Journal articles on the topic 'Lectin'
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1
Flower, Robert L. P. "Innate Immunity in Lobsters: Partial Purification and Characterization of a Panulirus cygnus Anti-A Lectin." ISRN Hematology 2012 (March 5, 2012): 1–5. http://dx.doi.org/10.5402/2012/964986.
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A lectin detected in haemolymph from the Australian spiny lobster Panulirus cygnus agglutinated human ABO Group A cells to a higher titre than Group O or B. The lectin also agglutinated rat and sheep erythrocytes, with reactivity with rat erythrocytes strongly enhanced by treatment with the proteolytic enzyme papain, an observation consistent with reactivity via a glycolipid. The lectin, purified by affinity chromatography on fixed rat-erythrocyte stroma, was inhibited equally by N-acetylglucosamine and N-acetylgalactosamine. Comparison of data from gel filtration of haemolymph (behaving as a 1,800,000 Da macromolecule), and polyacrylamide gel electrophoresis of purified lectin (a single 67,000 Da band), suggested that in haemolymph the lecin was a multimer. The purified anti-A lectin autoprecipitated unless the storage solution contained chaotropic inhibitors (125 mmol/L sucrose: 500 mmol/L urea). The properties of this anti-A lectin and other similar lectins are consistent with a role in innate immunity in these invertebrates.
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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 (July 17, 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 optimize the lectin staining methodology. We noted that the most effective conditions for lectin-labeling were when live HeLa cells were incubated with lectins diluted in Hank’s balanced salt solution (HBSS) with 3% Bovine serum albumin (BSA) for 10-30 minutes at 4 °C. Results: Incubating suspended cells with lectins necessitated smaller lectin concentrations, whereas lectin labeling of adherent cells required considerably larger concentrations. Wheat germ agglutinin (WGA) lectin mean fluorescence intensity (MFI) was concentration-dependent, but Concanavalin A (ConA) and Maclura pomifera (MPA) MFIs did not alter substantially with increasing lectin concentrations. Discussion: The optimal lectin concentration required was lectin-specific and based on whether the lectin fluorescence was assessed using flow cytometry or epifluorescence. Furthermore, the use of phosphate-buffered saline (PBS) for lectin dilution, cell permeabilization for intracellular labelling, and incubation of lectins in fixed cells reduced productive labelling of lectins on cell surfaces because it inhibited the lectin's ability to effectively bind the associated carbohydrate structure. Conclusion: Further research using diverse lectins on U937 macrophages is necessary to reach a definitive conclusion on the effect of Legionella on the overall host-cell glycocalyx composition during infection of these relevant immune cells.
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Ogilvie, Mary L., JoAnn Wilson Byl, and T. Kent Gartner. "Platelet Aggregation Is Stimulated by Lactose-lnhibitable Snake Venom Lectins." Thrombosis and Haemostasis 62, no. 02 (1989): 704–7. http://dx.doi.org/10.1055/s-0038-1646887.
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SummaryFive lactose-specific lectins from snake venoms were tested for the ability to stimulate the aggregation of human platelets. Three of the lectins, bushmaster (Lachesis muta), cottonmouth (Aricistrodon piscivorous leukostoma) and rattlesnake (Crotalus atrox) lectins, consistently stimulated secretion and aggregation. Thrombolectin (Bothrops atrox) occasionally caused aggregation. Copperhead (Agkistrodon contortrix contortrix) lectin did not by itself cause platelet aggregation. Lactose, a specific inhibitor of hemagglutination mediated by these lectins was a potent inhibitor of lectin-induced aggregation. Antiserum specific for bushmaster lectin inhibited aggregation by bushmaster lectin. In contrast, the same antiserum and anti-cottonmouth lectin serum enhanced aggregation by low levels of the other lectins.A variety of substances were assayed in the aggregometer for the ability to inhibit aggregation in response to these lectins. Both secretion and aggregation were inhibited by PGI2 and PGEx. Furthermore, lectin-induced aggregation was completely blocked by trifluoperazine and partially blocked by indomethacin. Monoclonal antibodies specific for GP IIb/IIIa (AP2, A2A9, LJP5, LJCP8) but not monoclonals directed against other platelet membrane proteins (API and AP3) inhibited lectin-induced aggregation. The peptide Arg-Gly-Asp-Ser but not Arg-Ala-Asp-Ser was a potent inhibitor of aggregation.
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Barre, Annick, Mathias Simplicien, Hervé Benoist, Els J. M. Van Damme, and Pierre Rougé. "Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties." Marine Drugs 17, no. 8 (July 26, 2019): 440. http://dx.doi.org/10.3390/md17080440.
