Journal articles: 'C-type lectin domain'

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Zelensky, Alex N., and Jill E. Gready. "The C-type lectin-like domain superfamily." FEBS Journal 272, no. 24 (December 2005): 6179–217. http://dx.doi.org/10.1111/j.1742-4658.2005.05031.x.

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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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XU, Qiang, Xiang-Fu WU, Qi-Chang XIA, and Ke-Yi WANG. "Cloning of a galactose-binding lectin from the venom of Trimeresurus stejnegeri." Biochemical Journal 341, no. 3 (July 26, 1999): 733–37. http://dx.doi.org/10.1042/bj3410733.

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A galactose-binding lectin isolated from the venom of Trimeresurus stejnegeri is a homodimer C-type lectin. The cloned cDNA encoding the monomer of Trimeresurus stejnegerilectin (TSL) was sequenced and found to contain a 5′-end non-coding region, a sequence which encodes 135 amino acids, including a typical 23 amino acid signal peptide followed by the mature protein sequence, a 3′-end non-coding region, a polyadenylation signal, and a poly(A) region. To completely characterize the deduced amino acid sequence, on-line HPLC-MS and tandem MS were used to analyse the intact monomer and its proteolytic peptides. A modified peptide fragment was also putatively identified by HPLC-MS analysis. The deduced amino acid sequence was found to contain a carbohydrate-recognition domain homologous with those of some known C-type animal lectins. Thus TSL belongs to group VII of the C-type animal lectins as classified by Drickamer [(1993) Prog. Nucleic Acid Res. Mol. Biol. 45, 207-232]. At present, a number of C-type lectins have been purified from snake venom, but most of them have been characterized only at the protein level. To our knowledge, this is the first known cDNA sequence of a true C-type lectin from snake venom.

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Zhao, Zhi-Ying, Zhi-Xin Yin, Xiao-Peng Xu, Shao-Ping Weng, Xia-Yu Rao, Zong-Xian Dai, Yong-Wen Luo, et al. "A Novel C-Type Lectin from the Shrimp Litopenaeus vannamei Possesses Anti-White Spot Syndrome Virus Activity." Journal of Virology 83, no. 1 (October 22, 2008): 347–56. http://dx.doi.org/10.1128/jvi.00707-08.

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ABSTRACT C-type lectins play key roles in pathogen recognition, innate immunity, and cell-cell interactions. Here, we report a new C-type lectin (C-type lectin 1) from the shrimp Litopenaeus vannamei (LvCTL1), which has activity against the white spot syndrome virus (WSSV). LvCTL1 is a 156-residue polypeptide containing a C-type carbohydrate recognition domain with an EPN (Glu99-Pro100-Asn101) motif that has a predicted ligand binding specificity for mannose. Reverse transcription-PCR analysis revealed that LvCTL1 mRNA was specifically expressed in the hepatopancreas of L. vannamei. Recombinant LvCTL1 (rLvCTL1) had hemagglutinating activity and ligand binding specificity for mannose and glucose. rLvCTL1 also had a strong affinity for WSSV and interacted with several envelope proteins of WSSV. Furthermore, we showed that the binding of rLvCTL1 to WSSV could protect shrimps from viral infection and prolong the survival of shrimps against WSSV infection. Our results suggest that LvCTL1 is a mannose-binding C-type lectin that binds to envelope proteins of WSSV to exert its antiviral activity. To our knowledge, this is the first report of a shrimp C-type lectin that has direct anti-WSSV activity.

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Bezouška, Karel. "Carbohydrate and Non-Carbohydrate Ligands for the C-Type Lectin-Like Receptors of Natural Killer Cells. A Review." Collection of Czechoslovak Chemical Communications 69, no. 3 (2004): 535–63. http://dx.doi.org/10.1135/cccc20040535.

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The superfamily of C-type animal lectins is defined by a sequence motif of the carbohydrate- recognition domains (CRDs) and comprises seven groups of molecules. The soluble proteins are group I proteoglycans, group III collectins, and group VII containing the isolated CRDs. Type I membrane proteins include group IV selectins and group VI macrophage receptors and related molecules. Type II membrane proteins are group II hepatic lectins and group V natural killer cell receptors. The latter group has recently attracted considerable attention of the biomedical community. These receptors are arranged at the surface of lymphocytes as homo- or heterodimers composed of two polypeptides consisting of N-terminal peptide tails responsible for signaling, transmembrane domain, neck regions of varying length, and C-terminal lectin-like domains (CTLDs). Since this group is evolutionarily most distant from the rest of C-type animal lectins, the sequence of the C-terminal ligand-binding domain has diversified to accommodate other ligands than calcium or carbohydrates. These domains are referred to as natural killer domains (NKDs) forming a large percentage of CTLDs in vertebrates. Here are summarized the data indicating that calcium, carbohydrates, peptides, and large proteins such as major histocompatibility complex (MHC) class I can all be ligands for NKDs. The wide range of ligands that can be recognized by NKDs includes some new, unexpected compounds such as signal peptide-derived fragments, heat shock proteins, or oxidized lipids. The biological importance of this extended range of recognition abilities is also discussed. A review with 134 references.

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Zhang, Huan, Xiaoyan Song, Lingling Wang, Pengfei Kong, Jialong Yang, Lin Liu, Limei Qiu, Ying Zhang, Lihua Qiu, and Linsheng Song. "AiCTL-6, a novel C-type lectin from bay scallop Argopecten irradians with a long C-type lectin-like domain." Fish & Shellfish Immunology 30, no. 1 (January 2011): 17–26. http://dx.doi.org/10.1016/j.fsi.2009.12.019.

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Flores-Ibarra, Andrea, Federico M. Ruiz, Sabine Vértesy, Sabine André, Hans-Joachim Gabius, and Antonio Romero. "Preliminary X-ray crystallographic analysis of an engineered variant of human chimera-type galectin-3 with a shortened N-terminal domain." Acta Crystallographica Section F Structural Biology Communications 71, no. 2 (January 28, 2015): 184–88. http://dx.doi.org/10.1107/s2053230x15000023.

