Alternative titles; symbols
HGNC Approved Gene Symbol: CD209
Cytogenetic location: 19p13.2 Genomic coordinates (GRCh38): 19:7,739,993-7,747,534 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 19p13.2 | {Dengue fever, protection against} | 614371 | 3 | |
| {HIV type 1, susceptibility to} | 609423 | 3 | ||
| {Mycobacterium tuberculosis, susceptibility to} | 607948 | 3 |
The C-type lectin receptors are involved in the primary interface between host and pathogens. Two prototypic members of the C-type lectin-receptor family act as both cell-adhesion receptors and pathogen-recognition receptors: CD209 and its close relative CD209L (CLEC4M; 605872) (review by Barreiro et al., 2005).
The binding of the human immunodeficiency virus (HIV) envelope glycoprotein gp120 to the cell surface receptor CD4 (186940) had been considered a primary determinant of viral tropism (see 609423). A number of cell types, however, can be infected by the virus, or bind gp120, in the absence of CD4 expression. Human placenta had been identified as a tissue that binds gp120 in a CD4-independent manner. By expression cloning, Curtis et al. (1992) screened a placenta cDNA library and isolated a cDNA (clone 11) encoding a gp120-binding protein unrelated to CD4. The 1.3-kb cDNA predicts a 404-amino acid protein with a calculated molecular mass of 45,775 Da. The gp120-binding protein is organized into 3 domains: an N-terminal cytoplasmic and hydrophobic region, a set of tandem repeats (7 complete and 1 incomplete), and a C-terminal domain with homology to C-type (calcium-dependent) lectins. A type II membrane orientation (N-terminal cytoplasmic) was predicted both by the cDNA sequence and by the reactivity of C-terminal peptide-specific antiserum with the surface of clone 11-transfected cells. Native and recombinant gp120 and whole virus bound transfected cells. Gp120 binding was high affinity (Kd, 1.3 to 1.6 nM) and was inhibited by mannan, D-mannose, and L-fucose; once bound, gp120 was internalized rapidly. These data demonstrated that the gp120-binding protein is a membrane-associated mannose-binding lectin. Curtis et al. (1992) suggested that proteins of this type may play an important role in the CD4-independent association of HIV with cells.
Contact between dendritic cells (DCs) and resting T cells is essential to initiate a primary immune response. Geijtenbeek et al. (2000) demonstrated that intercellular adhesion molecule-3 (ICAM3; 146631) expressed by resting T cells is important in this first contact with DCs. They discovered that instead of the common ICAM3 receptors LFA1 (see 153370) and alpha-D-beta-2, a novel DC-specific C-type lectin, which they called DCSIGN (DC-specific ICAM3-grabbing nonintegrin), binds ICAM3 with high affinity. DCSIGN is a type II transmembrane protein consisting of 404 amino acids with 3 distinct domains. The 40-amino acid N-terminal cytoplasmic domain is separated by a hydrophobic stretch of 15 amino acids from a region consisting of 1 incomplete and 7 complete tandem repeats of nearly identical sequence. The extracellular C-terminal region (cys253 to ala404) shows homology to C-type lectins. Sequence analysis revealed that DCSIGN is identical to the HIV-1 gp120-binding protein described by Curtis et al. (1992). DCSIGN, which is abundantly expressed by DCs both in vitro and in vivo, mediates transient adhesion with T cells. Since antibodies against DCSIGN inhibited DC-induced proliferation of resting T cells, these findings predicted that DCSIGN enables T-cell receptor engagement by stabilization of the DC/T-cell contact zone.
Soilleux et al. (2000) also cloned CD209. They noted that CD209 has dileucine and YXXL internalization motifs in its cytoplasmic tail. It also contains extracellular carbohydrate recognition domains, which are involved in calcium-dependent mannose binding, that are encoded by 3 separate exons, a structure also found in CD23 (151445). RT-PCR analysis detected CD209 expression in placenta and, at lower levels, in endometrium and a DC line.
