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C-type lectin domain family 4, member M

This gene encodes a transmembrane receptor and is often referred to as L-SIGN because of its expression in the endothelial cells of the lymph nodes and liver. 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 common and 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 30835; often referred to as DC-SIGN or CD209). DC-SIGN and L-SIGN differ in their ligand-binding properties and distribution. Alternative splicing results in multiple variants.[provided by RefSeq, Feb 2009] (from NCBI)
Top mentioned proteins: DC-SIGN, CAN, ICAM-3, CD45, HAD
Papers on DC-SIGNR
Endocytic function is critical for influenza A virus infection via DC-SIGN and L-SIGN.
Londrigan et al., Melbourne, Australia. In Sci Rep, Dec 2015
The C-type lectin receptors (CLRs) DC-SIGN (CD209) and L-SIGN (CD209L) enhance IAV infection however it is not known if they act as attachment factors, passing virions to other unknown receptors for virus entry, or as authentic entry receptors for CLR-mediated virus uptake and infection.
Virion-associated phosphatidylethanolamine promotes TIM1-mediated infection by Ebola, dengue, and West Nile viruses.
Choe et al., Jupiter, United States. In Proc Natl Acad Sci U S A, Dec 2015
The inhibitory effect of Duramycin is specific: it inhibits TIM1-mediated, but not L-SIGN-mediated, virus infection, and it does so by blocking virus attachment to TIM1.
Lewis Lung Cancer Cells Promote SIGNR1(CD209b)-Mediated Macrophages Polarization Induced by IL-4 to Facilitate Immune Evasion.
Mu et al., Xi'an, China. In J Cell Biochem, Nov 2015
Furthermore, polarized M2 cells immersed in a tumor microenvironment promoted the migration of LLCs, as measured by transwell assays, but migration was suppressed after blockade of SIGNR1 using CD209b antibody.
Association of DC-SIGNR Expression in Peripheral Blood Mononuclear Cells with DC-SIGNR Genotypes in HIV-1 Infection.
Luthra et al., New Delhi, India. In Viral Immunol, Oct 2015
Dendritic cell-specific intracellular adhesion molecule 3 grabbing nonintegrin related molecule (DC-SIGNR) is a C-type lectin, calcium-dependent carbohydrate-binding protein, which can act as a cell-adhesion and pathogen recognition receptor.
Low expression of dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin-related protein in lung cancer and significant correlations with brain metastasis and natural killer cells.
Zuo et al., Dalian, China. In Mol Cell Biochem, Sep 2015
Dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin-related protein (DC-SIGNR) is a type II transmembrane protein which has been reported to bind a variety of pathogens as well as participate in immunoregulation.
[Research on hepatitis C virus entry inhibitor].
Zhu et al., In Bing Du Xue Bao, 2015
the process of HCV entering into host cell is the important step of drug intervention, in which HCV envelope protein El and E2, Host cell factors including Heparan sulfate(HS), CD81, scavenger receptor class B type I (SR-BI), Occludin (OCLD), Claudin (CLDN), low densitity lipoprotein receptor (LDLR), dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN), Liver/lymph node specific ICAM-3-grabbing integrin(L-SIGN), trans- ferrin receptor 1 (TfR1) and so on play a important role.
DC-SIGN, DC-SIGNR and LSECtin: C-type lectins for infection.
Zuo et al., Dalian, China. In Int Rev Immunol, 2014
The C-type lectins DC-SIGN, DC-SIGNR and LSECtin are encoded by the lectin gene cluster on chromosome 19p13.3
Targeting the C-type lectins-mediated host-pathogen interactions with dextran.
Khan et al., Novosibirsk, Russia. In J Pharm Pharm Sci, 2013
Dextran-binding receptors in humans include the DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) family receptors: DC-SIGN (CD209) and L-SIGN (the liver and lymphatic endothelium homologue of DC-SIGN), the mannose receptor (CD206), and langerin.
IgA, IgA receptors, and their anti-inflammatory properties.
Monteiro et al., Paris, France. In Curr Top Microbiol Immunol, 2013
IgA functions mainly through interaction with multiple receptors including IgA Fc receptor I (FcαRI), transferrin receptor 1 (CD71), asialoglycoprotein receptor (ASGPR), Fcα/μR, FcRL4, and DC-SIGN/SIGNR1.
Hepatitis C virus entry: role of host and viral factors.
Jahan et al., Lahore, Pakistan. In Infect Genet Evol, 2012
CD81, SR-BI, LDL-R, CLDN1, Occludin, DC-SIGN, L-SIGN and Glycosaminoglycans).
Difference in fine specificity to polysaccharides of Candida albicans mannoprotein between mouse SIGNR1 and human DC-SIGN.
Inaba et al., Kyoto, Japan. In Infect Immun, 2012
These results indicate that murine SIGNR1 recognizes C. albicans/yeast through a specificity partly distinct from that of its homologue human DC-SIGN.
Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2.
Graham et al., Bethesda, United States. In J Virol, 2012
data demonstrate that the signaling events mediated by RSV G interactions with DC/L-SIGN are immunomodulatory and diminish DC activation, which may limit induction of RSV-specific immunity
Efficient capture of Candida albicans and zymosan by SIGNR1 augments TLR2-dependent TNF-α production.
Inaba et al., Kyoto, Japan. In Int Immunol, 2012
enhances TNF-alpha production by macrophages in cooperation with TLR2 upon microbial recognition
The origin and evolution of variable number tandem repeat of CLEC4M gene in the global human population.
Zhang et al., Nanjing, China. In Plos One, 2011
Findings do not support the hypothesis that the origin of the variable number tandem repeat (VNTR} alleles of CLEC4M were arisen by independent (separate) mutation events.
[Relationship between intrauterine infection and the gene polymorphism of DC-SIGN/DC-SIGNR in the pregnant women of HBV positive].
Tian et al., Hangzhou, China. In Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi, 2011
There were multiple genotypes of the gene DC-SIGNR in the pregnant women infected with HBV.
Oral tolerance to food-induced systemic anaphylaxis mediated by the C-type lectin SIGNR1.
Huang et al., Baltimore, United States. In Nat Med, 2010
sugar-modified antigens might be used to induce oral tolerance by targeting SIGNR1 and dendritic cells in the gastrointestinal lamina propria (LPDCs).
The Immunobiology of SARS*.
Subbarao et al., Bethesda, United States. In Annu Rev Immunol, 2006
Angiotensin-converting enzyme 2 is the functional receptor for SARS-CoV; DC-SIGN and CD209L (L-SIGN) can enhance viral entry.
Homozygous L-SIGN (CLEC4M) plays a protective role in SARS coronavirus infection.
Lin et al., Hong Kong, Hong Kong. In Nat Genet, 2006
genetic risk association study shows that individuals homozygous for CLEC4M tandem repeats are less susceptible to SARS infection.
Human cytomegalovirus binding to DC-SIGN is required for dendritic cell infection and target cell trans-infection.
Déchanet-Merville et al., Bordeaux, France. In Immunity, 2002
Moreover, blocking DC-SIGN by specific antibodies inhibited DC infection by primary CMV isolates and expression of DC-SIGN or its homolog DC-SIGNR rendered susceptible cells permissive to CMV infection.
Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR.
Weis et al., Stanford, United States. In Science, 2002
Crystal structures of carbohydrate-recognition domains of DC-SIGNR bound to oligosaccharide, in combination with binding studies, reveal that it selectively recognizes endogenous high-mannose oligosaccharides
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