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To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize mannose-containing glycans. Depending on the structural scaffold, man-specific seaweed lectins belong to five distinct structurally-related lectin families, namely (1) the griffithsin lectin family (β-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (β-barrel scaffold); (3) the legume lectin-like lectin family (β-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (β-prism II scaffold); and, (5) the MFP2-like lectin family (MFP2-like scaffold). Another algal lectin from Ulva pertusa, has been inferred to the methanol dehydrogenase related lectin family, because it displays a rather different GlcNAc-specificity. In spite of these structural discrepancies, all members from the five lectin families share a common ability to specifically recognize man-containing glycans and, especially, high-mannose type glycans. Because of their mannose-binding specificity, these lectins have been used as valuable tools for deciphering and characterizing the complex mannose-containing glycans from the glycocalyx covering both normal and transformed cells, and as diagnostic tools and therapeutic drugs that specifically recognize the altered high-mannose N-glycans occurring at the surface of various cancer cells. In addition to these anti-cancer properties, man-specific seaweed lectins have been widely used as potent human immunodeficiency virus (HIV-1)-inactivating proteins, due to their capacity to specifically interact with the envelope glycoprotein gp120 and prevent the virion infectivity of HIV-1 towards the host CD4+ T-lymphocyte cells in vitro.
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Bonnardel, François, Julien Mariethoz, Serge Pérez, Anne Imberty, and Frédérique Lisacek. "LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification." Nucleic Acids Research 49, no. D1 (November 11, 2020): D1548—D1554. http://dx.doi.org/10.1093/nar/gkaa1019.
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Abstract Lectins are non-covalent glycan-binding proteins mediating cellular interactions but their annotation in newly sequenced organisms is lacking. The limited size of functional domains and the low level of sequence similarity challenge usual bioinformatics tools. The identification of lectin domains in proteomes requires the manual curation of sequence alignments based on structural folds. A new lectin classification is proposed. It is built on three levels: (i) 35 lectin domain folds, (ii) 109 classes of lectins sharing at least 20% sequence similarity and (iii) 350 families of lectins sharing at least 70% sequence similarity. This information is compiled in the UniLectin platform that includes the previously described UniLectin3D database of curated lectin 3D structures. Since its first release, UniLectin3D has been updated with 485 additional 3D structures. The database is now complemented by two additional modules: PropLec containing predicted β-propeller lectins and LectomeXplore including predicted lectins from sequences of the NBCI-nr and UniProt for every curated lectin class. UniLectin is accessible at https://www.unilectin.eu/
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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 (September 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. Despite minor differences (carbohydrate content or A1%1cm), the two lectins showed similar molecular properties in that they consisted of two non-covalently linked monomers having a Mr of 29-30 kDa and their pI values indicated that both lectins were slightly acidic proteins. The C. ensiformis lectin (CEL-II) and D. grandiflora lectin (DGL-II) specifically recognised the H-type 2 blood group (alpha-L-Fuc (1-2)-beta-D-Gal (1-4)-beta-D-GlcNAc-O-R), while binding to H-type 1, H-type 3, H-type 4, Leª or Le y was weaker. Carbohydrate inhibition of erythroagglutination showed that simple sugars were weakly recognised by the lectins, if at all. The N-terminal region presented a unique sequence hitherto found only in some Diocleinae lectins (designated type II). The overall results confirmed the existence of a second distinct lectin type, phylogenetically close to Diocleinae species. The data indicate a functional similarity among lectins of this type which possesses distinctive characteristics differentiating them from "classical" Man/Glc lectins.
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Petrova, Natalia, and Natalia Mokshina. "Using FIBexDB for In-Depth Analysis of Flax Lectin Gene Expression in Response to Fusarium oxysporum Infection." Plants 11, no. 2 (January 7, 2022): 163. http://dx.doi.org/10.3390/plants11020163.
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Plant proteins with lectin domains play an essential role in plant immunity modulation, but among a plurality of lectins recruited by plants, only a few members have been functionally characterized. For the analysis of flax lectin gene expression, we used FIBexDB, which includes an efficient algorithm for flax gene expression analysis combining gene clustering and coexpression network analysis. We analyzed the lectin gene expression in various flax tissues, including root tips infected with Fusarium oxysporum. Two pools of lectin genes were revealed: downregulated and upregulated during the infection. Lectins with suppressed gene expression are associated with protein biosynthesis (Calreticulin family), cell wall biosynthesis (galactose-binding lectin family) and cytoskeleton functioning (Malectin family). Among the upregulated lectin genes were those encoding lectins from the Hevein, Nictaba, and GNA families. The main participants from each group are discussed. A list of lectin genes, the expression of which can determine the resistance of flax, is proposed, for example, the genes encoding amaranthins. We demonstrate that FIBexDB is an efficient tool both for the visualization of data, and for searching for the general patterns of lectin genes that may play an essential role in normal plant development and defense.
