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Journal articles on the topic 'C-lectins'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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1

Kothari, Sajani, Rebecca Heineman, and Rene Harrison. "Optimizing Lectin Staining Methodology to Assess Glycocalyx Composition of Legionella-Infected Cells." Undergraduate Research in Natural and Clinical Science and Technology (URNCST) Journal 7, no. 7 (2023): 1–10. http://dx.doi.org/10.26685/urncst.490.

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Introduction: Legionella is a gram-negative bacterium that replicates intracellularly within macrophages. Legionella utilizes effector proteins to hijack ER-Golgi vesicle trafficking to sustain proliferation in its intracellular niche. Legionella has a considerable influence on O-glycosylation but not N-glycosylation events in the Golgi of infected cells. This research aims to optimize the use of fluorescent lectins, which are proteins that bind carbohydrates, to effectively label host-cell glycocalyx during Legionella infection. Methods: Epifluorescence imaging or flow cytometry were used to

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2

Matsuno, Keita, Noriko Kishida, Katsuaki Usami, et al. "Different Potential of C-Type Lectin-Mediated Entry between Marburg Virus Strains." Journal of Virology 84, no. 10 (2010): 5140–47. http://dx.doi.org/10.1128/jvi.02021-09.

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ABSTRACT The glycoproteins (GPs) of filoviruses are responsible for virus entry into cells. It is known that GP interacts with cellular C-type lectins for virus attachment to cells. Since primary target cells of filoviruses express C-type lectins, C-type lectin-mediated entry is thought to be a possible determinant of virus tropism and pathogenesis. We compared the efficiency of C-type lectin-mediated entry between Marburg virus strains Angola and Musoke by using a vesicular stomatitis virus (VSV) pseudotype system. VSV pseudotyped with Angola GP (VSV-Angola) infected K562 cells expressing the

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3

Melgarejo, Luz Marina, Nohora Vega, and Gerardo Pérez. "Isolation and characterization of novel lectins from Canavalia ensiformis DC and Dioclea grandiflora Mart. ex Benth. seeds." Brazilian Journal of Plant Physiology 17, no. 3 (2005): 315–24. http://dx.doi.org/10.1590/s1677-04202005000300006.

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Two lectins were isolated from Canavalia ensiformis and Dioclea grandiflora seeds. Gel filtration produced a fraction corresponding to Con A or D. grandiflora lectin while erythroagglutination assays revealed a distinct fraction presenting a lectin that agglutinates human red blood cells (RBCs) but not rabbit RBCs. Hydrophobic interaction chromatography showed that the latter fraction yielded a protein that readily agglutinates human erythrocytes; the lectin was also purified by affinity chromatography on Lac-Sepharose showing similar properties to that of the Phenyl-Sepharose-purified lectin.

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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 (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, t

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5

Ahmmed, Mirja Kaizer, Shuva Bhowmik, Stephen G. Giteru, et al. "An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications." Marine Drugs 20, no. 7 (2022): 430. http://dx.doi.org/10.3390/md20070430.

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Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycoproteins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their origins, such as plant lectins, animal lectins, and fish lectins. Marine organisms including fish, crustaceans, and mollusks produce a myriad of lectins, including rhamnose binding lectins (RBL), fucose-binding lectins (FTL), mannose-binding lectin, galectins, galactose binding lectins, and C-type lectins. The widely used method of extracting lectins

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6

Drickamer, Kurt, and Andrew J. Fadden. "Genomic analysis of C-type lectins." Biochemical Society Symposia 69 (October 1, 2002): 59–72. http://dx.doi.org/10.1042/bss0690059.

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Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are p

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7

Ahmed, E. M. "Lectin Quantitation in Peanut and Soybean Seeds1." Peanut Science 13, no. 1 (1986): 4–7. http://dx.doi.org/10.3146/i0095-3679-13-1-2.

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Abstract A method was developed to determine amounts of lectin in peanut and soybean seeds. Both types of seeds contained active lectins in amounts ranging from 144.7 to 112.2 μg/g defatted meal for peanut and soybean seed, respectively. Lectins were inactivated by heat; moist heat was more effective than dry heat. Roasted peanuts seeds (177 C for 30 min) and boiled peanuts (5% saline solution for 1 hr) were devoid of active lectin.

