Journal articles: 'C-type lectin receptors'

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SUZUKI-INOUE, Katsue. "C-type lectin receptors." Japanese Journal of Thrombosis and Hemostasis 26, no. 1 (2015): 29–34. http://dx.doi.org/10.2491/jjsth.26.29.

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Jégouzo, Sabine A. F., Conor Nelson, Thomas Hardwick, S. T. Angel Wong, Noel Kuan Kiat Lau, Gaik Kin Emily Neoh, Rocío Castellanos-Rueda, et al. "Mammalian lectin arrays for screening host–microbe interactions." Journal of Biological Chemistry 295, no. 14 (February 24, 2020): 4541–55. http://dx.doi.org/10.1074/jbc.ra120.012783.

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Many members of the C-type lectin family of glycan-binding receptors have been ascribed roles in the recognition of microorganisms and serve as key receptors in the innate immune response to pathogens. Other mammalian receptors have become targets through which pathogens enter target cells. These receptor roles have often been documented with binding studies involving individual pairs of receptors and microorganisms. To provide a systematic overview of interactions between microbes and the large complement of C-type lectins, here we developed a lectin array and suitable protocols for labeling of microbes that could be used to probe this array. The array contains C-type lectins from cow, chosen as a model organism of agricultural interest for which the relevant pathogen–receptor interactions have not been previously investigated in detail. Screening with yeast cells and various strains of both Gram-positive and -negative bacteria revealed distinct binding patterns, which in some cases could be explained by binding to lipopolysaccharides or capsular polysaccharides, but in other cases they suggested the presence of novel glycan targets on many of the microorganisms. These results are consistent with interactions previously ascribed to the receptors, but they also highlight binding to additional sugar targets that have not previously been recognized. Our findings indicate that mammalian lectin arrays represent unique discovery tools for identifying both novel ligands and new receptor functions.

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Mischenko, A. A. "Transmembrane C-type lectin receptors in immunity." Вестник Сыктывкарского университета. Серия 2: Биология. Геология. Химия. Экология, no. 4 (2021): 8–21. http://dx.doi.org/10.34130/2306-6229-2021-4-8.

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Wevers, Brigitte A., Teunis BH Geijtenbeek, and Sonja I. Gringhuis. "C-type lectin receptors orchestrate antifungal immunity." Future Microbiology 8, no. 7 (July 2013): 839–54. http://dx.doi.org/10.2217/fmb.13.56.

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Willment, Janet A., and Gordon D. Brown. "C-type lectin receptors in antifungal immunity." Trends in Microbiology 16, no. 1 (January 2008): 27–32. http://dx.doi.org/10.1016/j.tim.2007.10.012.

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Hardison, Sarah E., and Gordon D. Brown. "C-type lectin receptors orchestrate antifungal immunity." Nature Immunology 13, no. 9 (August 21, 2012): 817–22. http://dx.doi.org/10.1038/ni.2369.

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Upham, Jacqueline P., Danielle Pickett, Tatsuro Irimura, E. Margot Anders, and Patrick C. Reading. "Macrophage Receptors for Influenza A Virus: Role of the Macrophage Galactose-Type Lectin and Mannose Receptor in Viral Entry." Journal of Virology 84, no. 8 (January 27, 2010): 3730–37. http://dx.doi.org/10.1128/jvi.02148-09.