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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 (February 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) the Helix pomatia lectin and Sambucus nigra L. lectin bound to type II but not type I cells; and (c) the Erythrina cristagalli lectin reacted with type I cells but was unreactive with type II cells. The specificity of staining was assessed by control experiments, including pre-absorption of the lectins with various oligosaccharides and enzymatic pre-treatment of sections with highly purified glycosidases to remove specific sugar residues. The results demonstrate that these lectins can be used to distinguish between type I and type II cells and would therefore be useful probes for investigating cell dynamics during lung development and remodeling.
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Levine, E., R. Werner, and G. Dahl. "Cell-cell channel formation and lectins." American Journal of Physiology-Cell Physiology 261, no. 6 (December 1, 1991): C1025—C1032. http://dx.doi.org/10.1152/ajpcell.1991.261.6.c1025.
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The oocyte cell-cell channel assay was used to investigate determinants of the rate of channel formation. After injection of connexin-specific mRNA, oocytes accumulate a pool of precursors from which cell-cell channels can form after oocytes are paired. Channel formation was found to be increased if oocytes are pretreated with lectins before pairing. Several lectins differing in their carbohydrate binding affinities can exert this effect. Lectin-specific sugars suppress the effect on cell-cell channel formation only if the sugar is mixed with the lectin before application to the oocyte. If the lectin is first bound to the oocyte and then the sugar is added, no significant inhibition is seen. The promotion of channel formation by lectins is enhanced by adding an incubation period in regular medium after lectin treatment, before pairing of the oocytes. Electron microscopic studies with gold-conjugated lectins show that the lectin receptors are clustered on the free membrane surface and are taken up in endocytotic vesicles. These data suggest that the observed acceleration of cell-cell channel formation by lectins can be attributed to the removal of steric hindrance, which is a consequence of clustering of the bulky glycoprotein lectin receptors as well as of the removal from the surface by endocytosis.
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Gerhardus, M. J. T., J. M. C. Baggen, W. P. W. Van Der Knaap, and T. Sminia. "Analysis of surface carbohydrates of Trichobilharzia ocellata miracidia and sporocysts using lectin binding techniques." Parasitology 103, no. 1 (August 1991): 51–59. http://dx.doi.org/10.1017/s003118200005928x.
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Miracidia and in vitro-derived primary sporocysts of the avian schistosome Trichobilharzia ocellata were studied for the expression and the characteristics of glycoconjugate moieties comprising the surface coat. Using a panel of 9 peroxidase labelled lectins, several different lectin binding sites were demonstrated on the larvae. Fixed miracidia have binding sites for 7 of the lectins; wheat-germ agglutinin binds to both the ciliated plates and the tegumental ridges between them; the other 6 lectins bind to the plates only. Three of the miracidia-binding lectins, wheat-germ agglutinin, concanavalin A and peanut agglutinin, also bind to fixed sporocysts. Since the miracidial ridges are devoid of binding sites for concanavalin A and peanut agglutinin, whereas the sporocyst tegument binds these lectins, it appears that these sites become exposed during or shortly after transformation. In saturation experiments, low concentrations of peanut agglutinin and concanavalin A are bound more avidly by sporocysts than by miracidia, indicating a higher binding affinity of the former. The two larval forms do not differ in affinity for wheat-germ agglutinin but they have different binding capacities; when offered in high concentrations, more of this lectin is bound by sporocysts than by miracidia. Lectin binding was competitively inhibited by adding the appropriate free saccharides. Live larvae showed the same lectin binding pattern as did fixed specimens. Proteinase treatment reduced lectin binding to living and, to a lesser extent, to fixed larvae, suggesting that binding sites are constituents of proteoglycoconjugates. After SDS–PAGE of extracts from miracidia and sporocysts and subsequent Western blotting, some of the lectins failed to bind glycoproteins, others reacted with an array of bands. The patterns differed among the lectins and each lectin gave different patterns for miracidia and sporocysts. The results obtained with these two lectin-binding techniques support the conclusion that stage-specific proteoglycoconjugates occur at the surface of T. ocellata larvae.
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Ooi, Linda SM, Hexiang Wang, T. B. Ng, and Vincent EC Ooi. "Isolation and characterization of a mannose-binding lectin from leaves of the Chinese daffodil Narcissus tazetta." Biochemistry and Cell Biology 76, no. 4 (August 1, 1998): 601–8. http://dx.doi.org/10.1139/o98-022.