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8

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 (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 proteol

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9

Chen, Pengyu, Kristof De Schutter, Els J. M. Van Damme, and Guy Smagghe. "Can Plant Lectins Help to Elucidate Insect Lectin-Mediated Immune Response?" Insects 12, no. 6 (2021): 497. http://dx.doi.org/10.3390/insects12060497.

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Lectins are carbohydrate-binding proteins that recognize and selectively bind to specific sugar structures. This group of proteins is widespread in plants, animals, and microorganisms, and exerts a broad range of functions. Many plant lectins were identified as exogenous stimuli of vertebrate immunity. Despite being the largest and most diverse taxon on earth, the study of lectins and their functions in insects is lagging behind. In insects, research on lectins and their biological importance has mainly focused on the C-type lectin (CTL) family, limiting our global understanding of the functio

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10

Lefebre, Jonathan, Torben Falk, Yunzhan Ning, and Christoph Rademacher. "Secondary sites of the C-type lectin-like fold." Chemistry: A European Journal 30, no. 30 (2024): e202400660. https://doi.org/10.5281/zenodo.10908543.

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C-type lectins are a large superfamily of proteins involved in a multitude of biological processes. In particular, their involvement in immunity and homeostasis has rendered them attractive targets for diverse therapeutic interventions. They share a characteristic C-type lectin-like domain whose adaptability enables them to bind a broad spectrum of ligands beyond the originally defined canonical Ca<sup>2+</sup>-dependent carbohydrate binding. Together with variable domain architecture and high-level conformational plasticity, this enables C-type lectins to meet diverse functional demands. Seco

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11

Ogawa, Tomohisa, Mizuki Watanabe, Takako Naganuma, and Koji Muramoto. "Diversified Carbohydrate-Binding Lectins from Marine Resources." Journal of Amino Acids 2011 (November 15, 2011): 1–20. http://dx.doi.org/10.4061/2011/838914.

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Marine bioresources produce a great variety of specific and potent bioactive molecules including natural organic compounds such as fatty acids, polysaccharides, polyether, peptides, proteins, and enzymes. Lectins are also one of the promising candidates for useful therapeutic agents because they can recognize the specific carbohydrate structures such as proteoglycans, glycoproteins, and glycolipids, resulting in the regulation of various cells via glycoconjugates and their physiological and pathological phenomenon through the host-pathogen interactions and cell-cell communications. Here, we re

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Taatjes, D. J., L. A. Barcomb, K. O. Leslie, and R. B. Low. "Lectin binding patterns to terminal sugars of rat lung alveolar epithelial cells." Journal of Histochemistry & Cytochemistry 38, no. 2 (1990): 233–44. http://dx.doi.org/10.1177/38.2.1688898.

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We used post-embedding cytochemical techniques to investigate the lectin binding profiles of rat lung alveolar epithelial cells. Sections from rat lung embedded in the hydrophilic resin Lowicryl K4M were incubated either directly with a lectin-gold complex or with an unlabeled lectin followed by a specific glycoprotein-gold complex. The binding patterns of the five lectins used could be divided into three categories according to their reactivity with alveolar epithelial cells: (a) the Limax flavus lectin and Ricinus communis I lectin bound to both type I and type II cell plasma membranes; (b)

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13

Takada, Ayato, Kouki Fujioka, Makoto Tsuiji, et al. "Human Macrophage C-Type Lectin Specific for Galactose and N-Acetylgalactosamine Promotes Filovirus Entry." Journal of Virology 78, no. 6 (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 (hMG

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14

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 (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

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15

Sawyer, J. T., and R. A. Akeson. "Differential redistribution of lectin receptor classes on clonal rat myotubes and myoblasts." Journal of Cell Science 83, no. 1 (1986): 181–96. http://dx.doi.org/10.1242/jcs.83.1.181.