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ABSTRACT Although sialic acid has long been recognized as the primary receptor determinant for attachment of influenza virus to host cells, the specific receptor molecules that mediate viral entry are not known for any cell type. For the infection of murine macrophages by influenza virus, our earlier study indicated involvement of a C-type lectin, the macrophage mannose receptor (MMR), in this process. Here, we have used direct binding techniques to confirm and characterize the interaction of influenza virus with the MMR and to seek additional macrophage surface molecules that may have potential as receptors for viral entry. We identified the macrophage galactose-type lectin (MGL) as a second macrophage membrane C-type lectin that binds influenza virus and is known to be endocytic. Binding of influenza virus to MMR and MGL occurred independently of sialic acid through Ca2+-dependent recognition of viral glycans by the carbohydrate recognition domains of the two lectins; influenza virus also bound to the sialic acid on the MMR. Multivalent ligands of the MMR and MGL inhibited influenza virus infection of macrophages in a manner that correlated with expression of these receptors on different macrophage populations. Influenza virus strain A/PR/8/34, which is poorly glycosylated and infects macrophages poorly, was not recognized by the C-type lectin activity of either the MMR or the MGL. We conclude that lectin-mediated interactions of influenza virus with the MMR or the MGL are required for the endocytic uptake of the virus into macrophages, and these lectins can thus be considered secondary or coreceptors with sialic acid for infection of this cell type.

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Marakalala, Mohlopheni J., and Hlumani Ndlovu. "Signaling C-type lectin receptors in antimycobacterial immunity." PLOS Pathogens 13, no. 6 (June 22, 2017): e1006333. http://dx.doi.org/10.1371/journal.ppat.1006333.

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Shiokawa, Moe, Sho Yamasaki, and Shinobu Saijo. "C-type lectin receptors in anti-fungal immunity." Current Opinion in Microbiology 40 (December 2017): 123–30. http://dx.doi.org/10.1016/j.mib.2017.11.004.

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Redelinghuys, Pierre, and Gordon D. Brown. "Inhibitory C-type lectin receptors in myeloid cells." Immunology Letters 136, no. 1 (April 2011): 1–12. http://dx.doi.org/10.1016/j.imlet.2010.10.005.

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Pyż, Elwira, Andrew S. J. Marshall, Siamon Gordon, and Gordon D. Brown. "C‐type lectin‐like receptors on myeloid cells." Annals of Medicine 38, no. 4 (January 2006): 242–51. http://dx.doi.org/10.1080/07853890600608985.

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Ruland, J. "C-type Lectin Receptors: Signaling and Therapeutic Opportunities." Arzneimittelforschung 62, S 01 (December 4, 2012): S17. http://dx.doi.org/10.1055/s-0032-1324910.

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van Kooyk, Yvette. "C-type lectins on dendritic cells: key modulators for the induction of immune responses." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1478–81. http://dx.doi.org/10.1042/bst0361478.

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DCs (dendritic cells) are specialized in the recognition of pathogens and play a pivotal role in the control of immune responses. DCs are also important for homoeostatic control, recognizing self-antigens and tolerizing the tissue environment. The nature of the antigen recognized tilts the balance towards immunity or tolerance. CLRs (C-type lectin receptors) expressed by DC are involved in the recognition and capture of many glycosylated self-antigens and pathogens. It is now becoming clear that these CLRs may not only serve as antigen receptors allowing internalization and antigen presentation, but also function in the recognition of glycosylated self-antigens, and as adhesion and/or signalling molecules. The expression of C-type lectins is very sensitive to maturation stimuli, leading to down-regulation as DCs mature. CLRs such as DC-SIGN (DC-specific intracellular adhesion molecule-3 grabbing non-integrin) recognizes high-mannose-containing structures and Lewis antigens (Lex, Ley, Leb and Lea), whereas the CLR MGL (macrophage galactose/N-acetylgalactosamine-specific C-type lectin) recognizes GalNAc. Lex, Ley and GalNAc glycan structures are often expressed on tumours. We have demonstrated that glycan modification of antigen can strongly enhance MHC class I responses and the induction of antigen-specific cytotoxic T-lymphocytes, indicating that glycosylated antigen targets C-type lectin to enhance antigen-specific T-cell responses. Moreover, these CLRs induce signalling processes in DCs and specific cytokine responses in combination with TLR (Toll-like receptor) triggering. This implies that specific C-type lectin-targeted antigens can regulate T-cell polarization. Understanding the diversity of C-type lectins being expressed on DCs as well as their carbohydrate-specific recognition profiles should promote understanding of pathogen recognition in many diseases, as well as the regulation of cellular interactions of DCs that are essential in the control of immunity.

