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CD209 encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages.
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The DC-SIGN -336G/A polymorphism significantly affects dengue hemorrhagic fever and dengue fever incidence with the effect more pronounced in certain analyzed patient subgroups (Meta-Analysis).
The results suggest that DC-SIGN SNPs rs7252229, rs4804803, and rs735240 may influence nasopharyngeal carcinoma risk in the Chinese population.
Polymorphism of CD209 and TLR3 (show TLR3 Proteins) genes in populations of North Eurasia
searched for the relationship between single nucleotide polymorphism in the promoter region of the CD209, IL-10, IL-28 and 32 base pair deletion in CCR5 coding region (Delta 32) with the human predisposition to development of various clinical presentations of tick-borne encephalitis
These results show that DC-SIGN and TLR-4 (show TLR4 Proteins) interactions regulate inflammatory responses in renal tubular epithelial cells and participate in AKI pathogenesis.
1,25(OH)2D3 suppressed the DCSIGN expression in Mycobacterium tuberculosis infected onocytes/macrophages.
Studied the association of CD209 promoter haplotypes with risk of HIV-1 infection in a cohort of Spanish male intravenous drug users (IDU) infected with hepatitis C virus (HCV).
Upon gp120 (show ITIH4 Proteins) binding to DC-SIGN, cellular NF-kappaB (show NFKB1 Proteins) signaling was triggered, leading to the induction of matrix metalloproteinases, which subsequently degraded tight junction proteins and disrupted the blood-retinal barrier integrity.
This study showed that N-glycans on the Gc and Gn surface glycoproteins redundantly support Rift Valley Fever Virus infection via DC-SIGN.
Ligand-driven triggering of TLR-3 (show TLR3 Proteins), -4, NOD2, and DC-SIGN, despite reducing viral replication, markedly increased the capacity of infected dendritic cells to stimulate HIV-specific cytotoxic T-cells.
The development and use of CD209 to characterize the phenotype of CD209 expressing cells in bovine blood using flow cytometry is reported.
a DC-SIGN-like molecule expressed specifically by bovine DC. This molecule may play an important role in the infection of bovine (DC) cells with M. bovis.
DC-SIGN+ cells showed a clear differential distribution in the decidua in the first 2 weeks of pregnancy, being found only adjacent to the implantation site
DC-SIGN expression in mesenteric lymph nodes is significantly downregulated in simian immunodeficiency virus-infected pig-tailed macaques.
The cloning and characterization of the cDNA and gene encoding porcine DC-SIGN (pDC (show PDC Proteins)-SIGN)is reported. The results will help better understand the biological role(s) of DC-SIGN family in innate immunity during the evolutionary process.
identification and functional characterization of DC-SIGN/CD209 molecule in zebrafish
M. scrofulaceum induces a semimature DC phenotype that is characterized by PD-L2 (show PDCD1LG2 Proteins) over-expression and elevated synthesis of IL-10 (show IL10 Proteins), most likely through TLR4 (show TLR4 Proteins) and Raf-1 (show RAF1 Proteins) signaling pathway-dependent DC-SIGN stimulation.
results suggested that podocytes in lupus nephritis can exert dendritic cell-like function through their expression of DC-SIGN, which may be involved in immune and inflammatory responses of renal tissues
High-resolution crystal structures of the SIGN-R1 carbohydrate recognition domain show 2 binding sites allowing SIGNR1 (show CD209B Proteins) to simultaneously bind both immune glycoproteins and microbial polysaccharide components.
Data suggest that serum amyloid P (SAP (show APCS Proteins)) activates CD209 DC-SIGN to regulate the innate immune system differently from C-reactive protein (CRP (show CRP Proteins)), and that DC-SIGN is a target for antifibrotics.
Intestinal enterocytes regulate tissue-associated immune compartments under the control of DC-SIGN in inflammatory bowel disease.
In vivo T cell activation induces the formation of CD209(+) PDL-2 (show PDCD1LG2 Proteins)(+) dendritic cells.
CD209a expression on dendritic cells is critical for the development of pathogenic Th17 cell responses in murine schistosomiasis.
CD209a is activated in macrophages by LECT2 (show LECT2 Proteins).
The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells
interactions between the CRD (show CRX Proteins) of DC-SIGN and the extracellular matrix and/or cis (show CISH Proteins) interactions with transmembrane scaffolding protein(s) play an essential role in organizing these microdomains
This gene encodes a transmembrane receptor and is often referred to as DC-SIGN because of its expression on the surface of dendritic cells and macrophages. The encoded protein is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses with a large impact on public health. The protein is organized into three distinct domains: an N-terminal transmembrane domain, a tandem-repeat neck domain and C-type lectin carbohydrate recognition domain. The extracellular region consisting of the C-type lectin and neck domains has a dual function as a pathogen recognition receptor and a cell adhesion receptor by binding carbohydrate ligands on the surface of microbes and endogenous cells. The neck region is important for homo-oligomerization which allows the receptor to bind multivalent ligands with high avidity. Variations in the number of 23 amino acid repeats in the neck domain of this protein are rare but have a significant impact on ligand binding ability. This gene is closely related in terms of both sequence and function to a neighboring gene (GeneID 10332\; often referred to as L-SIGN). DC-SIGN and L-SIGN differ in their ligand-binding properties and distribution. Alternative splicing results in multiple variants.
C-type lectin domain family 4 member L
, C-type lectin domain family 4, member L
, CD209 antigen
, HIV gpl20-binding protein
, dendritic cell-specific ICAM-3-grabbing non-integrin 1
, dendritic cell-specific intracellular adhesion molecules (ICAM)-3 grabbing non-integrin
, CD209-like protein
, dendritic cell-specific ICAM-3 grabbing non-integrin
, C-type lectin domain family 4, member M
, DC-SIGN protein
, putative mannose-binding C-type lectin
, CD209 antigen-like protein A
, dendritic cell-specific ICAM-3-grabbing non-integrin
, CD209 antigen-like protein C
, CD209c antigen
, Dendritic cell-specific ICAM-3-grabbing non-integrin 1
, dendritic cell-specific ICAM-3 grabbing nonintegrin