peripheral blood monocytes, where expression levels could be increased upon induction of inflammation.

Paired receptors are pairs or clusters of receptor proteins that bind to extracellular ligands but have opposing activating and inhibitory signaling effects. Traditionally, paired receptors are defined as homologous pairs with similar extracellular domains and different cytoplasmic regions, whose genes are located together in the genome as part of the same gene cluster and which evolved through gene duplication. Homologous paired receptors often, but not always, have a shared ligand in common. More broadly, pairs of receptors have been identified that exhibit paired functional behavior - responding to a shared ligand with opposing intracellular signals - but are not closely homologous or co-located in the genome. Paired receptors are highly expressed in the cells of the immune system, especially natural killer (NK) and myeloid cells, and are involved in immune regulation.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000172243 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000079293 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: CLEC7A C-type lectin domain family 7, member A".
1 2 3 Drummond RA, Brown GD (August 2011). "The role of Dectin-1 in the host defence against fungal infections". Current Opinion in Microbiology. 14 (4): 392–9. doi:10.1016/j.mib.2011.07.001. PMID 21803640.
↑ Brown J, O'Callaghan CA, Marshall AS, Gilbert RJ, Siebold C, Gordon S, et al. (June 2007). "Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function". Protein Science. 16 (6): 1042–52. doi:10.1110/ps.072791207. PMC 2206667 . PMID 17473009.
↑ Taylor PR, Brown GD, Reid DM, Willment JA, Martinez-Pomares L, Gordon S, Wong SY (October 2002). "The beta-glucan receptor, dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages". Journal of Immunology. 169 (7): 3876–82. doi: 10.4049/jimmunol.169.7.3876 . PMID 12244185.
1 2 Saijo S, Iwakura Y (August 2011). "Dectin-1 and Dectin-2 in innate immunity against fungi". International Immunology. 23 (8): 467–72. doi: 10.1093/intimm/dxr046 . PMID 21677049.
↑ Strasser D, Neumann K, Bergmann H, Marakalala MJ, Guler R, Rojowska A, et al. (January 2012). "Syk kinase-coupled C-type lectin receptors engage protein kinase C-δ to elicit Card9 adaptor-mediated innate immunity". Immunity. 36 (1): 32–42. doi:10.1016/j.immuni.2011.11.015. PMC 3477316 . PMID 22265677.
1 2 3 Huysamen C, Brown GD (January 2009). "The fungal pattern recognition receptor, Dectin-1, and the associated cluster of C-type lectin-like receptors". FEMS Microbiology Letters. 290 (2): 121–8. doi:10.1111/j.1574-6968.2008.01418.x. PMC 2704933 . PMID 19025564.
↑ Ray SC, Rappleye CA (May 2019). "Flying under the radar: Histoplasma capsulatum avoidance of innate immune recognition". Seminars in Cell & Developmental Biology. 89: 91–98. doi:10.1016/j.semcdb.2018.03.009. PMC 6150853 . PMID 29551572.

External links

Human CLEC7A genome location and CLEC7A gene details page in the UCSC Genome Browser .