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Torigoe, Shota, Charles R. Schutt, and Sho Yamasaki. "Immune discrimination of the environmental spectrum through C-type lectin receptors." International Immunology 33, no. 12 (October 2, 2021): 847–51. http://dx.doi.org/10.1093/intimm/dxab074.

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Abstract Our bodies are continuously assaulted by infection and tissue damage; most of these injurious insults are primarily sensed by immune receptors to maintain tissue homeostasis. Although immune recognition of proteins or nucleic acids has been well characterized, the molecular mechanisms by which immune receptors discriminate lipids to elicit suitable immune responses remain elusive. Recent studies have demonstrated that the C-type lectin receptor family functions as immune sensors for adjuvant lipids derived from pathogens and damaged tissues, thereby promoting innate/acquired immunity. In this review, we will discuss how these receptors recognize lipid components to initiate appropriate, but sometimes deleterious, immune responses against environmental stimuli. We will also discuss an aspect of inhibitory C-type lectin receptors; their ligands might reflect normal self which silences the immune response regarded as “silence”-associated molecular patterns or may be associated with escape strategies of pathogens as “evasion”-associated molecular patterns.

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Eble, Johannes. "Structurally Robust and Functionally Highly Versatile—C-Type Lectin (-Related) Proteins in Snake Venoms." Toxins 11, no. 3 (March 1, 2019): 136. http://dx.doi.org/10.3390/toxins11030136.

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Snake venoms contain an astounding variety of different proteins. Among them are numerous C-type lectin family members, which are grouped into classical Ca2+- and sugar-binding lectins and the non-sugar-binding snake venom C-type lectin-related proteins (SV-CLRPs), also called snaclecs. Both groups share the robust C-type lectin domain (CTLD) fold but differ in a long loop, which either contributes to a sugar-binding site or is expanded into a loop-swapping heterodimerization domain between two CLRP subunits. Most C-type lectin (-related) proteins assemble in ordered supramolecular complexes with a high versatility of subunit numbers and geometric arrays. Similarly versatile is their ability to inhibit or block their target molecules as well as to agonistically stimulate or antagonistically blunt a cellular reaction triggered by their target receptor. By utilizing distinct interaction sites differentially, SV-CLRPs target a plethora of molecules, such as distinct coagulation factors and receptors of platelets and endothelial cells that are involved in hemostasis, thrombus formation, inflammation and hematogenous metastasis. Because of their robust structure and their high affinity towards their clinically relevant targets, SV-CLRPs are and will potentially be valuable prototypes to develop new diagnostic and therapeutic tools in medicine, provided that the molecular mechanisms underlying their versatility are disclosed.

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Streng-Ouwehand, Ingeborg, Wendy W. J. Unger, and Yvette Van Kooyk. "C-type Lectin Receptors for Tumor Eradication: Future Directions." Cancers 3, no. 3 (August 8, 2011): 3169–88. http://dx.doi.org/10.3390/cancers3033169.

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Clemetson, Kenneth J., Qiumin Lu, and Jeannine M. Clemetson. "Snake C-Type Lectin-Like Proteins and Platelet Receptors." Pathophysiology of Haemostasis and Thrombosis 34, no. 4-5 (2005): 150–55. http://dx.doi.org/10.1159/000092414.

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Geijtenbeek, Teunis B. H., and Sonja I. Gringhuis. "Signalling through C-type lectin receptors: shaping immune responses." Nature Reviews Immunology 9, no. 7 (July 2009): 465–79. http://dx.doi.org/10.1038/nri2569.

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Hoving, J. Claire, Gillian J. Wilson, and Gordon D. Brown. "Signalling C-Type lectin receptors, microbial recognition and immunity." Cellular Microbiology 16, no. 2 (January 10, 2014): 185–94. http://dx.doi.org/10.1111/cmi.12249.

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Vautier, Simon, Donna M. MacCallum, and Gordon D. Brown. "C-type lectin receptors and cytokines in fungal immunity." Cytokine 58, no. 1 (April 2012): 89–99. http://dx.doi.org/10.1016/j.cyto.2011.08.031.