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How lectins translate sugar-encoded information into cellular effects not only depends on glycan recognition. Other domains of the protein can contribute to the functional profile of a lectin. Human galectin-3 (Gal-3), an adhesion/growth-regulatory galectin, is composed of three different domains and is thus called a chimera-type protein. In addition to the carbohydrate-recognition domain, this lectin encompasses an N-terminal domain consisting of a peptide harbouring two phosphorylation sites and nine non-triple-helical collagen-like repeats. This region plays an as yet structurally undefined role in Gal-3 aggregation and ligand recognition. To date, crystallization of full-length Gal-3 has not been achieved. With the aim of providing structural insights into this modular organization, a Gal-3 variant was crystallized maintaining the terminal peptide and three of the nine collagen-like repeats. The crystals belonged to the orthorhombic space groupP212121, with unit-cell parametersa= 94.04,b= 97.96,c= 236.20 Å, and diffracted to a resolution of 3.3 Å.

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Horstkorte, R., M. Schachner, J. P. Magyar, T. Vorherr, and B. Schmitz. "The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth." Journal of Cell Biology 121, no. 6 (June 15, 1993): 1409–21. http://dx.doi.org/10.1083/jcb.121.6.1409.

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We have previously shown that the neural adhesion molecules L1 and NCAM interact with each other to form a complex which binds more avidly to L1 than L1 to L1 alone (Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner. 1990a. J. Cell Biol. 110:193-208). This cis-association between L1 and NCAM is carbohydrate-dependent (Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner. 1990b. J. Cell Biol. 110:209-218). In the present study, we report that L1 and NCAM bind to each other via oligomannosidic carbohydrates expressed by L1, but not by NCAM, as shown in several experiments: (a) complex formation between L1 and NCAM is inhibited by a mAb to oligomannosidic carbohydrates and by the oligosaccharides themselves; (b) NCAM binds to oligomannosidic carbohydrates; (c) within the L1/NCAM complex, the oligomannosidic carbohydrates are hidden from accessibility to a mAb against oligomannosidic carbohydrates; (d) the recombinant protein fragment of NCAM containing the immunoglobulin-like domains and not the fragment containing the fibronectin type III homologous repeats binds to oligomannosidic glycans. Furthermore, the fourth immunoglobulin-like domain of NCAM shows sequence homology with carbohydrate recognition domains of animal C-type lectins and, surprisingly, also with plant lectins. A peptide comprising part of the C-type lectin consensus sequence in the fourth immunoglobulin-like domain of NCAM interferes with the association between L1 and NCAM. The functional importance of oligomannosidic glycans at the cell surface was shown for neurite outgrowth in vitro. When neurons from early postnatal mouse cerebellum were maintained on laminin or poly-L-lysine, neurite outgrowth was inhibited by oligomannosidic glycans, by glycopeptides, glycoproteins, or neoglycolipids containing oligomannosidic glycans, but not by nonrelated oligosaccharides or oligosaccharide derivates. Neurite outgrowth was also inhibited by the peptide comprising part of the C-type lectin consensus sequence in the fourth immunoglobulin-like domain of NCAM. The combined results suggest that carbohydrate-mediated cis-associations between adhesion molecules at the cell surface modulate their functional properties.

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Takada, Ayato, Kouki Fujioka, Makoto Tsuiji, Akiko Morikawa, Nobuaki Higashi, Hideki Ebihara, Darwyn Kobasa, Heinz Feldmann, Tatsuro Irimura, and Yoshihiro Kawaoka. "Human Macrophage C-Type Lectin Specific for Galactose and N-Acetylgalactosamine Promotes Filovirus Entry." Journal of Virology 78, no. 6 (March 15, 2004): 2943–47. http://dx.doi.org/10.1128/jvi.78.6.2943-2947.2004.

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ABSTRACT Filoviruses cause lethal hemorrhagic disease in humans and nonhuman primates. An initial target of filovirus infection is the mononuclear phagocytic cell. Calcium-dependent (C-type) lectins such as dendritic cell- or liver/lymph node-specific ICAM-3 grabbing nonintegrin (DC-SIGN or L-SIGN, respectively), as well as the hepatic asialoglycoprotein receptor, bind to Ebola or Marburg virus glycoprotein (GP) and enhance the infectivity of these viruses in vitro. Here, we demonstrate that a recently identified human macrophage galactose- and N-acetylgalactosamine-specific C-type lectin (hMGL), whose ligand specificity differs from DC-SIGN and L-SIGN, also enhances the infectivity of filoviruses. This enhancement was substantially weaker for the Reston and Marburg viruses than for the highly pathogenic Zaire virus. We also show that the heavily glycosylated, mucin-like domain on the filovirus GP is required for efficient interaction with this lectin. Furthermore, hMGL, like DC-SIGN and L-SIGN, is present on cells known to be major targets of filoviruses (i.e., macrophages and dendritic cells), suggesting a role for these C-type lectins in viral replication in vivo. We propose that filoviruses use different C-type lectins to gain cellular entry, depending on the cell type, and promote efficient viral replication.

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Melin Fürst, Camilla, Matthias Mörgelin, Kasper Vadstrup, Dick Heinegård, Anders Aspberg, and Anna M. Blom. "The C-Type Lectin of the Aggrecan G3 Domain Activates Complement." PLoS ONE 8, no. 4 (April 15, 2013): e61407. http://dx.doi.org/10.1371/journal.pone.0061407.

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Fürst, Camilla Melin, Matthias Mörgelin, Dick Heinegård, Anders Aspberg, and Anna Blom. "The C-type lectin of the aggrecan G3 domain activates complement." Immunobiology 217, no. 11 (November 2012): 1208. http://dx.doi.org/10.1016/j.imbio.2012.08.228.

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Villoutreix, Bruno O., and Björn Dahlbäck. "Molecular Model for the C-type Lectin Domain of Human Thrombomodulin." Journal of Molecular Modeling 4, no. 10 (October 30, 1998): 310–22. http://dx.doi.org/10.1007/s008940050088.

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Kansas, GS, KB Saunders, K. Ley, A. Zakrzewicz, RM Gibson, BC Furie, B. Furie, and TF Tedder. "A role for the epidermal growth factor-like domain of P-selectin in ligand recognition and cell adhesion." Journal of Cell Biology 124, no. 4 (February 15, 1994): 609–18. http://dx.doi.org/10.1083/jcb.124.4.609.