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A mannose-binding lectin was isolated from leaves of the Chinese daffodil Narcissus tazetta (family Amaryllidaceae) using a procedure that comprised extraction with aqueous buffer, ammonium sulfate precipitation, ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel Blue gel and mannose-agarose, and FPLC-gel filtration on Superose 12. The lectin was adsorbed on mannose-agarose and unadsorbed on DEAE-cellulose and Affi-gel Blue gel. It was an unglycosylated homodimer with a molecular mass of 26 kDa. Analysis of the N-terminal sequence of the N. tazetta lectin revealed considerable homology to lectins from the daffodil Narcissus pseudonarcissus, the snowdrop Galanthus nivalis (family Amaryllidaceae), the tulip Tulipa, and Kidachi aloe Aloe arborescens (family Liliaceae), and the orchid lectins (family Orchidaceae). The most striking likeness exists among the Amaryllidaceae lectins. The N. tazetta lectin exhibits hemagglutinating activity toward rabbit erythrocytes.Key words: daffodil, mannose-binding lectin, agglutinin.
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Rauschenberg, Melanie, Eva-Corrina Fritz, Christian Schulz, Tobias Kaufmann, and Bart Jan Ravoo. "Molecular recognition of surface-immobilized carbohydrates by a synthetic lectin." Beilstein Journal of Organic Chemistry 10 (June 16, 2014): 1354–64. http://dx.doi.org/10.3762/bjoc.10.138.
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The molecular recognition of carbohydrates and proteins mediates a wide range of physiological processes and the development of synthetic carbohydrate receptors (“synthetic lectins”) constitutes a key advance in biomedical technology. In this article we report a synthetic lectin that selectively binds to carbohydrates immobilized in a molecular monolayer. Inspired by our previous work, we prepared a fluorescently labeled synthetic lectin consisting of a cyclic dimer of the tripeptide Cys-His-Cys, which forms spontaneously by air oxidation of the monomer. Amine-tethered derivatives of N-acetylneuraminic acid (NANA), β-D-galactose, β-D-glucose and α-D-mannose were microcontact printed on epoxide-terminated self-assembled monolayers. Successive prints resulted in simple microarrays of two carbohydrates. The selectivity of the synthetic lectin was investigated by incubation on the immobilized carbohydrates. Selective binding of the synthetic lectin to immobilized NANA and β-D-galactose was observed by fluorescence microscopy. The selectivity and affinity of the synthetic lectin was screened in competition experiments. In addition, the carbohydrate binding of the synthetic lectin was compared with the carbohydrate binding of the lectins concanavalin A and peanut agglutinin. It was found that the printed carbohydrates retain their characteristic selectivity towards the synthetic and natural lectins and that the recognition of synthetic and natural lectins is strictly orthogonal.
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Abdulina, D. R., L. M. Purish, and G. O. Iutynska. "Specificity of Lectins Labeled with Colloidal Gold to the Exopolymeric Matrix Carbohydrates of the Sulfate-Reducing Bacteria Biofilm Formed on Steel." Mikrobiolohichnyi Zhurnal 82, no. 5 (October 17, 2020): 11–20. http://dx.doi.org/10.15407/microbiolj82.05.011.
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The studies of the carbohydrate composition of the sulfate-reducing bacteria (SRB) biofilms formed on the steel surface, which are a factor of microbial corrosion, are significant. Since exopolymers synthesized by bacteria could activate corrosive processes. The aim of the study was to investigate the specificity of commercial lectins, labeled with colloidal gold to carbohydrates in the biofilm exopolymeric matrix produced by the corrosive-relevant SRB strains from man-caused ecotopes. Methods. Microbiological methods (obtaining of the SRB biofilms during cultivation in liquid Postgate B media under microaerophilic conditions), biochemical methods (lectin-binding analysis of 10 commercial lectins, labeled with colloidal gold), transmission electron microscopy using JEM-1400 JEOL. Results. It was shown using transmission electron microscopy that the binding of lectins with carbohydrates in the biofilm of the studied SRB strains occurred directly in the exopolymerіс matrix, as well as on the surfaces of bacterial cells, as seen by the presence of colloidal gold particles. For detection of the neutral carbohydrates (D-glucose and D-mannose) in the biofilm of almost all studied bacterial strains PSA lectin was the most specific. This lectin binding in biofilms of Desulfotomaculum sp. К1/3 and Desulfovibrio sp. 10 strains was higher in 90.8% and 94.4%, respectively, then for ConA lectin. The presence of fucose in the SRB biofilms was detected using LABA lectin, that showed specificity to the biofilm EPS of all the studied strains. LBA lectin was the most specific to N-аcetyl-D-galactosamine for determination of amino sugars in the biofilm. The amount of this lectin binding in D. vulgaris DSM644 biofilm was 30.3, 10.1 and 9.3 times higher than SBA, SNA and PNA lectins, respectively. STA, LVA and WGA lectins were used to detect the N-acetyl-Dglucosamine and sialic acid in the biofilm. WGA lectin showed specificity to N-acetyl-D-glucosamine in the biofilm of all the studied SRB; maximum number of bounded colloidal gold particles (175 particles/μm2) was found in the Desulfotomaculum sp. TC3 biofilm. STA lectin was interacted most actively with N-acetyl-D-glucosamine in Desulfotomaculum sp. TC3 and Desulfomicrobium sp. TC4 biofilms. The number of bounded colloidal gold particles was in 9.2 and 7.4 times higher, respectively, than using LVA lectin. The lowest binding of colloidal gold particles was observed for LVA lectin. Conclusions. It was identified the individual specificity of the 10 commercial lectins to the carbohydrates of biofilm matrix on the steel surface, produced by SRB. It was estimated that lectins with identical carbohydrates specificity had variation in binding to the biofilm carbohydrates of different SRB strains. Establishing of the lectin range selected for each culture lead to the reduction of the scope of studies and labor time in the researching of the peculiarities of exopolymeric matrix composition of biofilms formed by corrosiverelevant SRB.