DCs capture microorganisms that enter peripheral mucosal tissues, and then migrate to secondary lymphoid organs, where they present these in antigenic form to resting T cells, thus initiating adaptive immune responses. Geijtenbeek et al. (2000) described the properties of DCSIGN, which is highly expressed on DCs present in mucosal tissues and binds to the HIV-1 envelope glycoprotein gp120. DCSIGN does not function as a receptor for viral entry into DCs but instead promotes efficient infection in trans of cells that express CD4 and chemokine receptors. Geijtenbeek et al. (2000) proposed that DCSIGN efficiently captures HIV-1 in the periphery and facilitates its transport to secondary lymphoid organs rich in T cells, to enhance infection in trans of these target cells.
Dengue virus (DV) is a mosquito-borne flavivirus that primarily targets DCs and causes hemorrhagic fever in humans (see 614371). Navarro-Sanchez et al. (2003) found that anti-DCSIGN and the soluble tetrameric ectodomain of DCSIGN inhibited DV infection. The data indicated that DCSIGN functions as a DV-binding lectin that interacts as an attachment factor with the DV envelope glycoprotein.
Using primary DCs naturally expressing DCSIGN and cell lines transfected with DCSIGN or its liver/lymph node-specific homolog, LSIGN (CD209L; 605872), Tassaneetrithep et al. (2003) showed that extensive infection by all 4 DV serotypes was dependent on expression of these lectins. Fluorescence microscopy indicated that DV infection could be blocked by antibody to DCSIGN but not by antibodies to other molecules expressed on DCs. Mutation analysis indicated that the cytoplasmic domain of DCSIGN enhanced but was not essential for infection. Because of the wide array of pathogens whose infectivity is DCSIGN-dependent, Tassaneetrithep et al. (2003) proposed that DCSIGN recognizes pathogen-associated microbial patterns, or PAMPs.
Geijtenbeek et al. (2003) found that DCSIGN captured and internalized intact Mycobacterium bovis BCG or avirulent M. tuberculosis (see 607948) through the glycolipid mycobacterial cell wall component ManLAM. Both bacilli and ManLAM were targeted to lysosomes and colocalized with LAMP1 (153330) in immature DCs. Antibodies against DCSIGN blocked BCG infection of DCs. Binding of secreted ManLAM to DCSIGN prevented mycobacteria- or LPS-induced DC maturation and induced IL10 (124092) production, suggesting that DCSIGN-ManLAM interaction may interfere with TLR-mediated signaling and development of an antiinflammatory response. Geijtenbeek et al. (2003) proposed that M. tuberculosis may target DCSIGN both to infect DCs and to downregulate DC-mediated immune responses.
Tailleux et al. (2003) showed that M. tuberculosis entered DCs after binding to DCSIGN, whereas the major macrophage receptors for M. tuberculosis, CR3 (see ITGAM; 120980) and MRC1 (153618), played only a minor role in DC infection. Flow cytometric and histopathologic analyses showed expression of DCSIGN on lung DCs from uninfected patients and on lymph node granuloma cells infected with M. tuberculosis.
Using flow cytometric analysis of bronchoalveolar lavage cells from tuberculosis (TB), asthma, and sarcoidosis patients and control individuals, Tailleux et al. (2005) found that most alveolar macrophages from TB patients expressed DCSIGN, whereas the lectin was barely detected in cells from the other subjects. FACS, RT-PCR, and ELISA analyses indicated that M. tuberculosis infection induced DCSIGN expression by a mechanism independent of TLR4 (603030), IL4 (147780), and IL13 (147683). Immunohistochemical analysis showed bacillary concentration in lung regions enriched in DCSIGN-expressing alveolar macrophages. Binding experiments revealed that DCSIGN-expressing alveolar macrophages were preferential targets for M. tuberculosis compared with DCSIGN-negative cells. Tailleux et al. (2005) did not detect IL10 in bronchoalveolar lavage or induction of IL10 in infected cells.