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The selectin family of adhesion molecules mediates the initial interactions of leukocytes with endothelium. The extracellular region of each selectin contains an amino-terminal C-type lectin domain, followed by an EGF-like domain and multiple short consensus repeat units (SCR). Previous studies have indirectly suggested a role for each of the extracellular domains of the selectins in cell adhesion. In this study, a panel of chimeric selectins created by exchange of domains between L- and P-selectin was used to directly examine the role of the extracellular domains in cell adhesion. Exchange of only the lectin domains between L- and P-selectin conferred the adhesive and ligand recognition functions of the lectin domain of the parent molecule. However, chimeric selectins which contained both the lectin domain of L-selectin and the EGF-like domain of P-selectin exhibited dual ligand-binding specificity. These chimeric proteins supported adhesion both to myeloid cells and to high endothelial venules (HEV) of lymph nodes and mesenteric venules in vivo. Exchange of the SCR domains had no detectable effect on receptor function or specificity. Thus, the EGF-like domain of P-selectin may play a direct role in ligand recognition and leukocyte adhesion mediated by P-selectin, with the lectin plus EGF-like domains collectively forming a functional ligand recognition unit.

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CHEN, Mingyi, Shuh NARUMIYA, Tomoh MASAKI, and Tatsuya SAWAMURA. "Conserved C-terminal residues within the lectin-like domain of LOX-1 are essential for oxidized low-density-lipoprotein binding." Biochemical Journal 355, no. 2 (April 6, 2001): 289–96. http://dx.doi.org/10.1042/bj3550289.

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Lectin-like oxidized low-density-lipoprotein (oxLDL) receptor-1 (LOX-1) is a cell-surface endocytosis receptor for atherogenic oxLDL, which is highly expressed in endothelial cells. Recent studies suggest that it may play significant roles in atherogenesis. LOX-1 is a type-II membrane protein that structurally belongs to the C-type lectin family molecules. This study was designed to characterize the specific domain on LOX-1 that recognizes oxLDL. Truncation of the lectin domain of LOX-1 abrogated oxLDL-binding activity. Deletion of the utmost C-terminal ten amino acid residues (261-270) was enough to disrupt the oxLDL-binding activity. Substitutions of Lys-262 and/or Lys-263 with Ala additively attenuated the activity. Serial-deletion analysis showed that residues up to 265 are required for the expression of minimal binding activity, although deletion of the C-terminal three residues (268-270) still retained full binding activity. Consistently, these alterations in LOX-1 impaired the recognition by a functionally blocking monoclonal antibody for LOX-1. These data demonstrated the distinct role of the lectin domain as the functional domain recognizing LOX-1 ligand. The conserved C-terminal residues of lectin-like domain are essential for binding oxLDL. Particularly, the basic amino acid pair is important for the binding.

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Pees, Barbara, Wentao Yang, Anke Kloock, Carola Petersen, Lena Peters, Li Fan, Meike Friedrichsen, et al. "Effector and regulator: Diverse functions of C. elegans C-type lectin-like domain proteins." PLOS Pathogens 17, no. 4 (April 1, 2021): e1009454. http://dx.doi.org/10.1371/journal.ppat.1009454.

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In C. elegans, 283 clec genes encode a highly diverse family of C-type lectin-like domain (CTLD) proteins. Since vertebrate CTLD proteins have characterized functions in defense responses against pathogens and since expression of C. elegans clec genes is pathogen-dependent, it is generally assumed that clec genes function in C. elegans immune defenses. However, little is known about the relative contribution and exact function of CLEC proteins in C. elegans immunity. Here, we focused on the C. elegans clec gene clec-4, whose expression is highly upregulated by pathogen infection, and its paralogs clec-41 and clec-42. We found that, while mutation of clec-4 resulted in enhanced resistance to the Gram-positive pathogen Bacillus thuringiensis MYBt18247 (Bt247), inactivation of clec-41 and clec-42 by RNAi enhanced susceptibility to Bt247. Further analyses revealed that enhanced resistance of clec-4 mutants to Bt247 was due to an increase in feeding cessation on the pathogen and consequently a decrease in pathogen load. Moreover, clec-4 mutants exhibited feeding deficits also on non-pathogenic bacteria that were in part reflected in the clec-4 gene expression profile, which overlapped with gene sets affected by starvation or mutation in nutrient sensing pathways. However, loss of CLEC-4 function only mildly affected life-history traits such as fertility, indicating that clec-4 mutants are not subjected to dietary restriction. While CLEC-4 function appears to be associated with the regulation of feeding behavior, we show that CLEC-41 and CLEC-42 proteins likely function as bona fide immune effector proteins that have bacterial binding and antimicrobial capacities. Together, our results exemplify functional diversification within clec gene paralogs.

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Sager, Christoph P., Deniz Eriş, Martin Smieško, Rachel Hevey, and Beat Ernst. "What contributes to an effective mannose recognition domain?" Beilstein Journal of Organic Chemistry 13 (December 4, 2017): 2584–95. http://dx.doi.org/10.3762/bjoc.13.255.

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In general, carbohydrate–lectin interactions are characterized by high specificity but also low affinity. The main reason for the low affinities are desolvation costs, due to the numerous hydroxy groups present on the ligand, together with the typically polar surface of the binding sites. Nonetheless, nature has evolved strategies to overcome this hurdle, most prominently in relation to carbohydrate–lectin interactions of the innate immune system but also in bacterial adhesion, a process key for the bacterium’s survival. In an effort to better understand the particular characteristics, which contribute to a successful carbohydrate recognition domain, the mannose-binding sites of six C-type lectins and of three bacterial adhesins were analyzed. One important finding is that the high enthalpic penalties caused by desolvation can only be compensated for by the number and quality of hydrogen bonds formed by each of the polar hydroxy groups engaged in the binding process. In addition, since mammalian mannose-binding sites are in general flat and solvent exposed, the half-lives of carbohydrate–lectin complexes are rather short since water molecules can easily access and displace the ligand from the binding site. In contrast, the bacterial lectin FimH benefits from a deep mannose-binding site, leading to a substantial improvement in the off-rate. Together with both a catch-bond mechanism (i.e., improvement of affinity under shear stress) and multivalency, two methods commonly utilized by pathogens, the affinity of the carbohydrate–FimH interaction can be further improved. Including those just described, the various approaches explored by nature to optimize selectivity and affinity of carbohydrate–lectin interactions offer interesting therapeutic perspectives for the development of carbohydrate-based drugs.

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Juneja, Puneet, Ashit Rao, Helmut Cölfen, Kay Diederichs, and Wolfram Welte. "Crystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 fromStrongylocentrotus purpuratus." Acta Crystallographica Section F Structural Biology Communications 70, no. 2 (January 22, 2014): 260–62. http://dx.doi.org/10.1107/s2053230x14000880.