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To evaluate the relative mobilities of cell surface glycoconjugates during myogenesis we have studied the redistribution of fluorescein-conjugated plant lectins on L6 rat myogenic cells. Previous experiments had demonstrated that the receptors for the lectins soybean agglutinin (SBA), wheat germ agglutinin, concanavalin A and Lens culinaris agglutinin all were relatively uniformly distributed on both myoblasts and myotubes, and that SBA receptors were capable of rapid redistribution on myotubes but not myoblasts at 4 degrees C (Sawyer & Akeson, 1983). Here we show that when SBA-labelled my

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16

Pinto, Nilson Vieira, Cláudia Ferreira Santos, Benildo Sousa Cavada, et al. "Homologous Canavalia Lectins Elicit Different Patterns of Antinociceptive Responses." Natural Product Communications 8, no. 11 (2013): 1934578X1300801. http://dx.doi.org/10.1177/1934578x1300801130.

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Canavalia gladiata (CGL), C. maritima (ConM) and C. brasiliensis (ConBr) lectins were evaluated in nociception models. ConBr inhibited first (32%) and second (100%) phases of the formalin test; CGL inhibited only the first (74%) and ConM only the second (59%) phase. Hypernociception evaluated in the Von Frey test was inhibited by ConM (55%), CGL (41%) and ConBr (38%). Acetic acid-induced abdominal writhing was reduced by ConBr (66%), CGL (52%) and ConM (60%). ConBr and CGL effects were reversed by the lectin association with its ligand sugar. The antinociceptive activity of the structural homo

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17

Jasim, Rasha Hasan, Dr Hathama Razooki Hasan, and Dr Majed Khadum Husain. "What Is The New and Sensitive Tumor Marker for Detection of Different Kidney Tumors? Modern Study to Isolation, Purification and Characterization of N-Acetyl Galactosamine Binding Lectin From Sera Of Patients With Kidney Cancer." JOURNAL OF ADVANCES IN CHEMISTRY 12, no. 7 (2013): 441–50. http://dx.doi.org/10.24297/jac.v12i7.6702.

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The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated. The age of patients and healthy individuals were 10-90 years. The measurement of total serum proteins revealed significant (p < 0.001) decrease in patients of malignant tumors when compared with those of b

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Jasim, Rasha Hasan, Dr Hathama Razooki Hasan, and Dr Majed Khadum Husain. "What Is The New and Sensitive Tumor Marker for Detection of Different Kidney Tumors? Modern Study to Isolation, Purification and Characterization of N-Acetyl Galactosamine Binding Lectin From Sera Of Patients With Kidney Cancer." JOURNAL OF ADVANCES IN CHEMISTRY 4, no. 2 (2008): 441–50. http://dx.doi.org/10.24297/jac.v4i2.2705.

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The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated. The age of patients and healthy individuals were 10-90 years. The measurement of total serum proteins revealed significant (p < 0.001) decrease in patients of malignant tumors when compared with those of b

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19

Końska, Grażyna. "A survey of domestic species of Basidiomycetes fungi for the presence of lectins inn their carpophores." Acta Societatis Botanicorum Poloniae 57, no. 2 (2014): 247–60. http://dx.doi.org/10.5586/asbp.1988.025.

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Preliminary investigations were conducted to determine the presence of active lectins in carpophores of fungi from the class <em>Basidiomycetes</em>, collected from natural localities in southern and south-eastern Poland. The degree of agglutination activity (expressed as the titre of agglutination) of aqueous extracts was determined at room temperature (18-20°C) and at +4°C in respect to human and animal erythrocytes suspended in physiological saline, part of which were additionally treated with proteolytic enzymes. From among the 104 tested species, extracts from 41 of them showe

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20

Weisz, O. A., and R. L. Schnaar. "Hepatocyte adhesion to carbohydrate-derivatized surfaces. II. Regulation of cytoskeletal organization and cell morphology." Journal of Cell Biology 115, no. 2 (1991): 495–504. http://dx.doi.org/10.1083/jcb.115.2.495.