The 2 lectin-coding genes CD209 and CD209L resulted from a duplication of an ancestral gene (Bashirova et al., 2003; Soilleux, 2003). An additional characteristic of both CD209 and CD209L is the presence of a neck region, primarily made up of 7 highly conserved 23-amino acid repeats, that separates the carbohydrate-recognition domain involved in pathogen binding from the transmembrane domain. This neck region presents high nucleotide identity between repeats, both within each molecule and between CD209 and CD209L. This region plays a crucial role in the oligomerization and support of the carbohydrate-recognition domain; therefore, it influences the pathogen-binding properties of these 2 receptors (Barreiro et al., 2005). CD209 is expressed primarily on phagocytic cells such as dendritic cells and macrophages, whereas CD209L expression is restricted to endothelial cells in liver and lymph nodes.
By challenging DCs with different phleboviruses, including Rift Valley fever and Uukuniemi viruses, in the presence or absence of antibody to DCSIGN, Lozach et al. (2011) demonstrated that DCSIGN was required for DC infection. Cells lacking DCSIGN resisted phlebovirus challenge, but they became susceptible when transfected with DCSIGN. Binding by DCSIGN, which was followed by virus internalization and infection, occurred via interactions with high-mannose N-glycans on viral glycoproteins. Mutation of DCSIGN to ablate endocytosis prevented infection. Lozach et al. (2011) concluded that DCSIGN is a phlebovirus entry receptor.
Lefevre et al. (2013) observed increased mRNA and protein expression for the C-lectin receptors dectin-1 (CLEC7A; 606264), Mr (MRC1), and Signr3, a mouse homolog of CD209, in mice infected with Leishmania infantum (Li) (see 608207). Mice lacking dectin-1 or Mr, but not those lacking Signr3, had higher parasite levels in blood and spleen. Peritoneal macrophages from dectin-1 -/- or Mrc1 -/- mice, but not Signr3 -/- mice, permitted Li growth and exhibited poor production of reactive oxygen species (ROS). ROS production required dectin-1-Syk (600085)-p47-phox (NCF1; 608512) phosphorylation and Mr-arachidonic acid-Nadph oxidase (NOX1; 300225) membrane translocation. Dectin-1 and Mr facilitated release of Il1b (147720) induced by Casp1 (147678) in response to Li infection, whereas Il1b was downregulated by Signr3 through Lta4h (151570). In human macrophages, small interfering RNA-mediated inactivation of CLEC7A and MRC1, but not CD209, resulted in responses to Li similar to those observed in mice. Lefevre et al. (2013) concluded that Leishmania-macrophage interaction is influenced by the stage of macrophage polarization (i.e., by cytokine and stimulatory milieu) and by members of the C-lectin receptor family. They proposed that alteration of these cellular and molecular factors may benefit patient responses.
Crystal Structure
Feinberg et al. (2001) generated crystal structures of DCSIGN and DCSIGNR and showed that the carbohydrate-recognition domains (CRDs) of both are specific for high-mannose N-linked oligosaccharides, such as those present on the envelope of HIV-1. One monomer of the DCSIGN pair of CRDs interacts with the terminal N-acetylglucosamine of GlcNAc1, while the partner monomer of DCSIGNR is bound to Ca+. Feinberg et al. (2001) proposed that the mechanistic basis of DCSIGN- and DCSIGNR-oligosaccharide interaction provides a starting point to the design of both therapeutic and prophylactic attacks on HIV-1 infection.