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Sea urchin spicules have a calcitic mesocrystalline architecture that is closely associated with a matrix of proteins and amorphous minerals. The mechanism underlying spicule formation involves complex processes encompassing spatio-temporally regulated organic–inorganic interactions. C-type lectin domains are present in several spicule matrix proteins inStrongylocentrotus purpuratus, implying their role in spiculogenesis. In this study, the C-type lectin domain of SM50 was overexpressed, purified and crystallized using a vapour-diffusion method. The crystal diffracted to a resolution of 2.85 Å and belonged to space groupP212121, with unit-cell parametersa= 100.6,b= 115.4,c= 130.6 Å, α = β = γ = 90°. Assuming 50% solvent content, six chains are expected to be present in the asymmetric unit.

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Brissett, Nigel C., and Stephen J. Perkins. "Molecular modelling analyses of the C-type lectin domain in human aggrecan." Biochemical Society Transactions 24, no. 1 (February 1, 1996): 99S. http://dx.doi.org/10.1042/bst024099s.

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Kastrup, J. S., B. B. Nielsen, H. Rasmussen, T. L. Holtet, J. H. Graversen, M. Etzerodt, H. C. Thøgerson, and I. K. Larsen. "Structure of the C-Type Lectin Carbohydrate Recognition Domain of Human Tetranectin." Acta Crystallographica Section D Biological Crystallography 54, no. 5 (September 1, 1998): 757–66. http://dx.doi.org/10.1107/s0907444997016806.

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Aspberg, A., C. Binkert, and E. Ruoslahti. "The versican C-type lectin domain recognizes the adhesion protein tenascin-R." Proceedings of the National Academy of Sciences 92, no. 23 (November 7, 1995): 10590–94. http://dx.doi.org/10.1073/pnas.92.23.10590.

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Ney, Andreas, Patrick Booms, Guido Epple, Matthias Mörgelin, Gao Guo, Gerhard Kettelgerdes, Reinhard Geßner, and Peter N. Robinson. "Calcium-dependent self-association of the C-type lectin domain of versican." International Journal of Biochemistry & Cell Biology 38, no. 1 (January 2006): 23–29. http://dx.doi.org/10.1016/j.biocel.2005.07.007.

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Rao, Xiang-Jun, Toufeeq Shahzad, Su Liu, Peng Wu, Yan-Ting He, Wei-Jia Sun, Xiang-Yun Fan, Yun-Fan Yang, Qiao Shi, and Xiao-Qiang Yu. "Identification of C-type lectin-domain proteins (CTLDPs) in silkworm Bombyx mori." Developmental & Comparative Immunology 53, no. 2 (December 2015): 328–38. http://dx.doi.org/10.1016/j.dci.2015.07.005.

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Timmer, Mattie S. M., Thomas J. Teunissen, Kristel Kodar, Amy J. Foster, Sho Yamasaki, and Bridget L. Stocker. "Cholesteryl glucosides signal through the carbohydrate recognition domain of the macrophage inducible C-type lectin (mincle)." Organic & Biomolecular Chemistry 19, no. 10 (2021): 2198–202. http://dx.doi.org/10.1039/d0ob02342f.

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EDA, Souji, Yasuhiko SUZUKI, Tetsuo KASE, Takao KAWAI, Katsuki OHTANI, Takashi SAKAMOTO, Takashi KURIMURA, and WAKAMIYA WAKAMIYA. "Recombinant bovine conglutinin, lacking the N-terminal and collagenous domains, has less conglutination activity but is able to inhibit haemagglutination by influenza A virus." Biochemical Journal 316, no. 1 (May 15, 1996): 43–48. http://dx.doi.org/10.1042/bj3160043.

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Conglutinin is a bovine serum protein which was first described as a vertebrate lectin. This protein belongs to the family of C-type lectins. These lectins are composed of four characteristic domains: (1) an N-terminal cysteine-rich domain, (2) a collagen-like domain, (3) a neck domain and (4) a carbohydrate recognition domain (CRD). Recently lectins have been shown to function as immunoglobulin-independent defence molecules due to a complement-mediated mechanism or opsonization. Our previous study showed that bovine conglutinin can inhibit haemagglutination by influenza A viruses and act by directly neutralizing them due to its lectin properties. In order to elucidate the biological role of the collagen-like domain, a recombinant partial conglutinin lacking this collagen-like domain was produced in an Escherichia coli system and its biological activities were examined. A 497 bp sequence, consisting of a short collagen region (two repeats of G-X-Y amino acid sequences), the neck domain, and the CRD of conglutinin cDNA, was amplified by the reverse-transcriptase PCR technique. The cDNA was transferred to a bacterial expression vector system (pRSET-A) and stable transfectants with a high level of conglutinin production were obtained. SDS/PAGE and Western blotting analyses showed a recombinant fusion protein of 27 kDa. Results of a cross-linking study and gel-filtration assay indicated that the recombinant conglutinin can form a trimeric structure and that it has sugar binding activity and specificity similar to that of native conglutinin. The recombinant conglutinin was also found to inhibit haemagglutination caused by influenza A virus as well as to possess less conglutination activity. These results suggest that in order for conglutinin to inhibit haemagglutination caused by the influenza virus, as well as to have sugar binding activity or to form trimers, it does not require the N-terminal and collagenous domains; however, they are essential for full conglutination activity.

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LOUKAS, A., A. DOEDENS, M. HINTZ, and R. M. MAIZELS. "Identification of a new C-type lectin, TES-70, secreted by infective larvae of Toxocara canis, which binds to host ligands." Parasitology 121, no. 5 (November 2000): 545–54. http://dx.doi.org/10.1017/s0031182099006721.

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Infective larvae of the dog roundworm Toxocara canis survive in the tissues of their hosts for extended periods in a state of developmental arrest, successfully evading immune destruction. This survival strategy is thought to be mediated by T. canis excretory/secretory (TES) products which downregulate or divert the immune response. We purified one of the major TES products, TES-70 and gained amino acid sequence from 4 tryptic peptides. These peptides were matched to a predicted protein from a cDNA that was isolated by expression screening a T. canis cDNA library with mouse anti-TES serum. The predicted protein (Tc-CTL-4) is similar to, but larger than, Tc-CTL-1, a 32-kDa C-type lectin secreted by T. canis larvae. Tc-CTL-4 has a signal peptide, 2 Cys-rich domains and a C-terminal calcium-dependent C-type lectin domain that shares sequence similarity with host immune cell receptors such as macrophage mannose receptor and CD23. The lectin domain was expressed in bacteria and antiserum to the purified recombinant protein was used to confirm that Tc-ctl-4 did encode the native TES-70 glycoprotein. TES-70 selectively bound to ligands on the surface of Madin–Darby Canine Kidney cells in vitro in a calcium-dependent manner, inhibitable by mammalian serum, indicating that a host glycan is the native ligand for this new parasite lectin.