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Mewe, Marco, Denis Tielker, Robert Schönberg, Melitta Schachner, Karl-Erich Jaeger, and Udo Schumacher. "Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia." Journal of Laryngology & Otology 119, no. 8 (August 2005): 595–99. http://dx.doi.org/10.1258/0022215054516313.
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The bacterium Pseudomonas aeruginosa (PA) produces two carbohydrate binding lectins, designated PA lectin-I and lectin-II (PA-IL, PA-IIL). Both lectins are used by the bacterium to adhere to the glycocalyx of mammalian cells. In addition, the lectins immobilize ciliary beat. The kinetics of ciliary beat inhibition by each individual lectin have been analysed; however, their joint action on cilia has not been reported. Here we demonstrate that PA-IL and PA-IIL inhibit ciliary beat in a similar time-dependent manner. If applied simultaneously, ciliary beat inhibition after five hours of incubation was weaker than if each lectin was applied separately. Thus it can be hypothesized that the lectins compete for the same binding site(s) of the glycocalyx. Sugar inhibition experiments demonstrate that D-galactose and L-fucose inhibit both lectins, although clear preferences of D-galactose for PA-IL and of L-fucose for PA-IIL exist. These interactions have to be kept in mind when designing sugar-based therapies.
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Battistella, Roberta, Marios Kritsilis, Hana Matuskova, Douglas Haswell, Anne Xiaoan Cheng, Anja Meissner, Maiken Nedergaard, and Iben Lundgaard. "Not All Lectins Are Equally Suitable for Labeling Rodent Vasculature." International Journal of Molecular Sciences 22, no. 21 (October 26, 2021): 11554. http://dx.doi.org/10.3390/ijms222111554.
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The vascular system is vital for all tissues and the interest in its visualization spans many fields. A number of different plant-derived lectins are used for detection of vasculature; however, studies performing direct comparison of the labeling efficacy of different lectins and techniques are lacking. In this study, we compared the labeling efficacy of three lectins: Griffonia simplicifolia isolectin B4 (IB4); wheat germ agglutinin (WGA), and Lycopersicon esculentum agglutinin (LEA). The LEA lectin was identified as being far superior to the IB4 and WGA lectins in histological labeling of blood vessels in brain sections. A similar signal-to-noise ratio was achieved with high concentrations of the WGA lectin injected during intracardial perfusion. Lectins were also suitable for labeling vasculature in other tissues, including spinal cord, dura mater, heart, skeletal muscle, kidney, and liver tissues. In uninjured tissues, the LEA lectin was as accurate as the Tie2–eGFP reporter mice and GLUT-1 immunohistochemistry for labeling the cerebral vasculature, validating its specificity and sensitivity. However, in pathological situations, e.g., in stroke, the sensitivity of the LEA lectin decreases dramatically, limiting its applicability in such studies. This work can be used for selecting the type of lectin and labeling method for various tissues.
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Ceri, Howard, Wei Sek Hwang, and Helen Cheung. "Endogenous heparin-binding lectin activity in human placenta: purification and developmental expression." Biochemistry and Cell Biology 68, no. 4 (April 1, 1990): 790–95. http://dx.doi.org/10.1139/o90-113.