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Rat hepatic lectins mediate adhesion of isolated rat hepatocytes to synthetic surfaces derivatized with galactosides. Initial weak adhesion is followed by rapid adhesion strengthening. After hepatocytes contact galactose-derivatized gels, the hepatic lectins move rapidly into an inaccessible patch at the adhesive surface (Weisz, O. A., and R. L. Schnaar. 1991. J. Cell Biol. 115:485-493). Hepatic lectin patching, which occurs both at 37 degrees C and 4 degrees C, is not responsible for adhesion strengthening, which does not occur at 4 degrees C. Of various cytoskeletal and metabolic perturbants

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Hjelle, J. Thomas, Barbara T. Golinska, Diane C. Waters, et al. "Lectin Staining of Peritoneal Mesothelial Cells in Vitro." Peritoneal Dialysis International: Journal of the International Society for Peritoneal Dialysis 11, no. 4 (1991): 307–16. http://dx.doi.org/10.1177/089686089101100403.

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A survey of lectin-binding specificities present on rodent and human mesothelial cells propagated and maintained in tissue culture was made using fluorescein isothiocynate conjugated (FITC) lectins. Rodent and human cells exhibited cell-associated fluorescence following exposure to the FITC-Iectins from C. ensiformis, T. vulgaris, A. hypogaea, E. cristagalli and B. simplicifolia, but not with lectins from G. max and D. biflorus. Rodent cells were also positive for FITC-M. pomifera lectin binding. Human, but not rodent, cells were positive for FITC T. purpureas lectin binding. Exposure of rabbi

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22

Matsumoto, Jun, Chiaki Nakamoto, Shigeki Fujiwara, Toshitsugu Yubisui, and Kazuo Kawamura. "A novel C-type lectin regulating cell growth, cell adhesion and cell differentiation of the multipotent epithelium in budding tunicates." Development 128, no. 17 (2001): 3339–47. http://dx.doi.org/10.1242/dev.128.17.3339.

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We have isolated two Ca2+-dependent, galactose-binding polypeptides from the budding tunicate, Polyandrocarpa misakiensis. Based on their partial amino acid sequences, full-length cDNAs were cloned. One of them was identical with a tunicate C-type lectin (TC14-2) reported previously. The other was a novel C-type lectin, referred to as TC14-3. In living animals, they appeared to be coupled. This complex of lectins, when applied in vitro to tunicate multipotent cells of epithelial origin, blocked cell proliferation and induced cell aggregation. The aggregates expressed a homolog of the integrin

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23

Pace, Angelica, Fabio Scirocchi, Chiara Napoletano, et al. "Glycan-Lectin Interactions as Novel Immunosuppression Drivers in Glioblastoma." International Journal of Molecular Sciences 23, no. 11 (2022): 6312. http://dx.doi.org/10.3390/ijms23116312.

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Despite diagnostic and therapeutic improvements, glioblastoma (GB) remains one of the most threatening brain tumor in adults, underlining the urgent need of new therapeutic targets. Lectins are glycan-binding proteins that regulate several biological processes through the recognition of specific sugar motifs. Lectins and their ligands are found on immune cells, endothelial cells and, also, tumor cells, pointing out a strong correlation among immunity, tumor microenvironment and vascularization. In GB, altered glycans and lectins contribute to tumor progression and immune evasion, shaping the t

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Wiggins, Joshua, Shazeed-Ul Karim, Baolong Liu, et al. "Identification of a Novel Antiviral Lectin against SARS-CoV-2 Omicron Variant from Shiitake-Mushroom-Derived Vesicle-like Nanoparticles." Viruses 16, no. 10 (2024): 1546. http://dx.doi.org/10.3390/v16101546.

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Lectins are a class of carbohydrate-binding proteins that may have antiviral activity by binding to the glycans on the virion surface to interfere with viral entry. We have identified a novel lectin (named Shictin) from Shiitake mushroom (Lentinula edodes)-derived vesicle-like nanoparticles (VLNs, or exosomes) that exhibits strong activity against the SARS-CoV-2 Omicron variant with an IC50 value of 87 nM. Shictin contains 298 amino acids and consists of two unique domains (N-terminal and C-terminal domain). The N-terminal domain is the carbohydrate-binding domain (CBD) that is homologous with

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Prado Acosta, Mariano, and Bernd Lepenies. "Bacterial glycans and their interactions with lectins in the innate immune system." Biochemical Society Transactions 47, no. 6 (2019): 1569–79. http://dx.doi.org/10.1042/bst20170410.