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Lepenies, Bernd, Junghoon Lee, and Sanjiv Sonkaria. "Targeting C-type lectin receptors with multivalent carbohydrate ligands." Advanced Drug Delivery Reviews 65, no. 9 (August 2013): 1271–81. http://dx.doi.org/10.1016/j.addr.2013.05.007.

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Goyal, Surabhi, Tilman E. Klassert, and Hortense Slevogt. "C-type lectin receptors in tuberculosis: what we know." Medical Microbiology and Immunology 205, no. 6 (July 28, 2016): 513–35. http://dx.doi.org/10.1007/s00430-016-0470-1.

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Pustylnikov, Sergey, Divya Sagar, Pooja Jain, and Zafar K. Khan. "Targeting the C-type Lectins-Mediated Host-Pathogen Interactions with Dextran." Journal of Pharmacy & Pharmaceutical Sciences 17, no. 3 (August 18, 2014): 371. http://dx.doi.org/10.18433/j3n590.

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Dextran, the α-1,6-linked glucose polymer widely used in biology and medicine, promises new applications. Linear dextran applied as a blood plasma substitute demonstrates a high rate of biocompatibility. Dextran is present in foods, drugs, and vaccines and in most cases is applied as a biologically inert substance. In this review we analyze dextran's cellular uptake principles, receptor specificity and, therefore, its ability to interfere with pathogen–lectin interactions: a promising basis for new antimicrobial strategies. 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. These receptors take part in the uptake of pathogens by dendritic cells and macrophages and may also participate in the modulation of immune responses, mostly shown to be beneficial for pathogens per se rather than host(s). It is logical to predict that owing to receptor-specific interactions, dextran or its derivatives can interfere with these immune responses and improve infection outcome. Recent data support this hypothesis. We consider dextran a promising molecule for the development of lectin–glycan interaction-blocking molecules (such as DC-SIGN inhibitors) that could be applied in the treatment of diseases including tuberculosis, influenza, hepatitis B and C, human immunodeficiency virus infection and AIDS, etc. Dextran derivatives indeed change the pathology of infections dependent on DC-SIGN and mannose receptors. Complete knowledge of specific dextran–lectin interactions may also be important for development of future dextran applications in biological research and medicine. This article is open to POST-PUBLICATION REVIEW. Registered readers (see “For Readers”) may comment by clicking on ABSTRACT on the issue’s contents page.

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McGreal, Eamon P., Joanna L. Miller, and Siamon Gordon. "Ligand recognition by antigen-presenting cell C-type lectin receptors." Current Opinion in Immunology 17, no. 1 (February 2005): 18–24. http://dx.doi.org/10.1016/j.coi.2004.12.001.

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Sancho, David, and Caetano Reis e Sousa. "Sensing of cell death by myeloid C-type lectin receptors." Current Opinion in Immunology 25, no. 1 (February 2013): 46–52. http://dx.doi.org/10.1016/j.coi.2012.12.007.

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Figdor, Carl G., Yvette van Kooyk, and Gosse J. Adema. "C-type lectin receptors on dendritic cells and langerhans cells." Nature Reviews Immunology 2, no. 2 (February 1, 2002): 77–84. http://dx.doi.org/10.1038/nri723.

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Yan, Huimin, Naohito Ohno, and Noriko M. Tsuji. "The role of C-type lectin receptors in immune homeostasis." International Immunopharmacology 16, no. 3 (July 2013): 353–57. http://dx.doi.org/10.1016/j.intimp.2013.04.013.

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Hoober, J. Kenneth. "ASGR1 and Its Enigmatic Relative, CLEC10A." International Journal of Molecular Sciences 21, no. 14 (July 8, 2020): 4818. http://dx.doi.org/10.3390/ijms21144818.