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Human placental extracts contain a herapin-inhibitable lectin activity. The lectin, which closely resembles those from chicken and rat tissues, was purified by heparin-affinity chromatography. It shares many properties with the previously reported lectins, including hapten specificity, molecular weight of monomers, and immunological cross-reactivity. Sections from different stages of placental development, stained by immunohistochemistry procedures using lectin-specific antibody, showed that the lectin was initially present only in cytotrophoblasts of early first trimester villi. Later in the first trimester, both cytotrophoblasts and syncytiotrophoblasts were stained positively for lectin. From second trimester to term, the lectin was seen only in syncytiotrophoblasts.Key words: lectin, human placenta, development, heparin, cytotrophoblast, syncytiotrophoblast.
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Matsuno, Keita, Noriko Kishida, Katsuaki Usami, Manabu Igarashi, Reiko Yoshida, Eri Nakayama, Masayuki Shimojima, et al. "Different Potential of C-Type Lectin-Mediated Entry between Marburg Virus Strains." Journal of Virology 84, no. 10 (March 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 C-type lectin, human macrophage galactose-type C-type lectin (hMGL), or dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN) more efficiently than VSV pseudotyped with Musoke GP (VSV-Musoke). Unexpectedly, the binding affinity of the C-type lectins to the carbohydrates on GPs did not correlate with the different efficiency of C-type lectin-mediated entry. Site-directed mutagenesis identified the amino acid at position 547, which switched the efficiency of C-type lectin-mediated entry. In a three-dimensional model of GP, this amino acid was in close proximity to the putative site of cathepsin processing. Interestingly, the cathepsin inhibitors reduced the infectivity of VSV-Angola less efficiently than that of VSV-Musoke in C-type lectin-expressing K562 cells, whereas only a limited difference was found in control cells. The amino acid at position 547 was critical for the different effects of the inhibitors on the virus infectivities. These results suggest that the efficiency of C-type lectin-mediated entry of filoviruses is controlled not only by binding affinity between C-type lectins and GP but also by mechanisms underlying endosomal entry, such as proteolytic processing by the cathepsins.
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GRUBHOFFER, L., V. KOVÁŘ, and N. RUDENKO. "Tick lectins: structural and functional properties." Parasitology 129, S1 (October 2004): S113—S125. http://dx.doi.org/10.1017/s0031182004004858.
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Few papers have been published on tick lectins so far, and therefore more data are needed to complete the mosaic of knowledge of their structural and functional properties. Tissue-specific lectin/haemagglutinin activities of both soft and hard ticks have been investigated. Some tick lectins are proteins with binding affinity for sialic acid, various derivatives of hexosamines and different glycoconjugates. Most tick lectin/haemagglutinin activities are blood meal enhanced, and could serve as molecular factors of self/non-self recognition in defence reactions against bacteria or fungi, as well as in pathogen/parasite transmission. Dorin M, the plasma lectin ofOrnithodoros moubata, is the first tick lectin purified so far from tick haemolymph, and the first that has been fully characterized. Partial characterization of other tick lectins/haemagglutinins has been performed mainly with respect to their carbohydrate binding specificities and immunochemical features.
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Xie, Yixuan, Ying Sheng, Qiongyu Li, Seunghye Ju, Joe Reyes, and Carlito B. Lebrilla. "Determination of the glycoprotein specificity of lectins on cell membranes through oxidative proteomics." Chemical Science 11, no. 35 (2020): 9501–12. http://dx.doi.org/10.1039/d0sc04199h.
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Lebreton, Annie, François Bonnardel, Yu-Cheng Dai, Anne Imberty, Francis M. Martin, and Frédérique Lisacek. "A Comprehensive Phylogenetic and Bioinformatics Survey of Lectins in the Fungal Kingdom." Journal of Fungi 7, no. 6 (June 7, 2021): 453. http://dx.doi.org/10.3390/jof7060453.
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Fungal lectins are a large family of carbohydrate-binding proteins with no enzymatic activity. They play fundamental biological roles in the interactions of fungi with their environment and are found in many different species across the fungal kingdom. In particular, their contribution to defense against feeders has been emphasized, and when secreted, lectins may be involved in the recognition of bacteria, fungal competitors and specific host plants. Carbohydrate specificities and quaternary structures vary widely, but evidence for an evolutionary relationship within the different classes of fungal lectins is supported by a high degree of amino acid sequence identity. The UniLectin3D database contains 194 fungal lectin 3D structures, of which 129 are characterized with a carbohydrate ligand. Using the UniLectin3D lectin classification system, 109 lectin sequence motifs were defined to screen 1223 species deposited in the genomic portal MycoCosm of the Joint Genome Institute. The resulting 33,485 putative lectin sequences are organized in MycoLec, a publicly available and searchable database. These results shed light on the evolution of the lectin gene families in fungi.
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Lesman-Movshovich, Efrat, Batia Lerrer, and Nechama Gilboa-Garber. "Blocking ofPseudomonas aeruginosalectins by human milk glycans." Canadian Journal of Microbiology 49, no. 3 (March 1, 2003): 230–35. http://dx.doi.org/10.1139/w03-027.