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Hermanz-Falcón P, Arce I, Roda-Navarro P, Fernández-Ruiz E (2001). "Cloning of human DECTIN-1, a novel C-type lectin-like receptor gene expressed on dendritic cells". Immunogenetics. 53 (4): 288–95. doi:10.1007/s002510100326. PMID 11491532. S2CID 9553842.
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Willment JA, Gordon S, Brown GD (November 2001). "Characterization of the human beta -glucan receptor and its alternatively spliced isoforms". The Journal of Biological Chemistry. 276 (47): 43818–23. doi: 10.1074/jbc.M107715200 . PMID 11567029.
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Ahrén IL, Eriksson E, Egesten A, Riesbeck K (November 2003). "Nontypeable Haemophilus influenzae activates human eosinophils through beta-glucan receptors". American Journal of Respiratory Cell and Molecular Biology. 29 (5): 598–605. doi:10.1165/rcmb.2002-0138OC. PMID 12689921.
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Taylor PR, Brown GD, Herre J, Williams DL, Willment JA, Gordon S (January 2004). "The role of SIGNR1 and the beta-glucan receptor (dectin-1) in the nonopsonic recognition of yeast by specific macrophages". Journal of Immunology. 172 (2): 1157–62. doi: 10.4049/jimmunol.172.2.1157 . PMID 14707091.
Mantegazza AR, Barrio MM, Moutel S, Bover L, Weck M, Brossart P, et al. (August 2004). "CD63 tetraspanin slows down cell migration and translocates to the endosomal-lysosomal-MIICs route after extracellular stimuli in human immature dendritic cells". Blood. 104 (4): 1183–90. doi: 10.1182/blood-2004-01-0104 . hdl: 11336/43490 . PMID 15130945.
de la Rosa G, Yáñez-Mó M, Samaneigo R, Serrano-Gómez D, Martínez-Muñoz L, Fernández-Ruiz E, et al. (May 2005). "Regulated recruitment of DC-SIGN to cell-cell contact regions during zymosan-induced human dendritic cell aggregation". Journal of Leukocyte Biology. 77 (5): 699–709. CiteSeerX 10.1.1.490.9674 . doi:10.1189/jlb.0904529. PMID 15728245. S2CID 36603012.
Willment JA, Marshall AS, Reid DM, Williams DL, Wong SY, Gordon S, Brown GD (May 2005). "The human beta-glucan receptor is widely expressed and functionally equivalent to murine Dectin-1 on primary cells". European Journal of Immunology. 35 (5): 1539–47. doi: 10.1002/eji.200425725 . PMID 15816015. S2CID 20018101.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000172243 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000079293 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 "Entrez Gene: CLEC7A C-type lectin domain family 7, member A".

[pmid21803640-6] 1 2 3 Drummond RA, Brown GD (August 2011). "The role of Dectin-1 in the host defence against fungal infections". Current Opinion in Microbiology. 14 (4): 392–9. doi:10.1016/j.mib.2011.07.001. PMID 21803640.

[pmid17473009-7] Brown J, O'Callaghan CA, Marshall AS, Gilbert RJ, Siebold C, Gordon S, et al. (June 2007). "Structure of the fungal beta-glucan-binding immune receptor dectin-1: implications for function". Protein Science. 16 (6): 1042–52. doi:10.1110/ps.072791207. PMC 2206667 . PMID 17473009.

[pmid12244185-8] Taylor PR, Brown GD, Reid DM, Willment JA, Martinez-Pomares L, Gordon S, Wong SY (October 2002). "The beta-glucan receptor, dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages". Journal of Immunology. 169 (7): 3876–82. doi: 10.4049/jimmunol.169.7.3876 . PMID 12244185.

[pmid21677049-9] 1 2 Saijo S, Iwakura Y (August 2011). "Dectin-1 and Dectin-2 in innate immunity against fungi". International Immunology. 23 (8): 467–72. doi: 10.1093/intimm/dxr046 . PMID 21677049.

[pmid22265677-10] Strasser D, Neumann K, Bergmann H, Marakalala MJ, Guler R, Rojowska A, et al. (January 2012). "Syk kinase-coupled C-type lectin receptors engage protein kinase C-δ to elicit Card9 adaptor-mediated innate immunity". Immunity. 36 (1): 32–42. doi:10.1016/j.immuni.2011.11.015. PMC 3477316 . PMID 22265677.

[pmid19025564-11] 1 2 3 Huysamen C, Brown GD (January 2009). "The fungal pattern recognition receptor, Dectin-1, and the associated cluster of C-type lectin-like receptors". FEMS Microbiology Letters. 290 (2): 121–8. doi:10.1111/j.1574-6968.2008.01418.x. PMC 2704933 . PMID 19025564.

[12] Ray SC, Rappleye CA (May 2019). "Flying under the radar: Histoplasma capsulatum avoidance of innate immune recognition". Seminars in Cell & Developmental Biology. 89: 91–98. doi:10.1016/j.semcdb.2018.03.009. PMC 6150853 . PMID 29551572.

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