Cryoelectron Microscopy
Using cryoelectron microscopy, Pokidysheva et al. (2006) determined the structure of DV serotype-2 (DV2) in complex with the CRD of human DCSIGN at 25-angstrom resolution. The structure showed that 1 CRD monomer binds to 2 glycosylation sites at asn67 of 2 neighboring DV envelope glycoproteins in each icosahedral asymmetric unit. The vacancy at the third asn67 site leaves space for primary DV receptor binding to domain III of the envelope protein. Pokidysheva et al. (2006) suggested that the use of carbohydrate moieties for receptor binding sites may be a mechanism for avoiding immune surveillance.
By genomic sequence analysis, Soilleux et al. (2000) determined that the CD209 gene contains 7 exons.
Soilleux et al. (2000) mapped the CD209 gene to 19p13.3, in a cluster with the CD209L (605872) and CD23 genes, by radiation hybrid analysis.
The lectin-coding genes CD209 and CD209L, which resulted from a duplication of an ancestral gene, are located within a segment of approximately 26 kb (Barreiro et al., 2005).
The innate immunity system constitutes the first line of host defense against pathogens. Two closely related innate immunity genes, CD209 and CD209L, directly recognize a cluster of pathogens, including bacteria, viruses, and parasites. To explore the extent to which pathogens have exerted selective pressure on these innate immunity genes, Barreiro et al. (2005) resequenced them in a group of samples from sub-Saharan Africa, Europe, and East Asia. Moreover, variation in the number of repeats in the neck region was defined in the entire Human Genome Diversity Panel for both genes. The results, which were based on diversity levels, neutrality tests, population genetic distances, and neck-region length variation, provided genetic evidence that CD209 has been under a strong selective constraint that prevents accumulation of any amino acid changes, whereas CD209L variability has most likely been shaped by the action of balancing selection in non-African populations. In addition, the data pointed to the neck region as the functional target of such selective pressures: CD209 presented a constant size in the neck region populationwide, whereas CD209L presented an excess of length variation, particularly in non-African populations. An additional interesting observation came from the coalescent-based CD209 gene tree, whose binary typology and time depth (approximately 2.8 million years ago) were compatible with an ancestral population structure in Africa.
Martin et al. (2004) found that European Americans at risk for parenteral HIV infection were more likely to carry the -336C SNP than the -336T SNP (604672.0001) in the promoter of DCSIGN. This association was not observed in those at risk for mucosally acquired infection. Although the -336C SNP was common in African Americans, no significant association with risk of infection was observed in this group.
Sakuntabhai et al. (2005) found that the same CD209 promoter polymorphism reported by Martin et al. (2004), which Sakuntabhai et al. (2005) called -336A-G, was associated with severity of dengue disease (614371). Specifically, the G allele of the variant was associated with strong protection against dengue fever as opposed to dengue hemorrhagic fever. These results indicated that CD209 has a crucial role in dengue pathogenesis, which discriminates between severe dengue fever and dengue hemorrhagic fever.
Barreiro et al. (2006) examined CD209 polymorphisms in 351 TB patients and 360 healthy controls from a South African Coloured population (historically derived from Khoisan, Malaysian, Bantu, and European descent populations) living in communities with some of the highest reported incidence rates of TB in the world. They identified 2 CD209 promoter variants, -871A (604672.0002) and -336G, that were associated with increased risk of TB. One haplotype of 8 SNPs, including -871G and -336A, showed a highly significant association with the control group. Further analysis of sub-Saharan African, European, and Asian populations showed that the protective -336A and -871G alleles were present at higher frequencies in Eurasians than in Africans. Barreiro et al. (2006) suggested that the longer and more intense duration of TB exposure in Europe may have exerted stronger selective pressures in this population and may have had an impact on susceptibility to infection by other pathogens, such as HIV and dengue.