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The opportunistic human pathogen Pseudomonas aeruginosa produces a D-galactophilic (PA-IL) lectin and another lectin (PA-IIL) that binds L-fucose > D-arabinose > D-mannose in close association with its host-attacking factors. These lectins contribute to the virulence of P. aeruginosa by their involvement in the production, adhesion, and pathogenic effects of its biofilm on host cells. Therefore, they are considered targets for anti-Pseudomonas therapy. The present study compares their blocking by human milk samples with that of the plant lectin Con A. It demonstrates that human milk inhibits the hemagglutinating activities of the three lectins, with PA-IIL much more strongly inhibited than PA-IL or Con A. Using these lectins, Western blots of the milk samples accord with the hemagglutination inhibition data and disclose the distribution of the human milk glycoproteins that inhibit each lectin. The data of this paper reveal the high efficiency of human milk components in blocking the P. aeruginosa lectins and the usefulness of these lectins for detecting milk glycoprotein saccharides, which may protect the infant against infections.Key words: Pseudomonas aeruginosa, lectins, human milk, glycoproteins, Western blotting.
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Coelho, Luana Cassandra Breitenbach Barroso, Priscila Marcelino dos Santos Silva, Vera Lúcia de Menezes Lima, Emmanuel Viana Pontual, Patrícia Maria Guedes Paiva, Thiago Henrique Napoleão, and Maria Tereza dos Santos Correia. "Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications." Evidence-Based Complementary and Alternative Medicine 2017 (2017): 1–22. http://dx.doi.org/10.1155/2017/1594074.
Full textAbstract:
Lectins are proteins extensively used in biomedical applications with property to recognize carbohydrates through carbohydrate-binding sites, which identify glycans attached to cell surfaces, glycoconjugates, or free sugars, detecting abnormal cells and biomarkers related to diseases. These lectin abilities promoted interesting results in experimental treatments of immunological diseases, wounds, and cancer. Lectins obtained from virus, microorganisms, algae, animals, and plants were reported as modulators and tool markers in vivo and in vitro; these molecules also play a role in the induction of mitosis and immune responses, contributing for resolution of infections and inflammations. Lectins revealed healing effect through induction of reepithelialization and cicatrization of wounds. Some lectins have been efficient agents against virus, fungi, bacteria, and helminths at low concentrations. Lectin-mediated bioadhesion has been an interesting characteristic for development of drug delivery systems. Lectin histochemistry and lectin-based biosensors are useful to detect transformed tissues and biomarkers related to disease occurrence; antitumor lectins reported are promising for cancer therapy. Here, we address lectins from distinct sources with some biological effect and biotechnological potential in the diagnosis and therapeutic of diseases, highlighting many advances in this growing field.
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Kuno, Atsushi, Yuzuru Ikehara, Yasuhito Tanaka, Takashi Angata, Sachiko Unno, Maki Sogabe, Hidenori Ozaki, et al. "Multilectin Assay for Detecting Fibrosis-Specific Glyco-Alteration by Means of Lectin Microarray." Clinical Chemistry 57, no. 1 (January 1, 2011): 48–56. http://dx.doi.org/10.1373/clinchem.2010.151340.
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BACKGROUND Despite the progress made in understanding glyco-alterations of specific glycoproteins such as α1-acid glycoprotein (AGP) associated with liver fibrosis, there has been no useful diagnostic assay with a lectin recognizing the fibrosis-specific alteration and an antibody against the core protein. We therefore developed a compatible multiple lectin-antibody sandwich immunoassay on the basis of the results obtained by the lectin microarray analysis for monitoring fibrosis. METHODS AGP-enriched fractions derived from 0.5-μL sera of 125 patients with staging-determined fibrosis (26.4% F0–F1, 25.6% F2, 24% F3, and 23.2% F4) were subjected to systematic analysis by antibody-overlay lectin microarray. Data were analyzed to statistically relate to the degree of fibrosis progression. Additionally, we applied an optimal lectin signal set on the microarray to distinguish 45 patients with cirrhosis from 43 patients with chronic hepatitis. RESULTS Signal patterns of the 12 selected lectins reflected fibrosis-associated glyco-alteration of AGP. Among the 12 lectins, we found a specific lectin at each stage of fibrosis (i.e., significant fibrosis, severe fibrosis, and cirrhosis) (P < 0.0001). The test for the detection of cirrhosis showed that combinational use of 3 lectins (AOL, MAL, and DSA) on the array enhanced the diagnostic value for liver cirrhosis to 95% diagnostic sensitivity and 91% diagnostic specificity. CONCLUSIONS The multiple lectin-antibody sandwich immunoassay targeting AGP enables monitoring of disease progression in chronic hepatitis patients at risk of developing hepatocellular carcinoma.