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The large family of C-type lectin (CLEC) receptors comprises carbohydrate-binding proteins that require Ca2+ to bind a ligand. The prototypic receptor is the asialoglycoprotein receptor-1 (ASGR1, CLEC4H1) that is expressed primarily by hepatocytes. The early work on ASGR1, which is highly specific for N-acetylgalactosamine (GalNAc), established the foundation for understanding the overall function of CLEC receptors. Cells of the immune system generally express more than one CLEC receptor that serve diverse functions such as pathogen-recognition, initiation of cellular signaling, cellular adhesion, glycoprotein turnover, inflammation and immune responses. The receptor CLEC10A (C-type lectin domain family 10 member A, CD301; also called the macrophage galactose-type lectin, MGL) contains a carbohydrate-recognition domain (CRD) that is homologous to the CRD of ASGR1, and thus, is also specific for GalNAc. CLEC10A is most highly expressed on immature DCs, monocyte-derived DCs, and alternatively activated macrophages (subtype M2a) as well as oocytes and progenitor cells at several stages of embryonic development. This receptor is involved in initiation of TH1, TH2, and TH17 immune responses and induction of tolerance in naïve T cells. Ligand-mediated endocytosis of CLEC receptors initiates a Ca2+ signal that interestingly has different outcomes depending on ligand properties, concentration, and frequency of administration. This review summarizes studies that have been carried out on these receptors.

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Thiem, Kathrin, Geerte Hoeke, Enchen Zhou, Anneke Hijmans, Tom Houben, Margien G. Boels, Isabel M. Mol, et al. "Deletion of haematopoietic Dectin-2 or CARD9 does not protect from atherosclerosis development under hyperglycaemic conditions." Diabetes and Vascular Disease Research 17, no. 1 (December 23, 2019): 147916411989214. http://dx.doi.org/10.1177/1479164119892140.

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Background: C-type lectin receptors, including Dectin-2, are pattern recognition receptors on monocytes and macrophages that mainly recognize sugars and sugar-like structures present on fungi. Activation of C-type lectin receptors induces downstream CARD9 signalling, leading to the production of cytokines. We hypothesized that under hyperglycaemic conditions, as is the case in diabetes mellitus, glycosylated protein (sugar-like) structures activate C-type lectin receptors, leading to immune cell activation and increased atherosclerosis development. Methods: Low-density lipoprotein receptor-deficient mice were lethally irradiated and transplanted with bone marrow from control wild-type, Dectin-2−/− or Card9−/− mice. After 6 weeks of recovery, mice received streptozotocin injections (50 mg/g BW; 5 days) to induce hyperglycaemia. After an additional 2 weeks, mice were fed a Western-type diet (0.1% cholesterol) for 10 weeks. Results and Conclusion: Deletion of haematopoietic Dectin-2 reduced the number of circulating Ly6Chi monocytes, increased pro-inflammatory cytokine production, but did not affect atherosclerosis development. Deletion of haematopoietic CARD9 tended to reduce macrophage and collagen content in atherosclerotic lesions, again without influencing the lesion size. Deletion of haematopoietic Dectin-2 did not influence atherosclerosis development under hyperglycaemic conditions, despite some minor effects on inflammation. Deletion of haematopoietic CARD9 induced minor alterations in plaque composition under hyperglycaemic conditions, without affecting lesion size.

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Suzuki, N., K. Yamamoto, S. Toyoshima, T. Osawa, and T. Irimura. "Molecular cloning and expression of cDNA encoding human macrophage C-type lectin. Its unique carbohydrate binding specificity for Tn antigen." Journal of Immunology 156, no. 1 (January 1, 1996): 128–35. http://dx.doi.org/10.4049/jimmunol.156.1.128.