Using a mouse model of food allergy, Zhou et al. (2010) found that mice pretreated with bovine serum albumin (BSA) with 51 molecules of mannoside (Man51-BSA) plus cholera toxin via oral delivery exhibited reduced BSA-induced anaphylaxis compared with mice pretreated with BSA plus cholera toxin. Man51-BSA selectively targeted lamina propria DCs (LPDCs) expressing Signr1, a mouse homolog of CD209 and CLEC4M, and induced Il10, but not Il6 (147620) or Il12 p70 (see 161560). Man51-BSA induced the same effects in Il10-GFP knockin (tiger) mice. Interaction of Man51-BSA with Signr1 resulted in the generation of Cd4-positive type-1 regulatory-like (Tr1-like) cells that expressed Il10 and Ifng (147570) in a Signr1- and Il10-dependent manner, but not Cd4-positive/Cd25 (IL2RA; 147730)-positive/Foxp3 (300292)-positive regulatory T cells. Tolerance could be transferred by the Tr1-like cells. Zhou et al. (2010) proposed that sugar-modified antigens may be useful in inducing tolerance by targeting Signr1 homologs and LPDCs.
To characterize the immunologic response associated with intravenous immunoglobulin administration, Anthony et al. (2011) generated humanized DCSIGN mice (hDCSIGN), and demonstrated that the antiinflammatory activity of intravenous immunoglobulin can be recapitulated by transfer into naive recipients of bone marrow-derived DCSIGN+ macrophages or dendritic cells treated with IgG crystallizable fragments (Fc) that contain glycans terminating in alpha-2,6 sialic acids (sFc). Furthermore, sFc administration resulted in the production of IL33 (608678), which, in turn, induced expansion of IL4 (147780)-producing basophils that promote increased expression of the inhibitory Fc receptor Fc-gamma-RIIB (604590) on effector macrophages. Systemic administration of the TH2 cytokines IL33 or IL4 upregulated Fc-gamma-RIIB on macrophages and suppressed serum-induced arthritis. Consistent with these results, transfer of IL33-treated basophils suppressed induced arthritic inflammation. Anthony et al. (2011) suggested that this novel DCSIGN-TH2 pathway initiated by an endogenous ligand, sFc, provides an intrinsic mechanism for maintaining immune homeostasis that could be manipulated to provide therapeutic benefit in autoimmune diseases.
By transplanting hearts into fully mismatched recipient mice and treating the recipients with anti-Cd40lg (300386) to induce tolerance, Conde et al. (2015) demonstrated that the monocyte-derived macrophage population required for tolerance expressed Dcsign. Conde et al. (2015) concluded that DCSIGN-positive suppressive macrophages are crucial mediators of immunologic tolerance.
Martin et al. (2004) found that European Americans at risk for parenteral HIV infection (see 609423) were more likely to carry the -336C SNP than the -336T SNP in the promoter of DCSIGN. This association was not observed in those at risk for mucosally acquired infection. Although the -336C SNP was common in African Americans, no significant association with risk of infection was observed in this group.
Sakuntabhai et al. (2005) reported strong association between the -336A-G polymorphism in the promoter of CD209, which they called DCSIGN1-336, and risk of dengue fever (614371). The G allele of the variant was associated with strong protection against dengue fever in 3 independent cohorts from Thailand, with a carrier frequency of 4.7% in individuals with dengue fever compared with 22.4% in individuals with dengue hemorrhagic fever (odds ratio for risk of dengue hemorrhagic fever vs dengue fever = 5.84) and 19.5% in controls (odds ratio for protection = 4.90). This variant affects an Sp1-like binding site and transcriptional activity in vitro. Carrington (2006) confirmed that the -336T-C SNP reported by Martin et al. (2004) and the -336A-G SNP reported by Sakuntabhai et al. (2005) are the same variant.
Barreiro et al. (2006) found an association between susceptibility to tuberculosis (607948) and -336G in a South African Coloured population.
Barreiro et al. (2006) found an association between susceptibility to tuberculosis (607948) and -871A in a South African Coloured population. The putative protective -871G allele was absent in a sample of sub-Saharan Africans, but was present in 12%, 21%, and 38% of South African Coloured, Asian, and European populations, respectively.
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