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Bacterial surfaces are rich in glycoconjugates that are mainly present in their outer layers and are of great importance for their interaction with the host innate immune system. The innate immune system is the first barrier against infection and recognizes pathogens via conserved pattern recognition receptors (PRRs). Lectins expressed by innate immune cells represent an important class of PRRs characterized by their ability to recognize carbohydrates. Among lectins in innate immunity, there are three major classes including the galectins, siglecs, and C-type lectin receptors. These lectins ma

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Hosoi, Masayuki, Shokei Kim, and Kenjiro Yamamoto. "Evidence for heterogeneity of glycosylation of human renin obtained by using lectins." Clinical Science 81, no. 3 (1991): 393–99. http://dx.doi.org/10.1042/cs0810393.

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1. In this study, the carbohydrate structure of pure human renin was examined by using various lectins. 2. Pure renin could be separated into three forms by concanavalin A chromatography, a concanavalin A-unbound form, a loosely bound form and a tightly bound form, termed renins A, B and C, respectively. Renins A, B and C accounted for 3, 13 and 84%, respectively, of the purified renin. These forms were all present in individual human plasma and the relative proportions in plasma were 27 ± 3, 33 ± 4 and 39 ± 5% (means ± sem) for renins A, B and C, respectively (n = 5). 3. Each form, electroblo

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Valadez-Vega, Carmen, Olivia Lugo-Magaña, Gabriel Betanzos-Cabrera, and José Roberto Villagómez-Ibarra. "Partial Characterization of Lectins Purified from the Surco and Vara (Furrow and Rod) Varieties of Black Phaseolus vulgaris." Molecules 27, no. 23 (2022): 8436. http://dx.doi.org/10.3390/molecules27238436.

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As they manifest specifically and reversibly, lectins are proteins or glycoproteins with the characteristic of agglutinating erythrocytes. Given that grain legume lectins can represent 10% of protein content and can have various biological functions, they are extensively studied. The objective of this work was to purify and partially characterize the lectins of Phaseolus vulgaris black, var surco and vara (LBBS and LBBV). Both lectin types were purified by affinity chromatography on stroma matrix, which agglutinated human erythrocytes type A, B, and O, as well as rabbit, hamster, pig, and chic

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Zhang, Xiaotian, Songying Sun, Wenchao Zhao, et al. "A single-pass type I membrane protein, mannose-specific L-type lectin, potentially involved in the adhesion and invasion of Cryptosporidium parvum." Parasite 31 (2024): 51. http://dx.doi.org/10.1051/parasite/2024051.

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Cryptosporidium is a globally distributed zoonotic protozoan parasite that can cause severe diarrhea in humans and animals. L-type lectins are carbohydrate-binding proteins involved in multiple pathways in animals and plants, including protein transportation, secretion, innate immunity, and the unfolded protein response signaling pathway. However, the biological function of the L-type lectins remains unknown in Cryptosporidium parvum. Here, we preliminarily characterized an L-type lectin in C. parvum (CpLTL) that contains a lectin-leg-like domain. Immunofluorescence assay confirmed that CpLTL

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Odiegwu C.N.C., Egbobe C.G., Ifejirika-Ugboaja E.C., Ogamba S.E., Odiegwu C.K.D., and Ifejirika-Ezeonyi E.C. "Assessment of lectinic activity potentials in extracts of some tropical Euphorbiaceace." World Journal of Advanced Research and Reviews 10, no. 3 (2021): 001–11. http://dx.doi.org/10.30574/wjarr.2021.10.3.0225.

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Lectins bind a variety of cells having cell surface glycoprotein or glycolipid, such as erythrocytes, leukemic cells, yeast and several types of bacteria. Several specificity groups have been identified such as mannose, galactose, N-acetyl glucoseamine, N-acetyl galactoseamine, L-fucose and N-acetyl neuraminic acid. The presence of two or more binding sites for each Lectin molecule allows the agglutination of many cell type. Sixteen (16) species of some tropical Euphorbiaceae plants were assessed for the presence of Lectins. The leaves of Acalypha torta, Acalypha wiskesiana, Acalypha hispida,

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Keller, Bettina G., and Christoph Rademacher. "Allostery in C-type lectins." Current Opinion in Structural Biology 62 (June 2020): 31–38. http://dx.doi.org/10.1016/j.sbi.2019.11.003.