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Abstract A human macrophage calcium-dependent (C-type) lectin cDNA clone was obtained from a library derived from IL-2-treated peripheral blood monocytes. The cDNA cloning was based on the structural homology to hepatic asialoglycoprotein receptors. The nucleotide sequence of this cDNA clone was homologous to those of the galactose- and N-acetylgalactosamine-specific C-type macrophage lectins of rodents. In the putative carbohydrate recognition domain, deduced amino acid sequence revealed 60 and 63% homology to galactose- and N-acetylgalactosamine-specific C-type macrophage lectins of mice and rats, respectively. The cDNA clone was ligated into a mammalian expression vector and transfected into COS-1 cells. In the lysates of these cells, an MR 38,000 component, which bound to galactose-Sepharose, was identified after electrophoretic separation by its interaction with polyclonal antisera against synthetic polypeptides representing a portion of the carbohydrate recognition domain. The carbohydrate-binding specificity of the recombinant macrophage lectin was investigated by comparing elution profiles of various glycopeptides having defined carbohydrate structures from immobilized macrophage lectins. When N-terminal octapeptides from human glycophorin A that bore NeuAc alpha 2-3 Gal beta 1-3 (NeuAc alpha 2-6) GalNAc and its sequentially deglycosylated derivatives were compared, glycopeptides carrying three constitutive GalNAc-Ser/Thr (Tn Ag) strongly bound to the recombinant human macrophage lectin. This is the first study to demonstrate that human macrophage cell surface lectin recognizes Tn Ag, a well-known human carcinoma-associated epitope.

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Brudner, Matthew, Marshall Karpel, Calli Lear, Li Chen, L. Michael Yantosca, Corinne Scully, Ashish Sarraju, et al. "Lectin-Dependent Enhancement of Ebola Virus Infection via Soluble and Transmembrane C-type Lectin Receptors." PLoS ONE 8, no. 4 (April 2, 2013): e60838. http://dx.doi.org/10.1371/journal.pone.0060838.

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Lech, Maciej, Heni Eka Susanti, Christoph Römmele, Regina Gröbmayr, Roman Günthner, and Hans-Joachim Anders. "Quantitative Expression of C-Type Lectin Receptors in Humans and Mice." International Journal of Molecular Sciences 13, no. 8 (August 14, 2012): 10113–31. http://dx.doi.org/10.3390/ijms130810113.

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Sionov, Ronit Vogt, Chrystelle Lamagna, and Zvi Granot. "Recognition of Tumor Nidogen-1 by Neutrophil C-Type Lectin Receptors." Biomedicines 10, no. 4 (April 15, 2022): 908. http://dx.doi.org/10.3390/biomedicines10040908.

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Neutrophil-mediated cytotoxicity toward tumor cells requires cell contact and is mediated by hydrogen peroxide. We have recently shown that Cathepsin G expressed on the neutrophil surface interacts with tumor RAGE, and this interaction facilitates neutrophil cytotoxicity. Interruption of the Cathepsin G–RAGE interaction led to 50–80% reduction in cytotoxicity, suggesting that additional interactions are also involved. Here we show that blocking antibodies to the C-type lectin receptors (CLRs) Clec4e and Dectin-1, but not those to NKG2D, attenuated murine neutrophil cytotoxicity towards murine tumor cells, suggesting a contributing role for these CLRs in neutrophil recognition of tumor cells. We further observed that the CLRs interact with tumor Nidogen-1 and Hspg2, two sulfated glycoproteins of the basement membrane. Both Nidogen-1 and Hspg2 were found to be expressed on the tumor cell surface. The knockdown of Nidogen-1, but not that of Hspg2, led to reduced susceptibility of the tumor cells to neutrophil cytotoxicity. Altogether, this study suggests a role for CLR–Nidogen-1 interaction in the recognition of tumor cells by neutrophils, and this interaction facilitates neutrophil-mediated killing of the tumor cells.

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Park, Chae Gyu. "Vaccine strategies utilizing C-type lectin receptors on dendritic cellsin vivo." Clinical and Experimental Vaccine Research 3, no. 2 (2014): 149. http://dx.doi.org/10.7774/cevr.2014.3.2.149.

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Monteiro, João, and Bernd Lepenies. "Myeloid C-Type Lectin Receptors in Viral Recognition and Antiviral Immunity." Viruses 9, no. 3 (March 22, 2017): 59. http://dx.doi.org/10.3390/v9030059.