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Nørregaard, Kirstine Sandal, Oliver Krigslund, Niels Behrendt, Lars H. Engelholm, and Henrik Jessen Jürgensen. "The collagen receptor uPARAP/Endo180 regulates collectins through unique structural elements in its FNII domain." Journal of Biological Chemistry 295, no. 27 (May 18, 2020): 9157–70. http://dx.doi.org/10.1074/jbc.ra120.013710.

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C-type lectins that contain collagen-like domains are known as collectins. These proteins are present both in the circulation and in extravascular compartments and are central players of the innate immune system, contributing to first-line defenses against viral, bacterial, and fungal pathogens. The collectins mannose-binding lectin (MBL) and surfactant protein D (SP-D) are regulated by tissue fibroblasts at extravascular sites via an endocytic mechanism governed by urokinase plasminogen activator receptor–associated protein (uPARAP or Endo180), which is also a collagen receptor. Here, we investigated the molecular mechanisms that drive the uPARAP-mediated cellular uptake of MBL and SP-D. We found that the uptake depends on residues within a protruding loop in the fibronectin type-II (FNII) domain of uPARAP that are also critical for collagen uptake. Importantly, however, we also identified FNII domain residues having an exclusive role in collectin uptake. We noted that these residues are absent in the related collagen receptor, the mannose receptor (MR or CD206), which consistently does not interact with collectins. We also show that the second C-type lectin-like domain (CTLD2) is critical for the uptake of SP-D, but not MBL, indicating an additional level of complexity in the interactions between collectins and uPARAP. Finally, we demonstrate that the same molecular mechanisms enable uPARAP to engage MBL immobilized on the surface of pathogens, thereby expanding the potential biological implications of this interaction. Our study reveals molecular details of the receptor-mediated cellular regulation of collectins and offers critical clues for future investigations into collectin biology and pathology.

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Ebner, Sharon, Nathan Sharon, and Nir Ben-Tal. "Evolutionary analysis reveals collective properties and specificity in the C-type lectin and lectin-like domain superfamily." Proteins: Structure, Function, and Bioinformatics 53, no. 1 (August 22, 2003): 44–55. http://dx.doi.org/10.1002/prot.10440.

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Conway, Edward M., Marlies Van de Wouwer, Saskia Pollefeyt, Kerstin Jurk, Hugo Van Aken, Astrid De Vriese, Jeffrey I. Weitz, et al. "The Lectin-like Domain of Thrombomodulin Confers Protection from Neutrophil-mediated Tissue Damage by Suppressing Adhesion Molecule Expression via Nuclear Factor κB and Mitogen-activated Protein Kinase Pathways." Journal of Experimental Medicine 196, no. 5 (September 2, 2002): 565–77. http://dx.doi.org/10.1084/jem.20020077.

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Thrombomodulin (TM) is a vascular endothelial cell (EC) receptor that is a cofactor for thrombin-mediated activation of the anticoagulant protein C. The extracellular NH2-terminal domain of TM has homology to C-type lectins that are involved in immune regulation. Using transgenic mice that lack this structure (TMLeD/LeD), we show that the lectin-like domain of TM interferes with polymorphonuclear leukocyte (PMN) adhesion to ECs by intercellular adhesion molecule 1–dependent and –independent pathways through the suppression of extracellular signal–regulated kinase (ERK)1/2 activation. TMLeD/LeD mice have reduced survival after endotoxin exposure, accumulate more PMNs in their lungs, and develop larger infarcts after myocardial ischemia/reperfusion. The recombinant lectin-like domain of TM suppresses PMN adhesion to ECs, diminishes cytokine-induced increase in nuclear factor κB and activation of ERK1/2, and rescues ECs from serum starvation, findings that may explain why plasma levels of soluble TM are inversely correlated with cardiovascular disease. These data suggest that TM has antiinflammatory properties in addition to its role in coagulation and fibrinolysis.

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Pees, Barbara, Anke Kloock, Rania Nakad, Camilo Barbosa, and Katja Dierking. "Enhanced behavioral immune defenses in a C. elegans C-type lectin-like domain gene mutant." Developmental & Comparative Immunology 74 (September 2017): 237–42. http://dx.doi.org/10.1016/j.dci.2017.04.021.

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Wienke, Dirk, John R. MacFadyen, and Clare M. Isacke. "Identification and Characterization of the Endocytic Transmembrane Glycoprotein Endo180 as a Novel Collagen Receptor." Molecular Biology of the Cell 14, no. 9 (September 2003): 3592–604. http://dx.doi.org/10.1091/mbc.e02-12-0814.

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Endo180, a member of the mannose receptor family, is constitutively recycled between clathrin-coated pits on the cell surface and intracellular endosomes. Its large extracellular domain contains an N-terminal cysteine-rich domain, a single fibronectin type II domain and eight C-type lectin-like domains. The second of these lectin-like domains has been shown to mediate Ca2+-dependent mannose binding. In addition, cross-linking studies have identified Endo180 as a urokinase plasminogen activator receptor–associated protein and this interaction can be blocked by collagen V. Here we demonstrate directly using in vitro assays, cell-based studies and tissue immunohistochemistry that Endo180 binds both to native and denatured collagens and provide evidence that this is mediated by the fibronectin type II domain. In cell culture systems, expression of Endo180 results in the rapid uptake of soluble collagens for delivery to lysosomal degradative compartments. Together with the observed restricted expression of Endo180 in both embryonic and adult tissue, we propose that Endo180 plays a physiological role in mediating collagen matrix remodelling during tissue development and homeostasis and that the observed receptor upregulation in pathological conditions may contribute to disease progression.

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MISTRY, Abinash Chandra, Shinji HONDA, and Shigehisa HIROSE. "Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica)." Biochemical Journal 360, no. 1 (November 8, 2001): 107–15. http://dx.doi.org/10.1042/bj3600107.