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Kerrigan, Ann M., and Gordon D. Brown. "C-type lectins and phagocytosis." Immunobiology 214, no. 7 (2009): 562–75. http://dx.doi.org/10.1016/j.imbio.2008.11.003.

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Toribio, M. L., A. de la Hera, P. Pereira, and M. O. de Landázuri. "Modulation of cytolytic T cell function by lectins." Journal of Immunology 134, no. 4 (1985): 2179–84. http://dx.doi.org/10.4049/jimmunol.134.4.2179.

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Abstract Human thymocytes cultured for 5 days in interleukin 2 containing supernatants (IL 2 Sup) virtually become a population of mature T cells (T3+, HTA-) that acquires strong cytotoxic activity against NK-sensitive and NK-resistant target cells. The addition of different lectins to the cultures abrogated the expression of the cytotoxic activity and enhanced thymocyte proliferation. The modulation of this cytotoxic activity by lectins has the following properties: a) inhibition of cytotoxicity is related to the concentration of lectins added, but does not correlate with their mitogenic prop

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Matsumoto, Makoto, Takashi Tanaka, Tsuneyasu Kaisho, et al. "A Novel LPS-Inducible C-Type Lectin Is a Transcriptional Target of NF-IL6 in Macrophages." Journal of Immunology 163, no. 9 (1999): 5039–48. http://dx.doi.org/10.4049/jimmunol.163.9.5039.

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Abstract C-type lectins serve multiple functions through recognizing carbohydrate chains. Here we report a novel C-type lectin, macrophage-inducible C-type lectin (Mincle), as a downstream target of NF-IL6 in macrophages. NF-IL6 belongs to the CCAAT/enhancer binding protein (C/EBP) of transcription factors and plays a crucial role in activated macrophages. However, what particular genes are regulated by NF-IL6 has been poorly defined in macrophages. Identification of downstream targets is required to elucidate the function of NF-IL6 in more detail. To identify downstream genes of NF-IL6, we sc

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Padiyappa, Shruthishree D., Hemavathi Avalappa, Madhusudana Somegowda, et al. "Immunoadjuvant and Humoral Immune Responses of Garlic (Allium sativum L.) Lectins upon Systemic and Mucosal Administration in BALB/c Mice." Molecules 27, no. 4 (2022): 1375. http://dx.doi.org/10.3390/molecules27041375.

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Dietary food components have the ability to affect immune function; following absorption, specifically orally ingested dietary food containing lectins can systemically modulate the immune cells and affect the response to self- and co-administered food antigens. The mannose-binding lectins from garlic (Allium sativum agglutinins; ASAs) were identified as immunodulatory proteins in vitro. The objective of the present study was to assess the immunogenicity and adjuvanticity of garlic agglutinins and to evaluate whether they have adjuvant properties in vivo for a weak antigen ovalbumin (OVA). Garl

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Hart, Derek N. J., Seema Khan, Elisabetta d’Aniello, Kylie J. McDonald, and Masato Kato. "Role of Novel C-Type Lectin Receptor DCL-1 in Phagocytes and Dendritic Cells." Blood 110, no. 11 (2007): 2419. http://dx.doi.org/10.1182/blood.v110.11.2419.2419.

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Abstract Cell surface C-type lectins are implicated in many aspects of immunity. For example, professional phagocytes utilise cell surface C-type lectins in pathogen recognition/binding and phagocytosing the pathogens for destruction and/or antigen processing (e.g. mannose receptor, DC-SIGN, dectin-1). Some C-type lectins are involved in cell-cell adhesion and trafficking of leukocytes (e.g. selectins). DCL-1 is a small type I transmembrane C-type lectin receptor, discovered as a genetic fusion partner of DEC-205. DCL-1 protein was highly conserved amongst the human, mouse and rat orthologs. T

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Weisz, O. A., and R. L. Schnaar. "Hepatocyte adhesion to carbohydrate-derivatized surfaces. I. Surface topography of the rat hepatic lectin." Journal of Cell Biology 115, no. 2 (1991): 485–93. http://dx.doi.org/10.1083/jcb.115.2.485.