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Saruhan-Direskeneli, G. "Expression of KIR and C-type lectin receptors in Behcet's disease." Rheumatology 43, no. 4 (January 6, 2004): 423–27. http://dx.doi.org/10.1093/rheumatology/keh063.

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Osorio, Fabiola, and Caetano Reis e Sousa. "Myeloid C-type Lectin Receptors in Pathogen Recognition and Host Defense." Immunity 34, no. 5 (May 2011): 651–64. http://dx.doi.org/10.1016/j.immuni.2011.05.001.

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Sancho, David, and Caetano Reis e Sousa. "Signaling by Myeloid C-Type Lectin Receptors in Immunity and Homeostasis." Annual Review of Immunology 30, no. 1 (April 23, 2012): 491–529. http://dx.doi.org/10.1146/annurev-immunol-031210-101352.

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Figdor, Carl G., Yvette van Kooyk, and Adema Gosse J. "Erratum: C-type lectin receptors on dendritic cells and langerhans cells." Nature Reviews Immunology 2, no. 5 (May 2002): 377. http://dx.doi.org/10.1038/nri827.

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Tang, Ce, Yulia Makusheva, Haiyang Sun, Wei Han, and Yoichiro Iwakura. "Myeloid C‐type lectin receptors in skin/mucoepithelial diseases and tumors." Journal of Leukocyte Biology 106, no. 4 (April 9, 2019): 903–17. http://dx.doi.org/10.1002/jlb.2ri0119-031r.

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Maldonado, Samuel D., Jihong Dai, Orchi Dutta, Harry J. Hurley, Sukhwinder Singh, Lisa Gittens-Williams, Evelyne Kalyoussef, Karen L. Edelblum, Amariliz Rivera, and Patricia Fitzgerald-Bocarsly. "Human Plasmacytoid Dendritic Cells Express C-Type Lectin Receptors and Attach and Respond to Aspergillus fumigatus." Journal of Immunology 209, no. 4 (August 15, 2022): 675–83. http://dx.doi.org/10.4049/jimmunol.2000632.

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Abstract Plasmacytoid dendritic cells (pDCs) have been implicated as having a role in antifungal immunity, but mechanisms of their interaction with fungi and the resulting cellular responses are not well understood. In this study, we identify the direct and indirect biological response of human pDCs to the fungal pathogen Aspergillus fumigatus and characterize the expression and regulation of antifungal receptors on the pDC surface. Results indicate pDCs do not phagocytose Aspergillus conidia, but instead bind hyphal surfaces and undergo activation and maturation via the upregulation of costimulatory and maturation markers. Measuring the expression of C-type lectin receptors dectin-1, dectin-2, dectin-3, and mannose receptor on human pDCs revealed intermediate expression of each receptor compared with monocytes. The specific dectin-1 agonist curdlan induced pDC activation and maturation in a cell-intrinsic and cell-extrinsic manner. The indirect activation of pDCs by curdlan was much stronger than direct stimulation and was mediated through cytokine production by other PBMCs. Overall, our data indicate pDCs express various C-type lectin receptors, recognize and respond to Aspergillus hyphal Ag, and serve as immune enhancers or modulators in the overarching fungal immune response.

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Sagar, Divya, Catherine Foss, Zafar Khan, Martin Pomper, and Pooja Jain. "Lectin-targeted dendritic cell immunotherapies against experimental autoimmune encephalitis/multiple sclerosis (CAM5P.242)." Journal of Immunology 192, no. 1_Supplement (May 1, 2014): 180.13. http://dx.doi.org/10.4049/jimmunol.192.supp.180.13.