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Using a Japanese-eel (Anguilla japonica) gill cDNA subtraction library, two novel β-d-galactose-binding lectins were identified that belong to group VII of the animal C-type lectin family. The eel C-type lectins, termed eCL-1 and eCL-2, are simple lectins composed of 163 amino acid residues, including a 22-residue signal peptide for secretion and a single carbohydrate-recognition domain (CRD) of ∼ 130 residues typical of C-type lectins. The galactose specificity of the CRD was suggested by the presence of a QPD motif and confirmed by a competitive binding assay. Using Ruthenium Red staining, the lectins were shown to bind Ca2+ ions. SDS/PAGE showed that native eCL-1 and eCL-2have an SDS-resistant octameric structure (a tetramer of disulphide-linked dimers). Northern and Western blot analyses demonstrated high-level expression of eCL-1 and eCL-2 mRNAs and their protein products in gills from freshwater eels, which decreased markedly when the eels were transferred from freshwater to seawater. Immunohistochemistry showed that the eel lectins are localized in the exocrine mucous cells of the gill.

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Dulal, Hari P., Yoshiyuki Adachi, Naohito Ohno, and Yoshiki Yamaguchi. "β-Glucan-induced cooperative oligomerization of Dectin-1 C-type lectin-like domain." Glycobiology 28, no. 8 (May 11, 2018): 612–23. http://dx.doi.org/10.1093/glycob/cwy039.

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PANCER, ZEEV, BÄRBEL DIEHL-SEIFERT, BARUCH RINKEVICH, and WERNER E. G. MÜLLER. "A Novel Tunicate (Botryllus schlosseri) Putative C-Type Lectin Features an Immunoglobulin Domain." DNA and Cell Biology 16, no. 6 (June 1997): 801–6. http://dx.doi.org/10.1089/dna.1997.16.801.

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Zelensky, Alex N., and Jill E. Gready. "Comparative analysis of structural properties of the C-type-lectin-like domain (CTLD)." Proteins: Structure, Function, and Bioinformatics 52, no. 3 (July 7, 2003): 466–77. http://dx.doi.org/10.1002/prot.10626.

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Khan, Kabir A., Jack L. McMurray, Fiyaz Mohammed, and Roy Bicknell. "C‐type lectin domain group 14 proteins in vascular biology, cancer and inflammation." FEBS Journal 286, no. 17 (July 29, 2019): 3299–332. http://dx.doi.org/10.1111/febs.14985.

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Kolatkar, Anand R., Anthony K. Leung, Rainer Isecke, Reinhard Brossmer, Kurt Drickamer, and William I. Weis. "Mechanism ofN-Acetylgalactosamine Binding to a C-type Animal Lectin Carbohydrate-recognition Domain." Journal of Biological Chemistry 273, no. 31 (July 31, 1998): 19502–8. http://dx.doi.org/10.1074/jbc.273.31.19502.

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Pålsson-McDermott, E. M., and L. A. J. O'Neill. "Building an immune system from nine domains." Biochemical Society Transactions 35, no. 6 (November 23, 2007): 1437–44. http://dx.doi.org/10.1042/bst0351437.

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Four families of PRRs (pattern-recognition receptors) have been identified as important components of innate immunity, participating in the sensory system for host defence against the invasion of infectious agents. The TLRs (Toll-like receptors) recognize a variety of conserved microbial PAMPs (pathogen-associated molecular patterns) derived from bacteria, viruses, protozoa and fungi. They work in synergy with the cytosolic NLRs [NOD (nucleotide binding and oligomerization domain)-like receptors] (which sense bacteria), RLRs [RIG-I (retinoic acid-inducible gene 1)-like receptors] (which sense viruses) and CLRs (C-type lectin receptors) (which sense fungi). All of these receptor families signal an increase in the expression of a range of immune and inflammatory genes. The structural architecture of these receptors is conserved, involving seven distinct domains: the LRR (leucine-rich repeat) domain, the TIR [Toll/IL (interleukin)-1 receptor] domain, the NBS (nucleotide-binding site), the CARD (caspase recruitment domain), the PYD (pyrin domain), the helicase domain and the CTLD (C-type lectin domain). Two other domains, the Ig domain and the ITAM (immunoreceptor tyrosine-based activation motif) domain also participate and are also found in antibodies and TCRs (T-cell receptors), key proteins in adaptive immunity. This total of nine domains can therefore be used to construct immune systems which are common to many, if not all, species, allowing us to speculate on the minimum requirement for a complex immune system in structural terms. These insights are important for our overall understanding of the regulation of immunity in health and disease.

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Sheikh, H., H. Yarwood, A. Ashworth, and C. M. Isacke. "Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor." Journal of Cell Science 113, no. 6 (March 15, 2000): 1021–32. http://dx.doi.org/10.1242/jcs.113.6.1021.

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Endo180 was previously characterized as a novel, cell type specific, recycling transmembrane glycoprotein. This manuscript describes the isolation of a full length human Endo180 cDNA clone which was shown to encode a fourth member of a family of proteins comprising the macrophage mannose receptor, the phospholipase A(2) receptor and the DEC-205/MR6 receptor. This receptor family is unusual in that they contain 8–10 C-type lectin carbohydrate recognition domains in a single polypeptide backbone, however, only the macrophage mannose receptor had been shown to function as a lectin. Sequence analysis of Endo180 reveals that the second carbohydrate recognition domain has retained key conserved amino acids found in other functional C-type lectins. Furthermore, it is demonstrated that this protein displays Ca(2+)-dependent binding to N-acetylglucosamine but not mannose affinity columns. In order to characterize the physiological function of Endo180, a series of biochemical and morphological studies were undertaken. Endo180 is found to be predominantly expressed in vivo and in vitro on fibroblasts, endothelial cells and macrophages, and the distribution and post-translational processing in these cells is consistent with Endo180 functioning to internalize glycosylated ligands from the extracellular milieu for release in an endosomal compartment.

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May, Carolyn, Suena Ji, Zulfeqhar A. Syed, Leslie Revoredo, Earnest James Paul Daniel, Thomas A. Gerken, Lawrence A. Tabak, Nadine L. Samara, and Kelly G. Ten Hagen. "Differential splicing of the lectin domain of an O-glycosyltransferase modulates both peptide and glycopeptide preferences." Journal of Biological Chemistry 295, no. 35 (July 15, 2020): 12525–36. http://dx.doi.org/10.1074/jbc.ra120.014700.