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The rat hepatic lectins, galactose- and N-acetylgalactosamine-binding proteins found on the hepatocyte cell surface, mediate adhesion of isolated primary rat hepatocytes to artificial galactose-derivatized polyacrylamide gels. Biochemical and immunohistochemical techniques were used to examine the topographical redistribution of the rat hepatic lectins in response to galactose-mediated cell adhesion. Hepatocytes isolated from rat liver by collagenase perfusion had an average of 7 x 10(5) cell surface lectin molecules per cell, representing 30-50% of the total lectin molecules per cell, the rem

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Hioe, Catarina E., Muzafar Jan, Roya Feyznezhad, Vincenza Itri, Xiaomei Liu, and Chitra Upadhyay. "HIV-1 envelope glycan composition influences virus-host interaction." Journal of Immunology 202, no. 1_Supplement (2019): 197.17. http://dx.doi.org/10.4049/jimmunol.202.supp.197.17.

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Abstract HIV-1 envelope (Env) is densely shrouded with oligomannose- and complex-type glycans. These glycans interact with lectins, a family of carbohydrate-recognizing proteins. We evaluated lectins for the ability to block infection of HIV-1 isolates that differ in their sensitivity to neutralizing antibodies. The antibody-sensitive tier 1 viruses were blocked by lectins more easily than the resistant tier 2 viruses. When tier 2 viruses were produced with glycosidase inhibitors to express homogenously oligomannose-type glycans, they became more sensitive to mannose-binding lectins (GNA, GRFT

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Jégouzo, Sabine A. F., Conor Nelson, Thomas Hardwick, et al. "Mammalian lectin arrays for screening host–microbe interactions." Journal of Biological Chemistry 295, no. 14 (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

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L’Hôte, Corine, Sylvie Berger, and Yannis Karamanos. "O-glycosylation of Fibrinogen from Different Mammalian Species as Revealed by the Binding of Escherichia coli Biotinylated Lectins." Thrombosis and Haemostasis 76, no. 05 (1996): 710–14. http://dx.doi.org/10.1055/s-0038-1650648.

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SummaryAfter the demonstration that neither N-glycans nor neuraminic acid are involved in the binding of K88 lectins to the Bp and y chains of porcine fibrinogen and that their recognition was due to O-glycans (L’Hôte C, Berger S, Bourgerie S, Duval-Iflah Y, Julien R, Karamanos Y. Infect Immun 1995; 63: 1927-1932) it clearly appeared that these lectins could be used as probes to detect O-glycans on fibrinogens of other species. The conclusion of the present study is that many mammalian fibrinogens contain complex O-glycans on βp and γ chains. In addition, the combined use of the biotinylated K

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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 (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 presentatio

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Mizgina, Tatyana O., Sergey N. Baldaev, Galina N. Likhatskaya, et al. "Molecular Cloning and Characteristics of a Lectin from the Bivalve Glycymeris yessoensis." Marine Drugs 21, no. 2 (2023): 55. http://dx.doi.org/10.3390/md21020055.

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C-type lectins (CTLs) are a family of carbohydrate-binding proteins that mediate multiple biological events, including adhesion between cells, the turnover of serum glycoproteins, and innate immune system reactions to prospective invaders. Here, we describe the cDNA cloning of lectin from the bivalve Glycymeris yessoensis (GYL), which encodes 161 amino acids and the C-type carbohydrate recognition domain (CRD) with EPN and WND motifs. The deduced amino acid sequence showed similarity to other CTLs. GYL is a glycoprotein containing two N-glycosylation sites per subunit. N-glycans are made up of

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Rodrigues, Raquel, Maria Eduardo Figueira, Rosa Direito, Andreia Bento-Silva, Ricardo Boavida Ferreira, and Ana Cristina Ribeiro. "Exploring Lectin Bioactivity and Total Phenolic Compounds in Kiwifruit (Actinidia deliciosa var. Hayward)." Nutrients 16, no. 19 (2024): 3292. http://dx.doi.org/10.3390/nu16193292.