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Abstract The molecular mechanisms of how circulating dendritic cells (DCs) access the CNS across the blood-brain barrier (BBB) remains to be investigated. During neuroinflammation, DCs transmigrate across the BBB in the presence of chemoattractants, particularly CCL2, and initiate immune response. We showed through near-infrared imaging that DC accumulation into lesions within the CNS correlated with severity of inflammation during experimental autoimmune encephalitis (EAE). Actin polymerization on DCs upon CCL2 exposure indicated a migratory phenotype. Transmigration of DCs was paracellular and more efficient than T cells in vitro. To selectively attenuate DC transmigration, we sought to study expression of DC specific C type lectin receptors- CD205 & CD206 (Type I), CD207, -209, -303, CLEC4A, -9A, -10A & -12A (Type II). Different DC subsets- myeloid (mDC), plasmacytoid (pDC) and monocyte-derived (MDDC) had a unique enrichment of lectin receptors and each subset utilized a different receptor to adhere and transmigrate in the presence of CCL2. Phosphoproteomics revealed that these receptors when triggered, activate molecular events known to be involved in actin dynamics, thus substantiating their role in DC transmigration. Importantly, in EAE mice these lectins were validated targets for inhibiting DC transmigration. Thus, the prospect of selectively regulating DC entry into the CNS will open up new treatments against disease pathogenesis and propagation in multiple sclerosis.

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Alshehri, Osama M., Samantha Montague, Stephanie Watson, Paul Carter, Najiat Sarker, Bhanu K. Manne, Jeanette L. C. Miller, et al. "Activation of glycoprotein VI (GPVI) and C-type lectin-like receptor-2 (CLEC-2) underlies platelet activation by diesel exhaust particles and other charged/hydrophobic ligands." Biochemical Journal 468, no. 3 (June 15, 2015): 459–73. http://dx.doi.org/10.1042/bj20150192.

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Structurally diverse stimuli induce glycoprotein VI (GPVI) and C-type lectin-like receptor-2 (CLEC-2) activation but also activate other tyrosine kinase-linked receptors. This has pathophysiological significance in situations such as exposure to diesel exhaust particles (DEP) and elevation of histones.

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YANG, Long, Ying WANG, and LeLe ZHU. "Preparation of monoclonal antibody of human C-type lectin receptors dectin-1." Pharmaceutical Care and Research 15, no. 2 (April 30, 2015): 95–146. http://dx.doi.org/10.5428/pcar20150204.

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Willment, Janet A. "Fc‐conjugated C‐type lectin receptors: Tools for understanding host–pathogen interactions." Molecular Microbiology 117, no. 3 (December 6, 2021): 632–60. http://dx.doi.org/10.1111/mmi.14837.

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Tang, Choon-Kit, Kuo-Ching Sheng, Vasso Apostolopoulos, and Geoffrey A. Pietersz. "Protein/peptide and DNA vaccine delivery by targeting C-type lectin receptors." Expert Review of Vaccines 7, no. 7 (September 2008): 1005–18. http://dx.doi.org/10.1586/14760584.7.7.1005.

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Kerscher, Bernhard, Janet A. Willment, and Gordon D. Brown. "The Dectin-2 family of C-type lectin-like receptors: an update." International Immunology 25, no. 5 (April 12, 2013): 271–77. http://dx.doi.org/10.1093/intimm/dxt006.

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Cambi, Alessandra, and Carl G. Figdor. "Dual function of C-type lectin-like receptors in the immune system." Current Opinion in Cell Biology 15, no. 5 (October 2003): 539–46. http://dx.doi.org/10.1016/j.ceb.2003.08.004.

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Turville, Stuart, John Wilkinson, Paul Cameron, Joanne Dable, and Anthony L. Cunningham. "The role of dendritic cell C-type lectin receptors in HIV pathogenesis." Journal of Leukocyte Biology 74, no. 5 (November 2003): 710–18. http://dx.doi.org/10.1189/jlb.0503208.

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Geijtenbeek, Teunis B. H., and Sonja I. Gringhuis. "C-type lectin receptors in the control of T helper cell differentiation." Nature Reviews Immunology 16, no. 7 (June 13, 2016): 433–48. http://dx.doi.org/10.1038/nri.2016.55.

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Journal articles on the topic 'C-type lectin receptors'

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