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Mucin-type O-glycosylation is an essential post-translational modification required for protein secretion, extracellular matrix formation, and organ growth. O-Glycosylation is initiated by a large family of enzymes (GALNTs in mammals and PGANTs in Drosophila) that catalyze the addition of GalNAc onto the hydroxyl groups of serines or threonines in protein substrates. These enzymes contain two functional domains: a catalytic domain and a C-terminal ricin-like lectin domain comprised of three potential GalNAc recognition repeats termed α, β, and γ. The catalytic domain is responsible for binding donor and acceptor substrates and catalyzing transfer of GalNAc, whereas the lectin domain recognizes more distant extant GalNAc on previously glycosylated substrates. We previously demonstrated a novel role for the α repeat of lectin domain in influencing charged peptide preferences. Here, we further interrogate how the differentially spliced α repeat of the PGANT9A and PGANT9B O-glycosyltransferases confers distinct preferences for a variety of endogenous substrates. Through biochemical analyses and in silico modeling using preferred substrates, we find that a combination of charged residues within the α repeat and charged residues in the flexible gating loop of the catalytic domain distinctively influence the peptide substrate preferences of each splice variant. Moreover, PGANT9A and PGANT9B also display unique glycopeptide preferences. These data illustrate how changes within the noncatalytic lectin domain can alter the recognition of both peptide and glycopeptide substrates. Overall, our results elucidate a novel mechanism for modulating substrate preferences of O-glycosyltransferases via alternative splicing within specific subregions of functional domains.

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Decout, Alexiane, Sandro Silva-Gomes, Daniel Drocourt, Sophie Barbe, Isabelle André, Francisco J. Cueto, Thierry Lioux, et al. "Rational design of adjuvants targeting the C-type lectin Mincle." Proceedings of the National Academy of Sciences 114, no. 10 (February 21, 2017): 2675–80. http://dx.doi.org/10.1073/pnas.1612421114.

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The advances in subunit vaccines development have intensified the search for potent adjuvants, particularly adjuvants inducing cell-mediated immune responses. Identification of the C-type lectin Mincle as one of the receptors underlying the remarkable immunogenicity of the mycobacterial cell wall, via recognition of trehalose-6,6′-dimycolate (TDM), has opened avenues for the rational design of such molecules. Using a combination of chemical synthesis, biological evaluation, molecular dynamics simulations, and protein mutagenesis, we gained insight into the molecular bases of glycolipid recognition by Mincle. Unexpectedly, the fine structure of the fatty acids was found to play a key role in the binding of a glycolipid to the carbohydrate recognition domain of the lectin. Glucose and mannose esterified atO-6 by a synthetic α-ramified 32-carbon fatty acid showed agonist activity similar to that of TDM, despite their much simpler structure. Moreover, they were seen to stimulate proinflammatory cytokine production in primary human and murine cells in a Mincle-dependent fashion. Finally, they were found to induce strong Th1 and Th17 immune responses in vivo in immunization experiments in mice and conferred protection in a murine model ofMycobacterium tuberculosisinfection. Here we describe the rational development of new molecules with powerful adjuvant properties.

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Larvie, Mykol, Timothy Shoup, Wei-Chuan Chang, Lorencia Chigweshe, Kevan Hartshorn, Mitchell R. White, Gregory L. Stahl, David R. Elmaleh, and Kazue Takahashi. "Mannose-Binding Lectin Binds to Amyloid Protein and Modulates Inflammation." Journal of Biomedicine and Biotechnology 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/929803.

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Mannose-binding lectin (MBL), a soluble factor of the innate immune system, is a pattern recognition molecule with a number of known ligands, including viruses, bacteria, and molecules from abnormal self tissues. In addition to its role in immunity, MBL also functions in the maintenance of tissue homeostasis. We present evidence here that MBL binds to amyloidβpeptides. MBL binding to other known carbohydrate ligands is calcium-dependent and has been attributed to the carbohydrate-recognition domain, a common feature of other C-type lectins. In contrast, we find that the features of MBL binding to Aβare more similar to the reported binding characteristics of the cysteine-rich domain of the unrelated mannose receptor and therefore may involve the MBL cysteine-rich domain. Differences in MBL ligand binding may contribute to modulation of inflammatory response and may correlate with the function of MBL in processes such as coagulation and tissue homeostasis.

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BRISSETT, C. Nigel, and J. Stephen PERKINS. "Conserved basic residues in the C-type lectin and short complement repeat domains of the G3 region of proteoglycans." Biochemical Journal 329, no. 2 (January 15, 1998): 415–24. http://dx.doi.org/10.1042/bj3290415.

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Aggrecan is the major proteoglycan of the extracellular matrix in cartilage. It contains two N-terminal globular regions, G1 and G2, and one C-terminal globular region, G3. G3 is implicated in the intracellular processing of aggrecan and contains a C-type lectin carbohydrate recognition domain (CRD), frequent occurrences of a C-terminal short complement repeat (SCR) domain, and occasionally an N-terminal epidermal growth factor domain. The CRD and SCR domains in 13 G3 sequences were each subjected to structural analysis. Alignment of 131 sequences from all seven groups in the CRD superfamily defined a consensus length of 136 residues, in which 32% of residues were conserved. Although the G3 CRD sequences agreed with this consensus, they also contained five fully conserved basic residues that are atypical of the CRD superfamily. Homology modelling showed that four of these residues are located on a surface region on the CRD that is separate from the Ca2+-binding residues involved in carbohydrate interactions. One conserved basic residue is identical in position with that of a conserved basic residue that mediates hyaluronate binding in the structurally related proteoglycan tandem repeat (PTR) domain in G1 and in link protein. The alignment of 13 G3 SCR sequences with 101 sequences in the SCR superfamily showed good agreement with conserved residues in the SCR superfamily. There are also five conserved basic residues in the G3 SCR that are atypical of the SCR superfamily, and homology modelling showed that all five were located on one surface of the SCR. It is concluded that both the CRD and SCR domains in G3 possess basic residues that are atypical of their superfamilies and might be related to function, and that the G3 CRD domain shows an evolutionary relationship to the PTR domain in G1.

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LEDUC, Mireille, and Cassian BON. "Cloning of subunits of convulxin, a collagen-like platelet-aggregating protein from Crotalus durissus terrificus venom." Biochemical Journal 333, no. 2 (July 15, 1998): 389–93. http://dx.doi.org/10.1042/bj3330389.