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Background: The consumption of kiwifruit (Actinidia deliciosa var. Hayward) is recognized for its health benefits due to its high vitamin C content and bioactive secondary metabolites, such as phenolic compounds with antioxidant properties. These compounds may help prevent chronic noncommunicable diseases, currently the leading cause of death. Additionally, plants and fruits contain proteins like lectins, which contribute to plant defense and may also have health-promoting effects, including antitumor and hypoglycemic activities. Objectives: The objective of this work was to evaluate and ident

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Giannasca, P. J., K. T. Giannasca, P. Falk, J. I. Gordon, and M. R. Neutra. "Regional differences in glycoconjugates of intestinal M cells in mice: potential targets for mucosal vaccines." American Journal of Physiology-Gastrointestinal and Liver Physiology 267, no. 6 (1994): G1108—G1121. http://dx.doi.org/10.1152/ajpgi.1994.267.6.g1108.

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We have used a panel of lectins and antibodies to describe the composition of complex carbohydrates associated with M cells in various regions of the intestinal tract of adult BALB/c mice. The fucose-specific lectin Ulex europaeus agglutinin type I (UEA I) is a marker of M cells in the small intestine and recognized M cells at an early stage of differentiation. Subpopulations of M cells in a single follicle-associated epithelium (FAE) could be distinguished by different fucose-specific probes. Certain lectins revealed that M cells have basal processes that extend into the underlying lymphoid t

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Drickamer, K. "Genomic screening for C-type lectins." Biochemical Society Transactions 30, no. 1 (2002): A3. http://dx.doi.org/10.1042/bst030a003a.

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Cambi, Alessandra, Marjolein Koopman, and Carl G. Figdor. "How C-type lectins detect pathogens." Cellular Microbiology 7, no. 4 (2005): 481–88. http://dx.doi.org/10.1111/j.1462-5822.2005.00506.x.

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Ding, Dongbing, Yao Yao, Songbai Zhang, Chunjie Su, and Yonglian Zhang. "C-type lectins facilitate tumor metastasis." Oncology Letters 13, no. 1 (2016): 13–21. http://dx.doi.org/10.3892/ol.2016.5431.

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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 (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 potenti

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Onishi, Yasuhiro, Koki Mise, Chieko Kawakita, et al. "Development of Urinary Diagnostic Biomarker for IgA Nephropathy by Lectin Microarray." American Journal of Nephrology 53, no. 1 (2021): 10–20. http://dx.doi.org/10.1159/000520998.

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<b><i>Introduction:</i></b> The pathogenic roles of aberrantly glycosylated IgA1 have been reported. However, it is unexplored whether the profiling of urinary glycans contributes to the diagnosis of IgAN. <b><i>Methods:</i></b> We conducted a retrospective study enrolling 493 patients who underwent renal biopsy at Okayama University Hospital between December 2010 and September 2017. We performed lectin microarray in urine samples and investigated whether c-statistics of the reference standard diagnosis model employing hematuria, proteinuria, and

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Wood, Stephen D., Lisa M. Wright, Colin D. Reynolds, et al. "Structure of the native (unligated) mannose-specific bulb lectin from Scilla campanulata (bluebell) at 1.7 Å resolution." Acta Crystallographica Section D Biological Crystallography 55, no. 7 (1999): 1264–72. http://dx.doi.org/10.1107/s0907444999005326.

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The X-ray crystal structure of native Scilla campanulata agglutinin, a mannose-specific lectin from bluebell bulbs and a member of the Liliaceae family, has been determined by molecular replacement and refined to an R value of 0.186 at 1.7 Å resolution. The lectin crystallizes in space group P21212 with unit-cell parameters a = 70.42, b = 92.95, c = 46.64 Å. The unit cell contains eight protein molecules of Mr = 13143 Da (119 amino-acid residues). The asymmetric unit comprises two chemically identical molecules, A and B, related by a non-crystallographic twofold axis perpendicular to c. This d

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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 arrang

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