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Convulxin (CVX) is a potent platelet-aggregating glycoprotein from the venom of the snake Crotalus durissus terrificus. It consists of two subunits, α and β, joined by disulphide bridges in a hexameric structure. A cDNA library from venom gland was constructed in the vector pT3T7. The cloned cDNAs encoding the two chains of CVX were sequenced. Both are preceded by an identical 23-amino acid peptide signal sequence and encode sequences of 135 amino acids for the α chain and 125 amino acids for the β chain. These polypeptides include a carbohydrate-recognition domain (CRD) in which some of the specific amino acids required for binding Ca2+ and galactose or mannose are absent. The presence of such a domain means that CVX can be included in the family of C-type lectins along with other snake venom proteins, although it is not a true lectin. Assuming that the localization of intracatenary disulphide bridges of each CVX chain is similar to that of the CRD and that an intercatenary bridge between the α and β chains is similar to that of the C-type lectin botrocetin, we postulate the existence of an additional intercatenary bridge, which explains the tridimeric structure (αβ)3 of CVX.

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Vohra, Ravinder S., Jane E. Murphy, John H. Walker, Shervanthi Homer-Vanniasinkam, and Sreenivasan Ponnambalam. "Functional refolding of a recombinant C-type lectin-like domain containing intramolecular disulfide bonds." Protein Expression and Purification 52, no. 2 (April 2007): 415–21. http://dx.doi.org/10.1016/j.pep.2006.11.012.

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Pees, Barbara, Wentao Yang, Alejandra Zárate-Potes, Hinrich Schulenburg, and Katja Dierking. "High Innate Immune Specificity through Diversified C-Type Lectin-Like Domain Proteins in Invertebrates." Journal of Innate Immunity 8, no. 2 (November 19, 2015): 129–42. http://dx.doi.org/10.1159/000441475.

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A key question in current immunity research is how the innate immune system can generate high levels of specificity. Evidence is accumulating that invertebrates, which exclusively rely on innate defense mechanisms, can differentiate between pathogens on the species and even strain level. In this review, we identify and discuss the particular potential of C-type lectin-like domain (CTLD) proteins to generate high immune specificity. Whilst several CTLD proteins are known to act as pattern recognition receptors in the vertebrate innate immune system, the exact role of CTLD proteins in invertebrate immunity is much less understood. We show that CTLD genes are highly abundant in most metazoan genomes and summarize the current state of knowledge on CTLD protein function in insect, crustacean and nematode immune systems. We then demonstrate extreme CTLD gene diversification in the genomes of Caenorhabditis nematodes and provide an update of data from CTLD gene function studies in C. elegans, which indicate that the diversity of CTLD genes could contribute to immune specificity. In spite of recent achievements, the exact functions of the diversified invertebrate CTLD genes are still largely unknown. Our review therefore specifically discusses promising research approaches to rectify this knowledge gap.

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Lu, Yuzhen, Fanghua Su, Kesen Zhu, Mengyao Zhu, Qilin Li, Qihao Hu, Jie Zhang, Ruonan Zhang, and Xiao-Qiang Yu. "Comparative genomic analysis of C-type lectin-domain genes in seven holometabolous insect species." Insect Biochemistry and Molecular Biology 126 (November 2020): 103451. http://dx.doi.org/10.1016/j.ibmb.2020.103451.

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Rust, Kevin, Leonard Grosso, Vivian Zhang, Donald Chang, Anders Persson, William Longmore, Guang-Zuan Cai, and Edmond Crouch. "Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain." Archives of Biochemistry and Biophysics 290, no. 1 (October 1991): 116–26. http://dx.doi.org/10.1016/0003-9861(91)90597-c.

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Jacobsen, Kristian M., Ulrik B. Keiding, Lise L. Clement, Eva S. Schaffert, Neela D. S. Rambaruth, Mogens Johannsen, Kurt Drickamer, and Thomas B. Poulsen. "The natural product brartemicin is a high affinity ligand for the carbohydrate-recognition domain of the macrophage receptor mincle." MedChemComm 6, no. 4 (2015): 647–52. http://dx.doi.org/10.1039/c4md00512k.

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We demonstrate that the natural product brartemicin, a newly discovered inhibitor of cancer cell invasion, is a high-affinity ligand of the carbohydrate-recognition domain (CRD) of the C-type lectin mincle.

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Kilpatrick, David. "Therapeutic applications of mannan-binding lectin." Biochemist 25, no. 4 (August 1, 2003): 33–34. http://dx.doi.org/10.1042/bio02504033.

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Mannan-binding lectin (MBL) is perhaps the best known of the collectins, a subfamily of C-type lectins possessing an additional collagen-like domain. MBL is thought to be an important component of innate immunity. Since the discovery, around 15 years ago, that MBL was identical to a factor responsible for the opsonization of baker's yeast in vitro, a large number of disease-association studies have been conducted. Most of these investigations support the view that MBL can influence susceptibility to, or affect the course of, many diseases. These include bacterial infections, rheumatoid arthritis, cystic fibrosis and recurrent miscarriage. This meeting was arranged to bring together scientists and clinicians to review the clinical significance of MBL, and to consider the most appropriate target disorders for MBL-replacement therapy.

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Adelman, Zach, and Kevin Myles. "The C-Type Lectin Domain Gene Family in Aedes aegypti and Their Role in Arbovirus Infection." Viruses 10, no. 7 (July 12, 2018): 367. http://dx.doi.org/10.3390/v10070367.

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Several medically important flaviviruses that are transmitted by mosquitoes have been shown to bind to the C-type lectin fold that is present in either vertebrate or invertebrate proteins. While in some cases this interaction is part of a neutralizing anti-viral immune response, many reports have implicated this as critical for successful virus entry. Despite the establishment of mosquito C-type lectin domain containing proteins (CTLDcps) as known host factors in assisting the infectious process for flaviviruses, little is known about the structural characteristics of these proteins and their relationships to each other. In this report, we describe the manual annotation and structural characterization of 52 Aedes aegypti CTLDcps. Using existing RNAseq data, we establish that these genes can be subdivided into two classes: those highly conserved with expression primarily in development (embryo/early larvae) and those with no clear orthologs with expression primarily in late larvae/pupae or adults. The latter group contained all CTLDcps that are regulated by the Toll/Imd immune pathways, all known microbiome-regulating CTLDcps, and almost all CTLDcps that are implicated as flavivirus host factors in A. aegypti. Finally, we attempt to synthesize results from multiple conflicting gene expression profiling experiments in terms of how flavivirus infection changes steady-state levels of mRNA encoding CTLDcps.

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

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