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PT, Arokya Glory, Basil Rose MR, Josephine Priyatharshini C, Anitha C, and Venci Candida X. "Purification, Characterization and Antimicrobial Properties of Hemolymph Lectin from the Larva of Red Palm Weevil, Rhynchophorus ferrugineus." Journal of Advanced Zoology 44, S-5 (November 2, 2023): 1749–60. http://dx.doi.org/10.17762/jaz.v44is-5.1454.
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Lectins are renowned hemagglutinins and multivalent proteins with a well-known quality for sugar-binding specificity that participate significantly in invertebrate defense functions. Studies on biological activity of lectin from coleopteran insect are very scarce. A lectin with specific affinity for N-acetyl neuraminic acid was purified from the hemolymph of the larva of the red palm weevil, Rhynchophorus ferrugineus by biospecific adsorption using formalinized rabbit erythrocytes and affinity chromatography using PSM-linked cyanogen bromide activated Sepharose 4B. The specific activity of the lectin purified by affinity chromatography was much higher than the lectin purified by biospecific adsorption. The binding specificity of the weevil lectin distinguishes it from other known insect lectins. Like the crude agglutinin, the lectin purified by affinity chromatography also showed the same pattern of specificity towards erythrocytes. However, 4-to-8-fold decrease in HA titer was observed when tested with the purified lectin. In the same way, reduction is also observed in the HAI titer of the purified lectin with most of the inhibitors except PSM where the HAI titer was identical both in the crude agglutinin and purified lectin. Sugars N-acetyl neuraminic acid, N-acetyl mannosamine and N-acetyl-D-galactosamine inhibited the HA titer of the purified lectin with greater efficacy than the crude agglutinin. The sialic acid specificity of the lectin was confirmed by 16-fold reduction in HA titer with asialo rabbit erythrocytes and 32-fold reduction in HAI titer with desialylated PSM. The purified lectin is homogenous on sodium dodecyl sulphate-polyacrylamide electrophorogram with a molecular weight of about 60 kDa. The lectin showed antimicrobial activity against pathogenic bacteria Streptococcus mutans, Escherichia coli, Klebsiella pneumoniae and Pseudomonas aeroginosa and fungi Candida albicans and Aspergillus niger.
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Bols, N. C., M. M. Roberson, P. L. Haywood-Reid, R. F. Cerra, and S. H. Barondes. "Secretion of a cytoplasmic lectin from Xenopus laevis skin." Journal of Cell Biology 102, no. 2 (February 1, 1986): 492–99. http://dx.doi.org/10.1083/jcb.102.2.492.
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The skin of Xenopus laevis contains a soluble beta-galactoside-binding lectin with a approximately 16,000-mol-wt subunit. It resembles similar lectins purified from a variety of tissues from other vertebrates, and differs from two other soluble X. laevis lectins from oocytes and serum that bind alpha-galactosides. The skin lectin is concentrated in the cytoplasm of granular gland and mucous gland cells, as demonstrated by immunohistochemistry with the electron microscope. Upon injection with epinephrine, there is massive secretion of the cytoplasmic lectin from the granular gland cells.
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Milcheva, R., S. Petkova, and P. Babál. "Detection of O-glycosylated proteins from different Trichinella species muscle larvae total extracts." Helminthologia 46, no. 3 (September 1, 2009): 139–44. http://dx.doi.org/10.2478/s11687-009-0027-6.
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AbstractThe aim of the work was to analyze oligosaccharide composition with the focus on O-linked glycoproteins presence in the total extract obtained from different Trichinella species muscle larvae by means of lectin affino-blot with lectins selected for their sugar specificity. The absence of reactivity with two lectins, Tritrichomonas mobilensis lectin and Maackia amurensis agglutinin, indicated that the species of the Trichinella genus do not synthesize sialic acid. Reactivity with Helix pomatia lectin, Vicia villosa lectin-B4, peanut agglutinin and Ulex europeus lectin-I identified the presence of O-linked glycans identical to carcinoma-associated Tn-antigen (GalNAc-α-Ser/Thr) and T-antigen (Gal-β1,3-GalNAc-α-Ser/Thr) and also structures analogous to ABH-blood group antigens. The results obtained may contribute to a better understanding of the glycobiology of this parasitic nematode in relation to occupation of its intracellular niches.
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Chen, C., H. J. Durrant, R. P. Newton, and N. A. Ratcliffe. "A study of novel lectins and their involvement in the activation of the prophenoloxidase system in Blaberus discoidalis." Biochemical Journal 310, no. 1 (August 15, 1995): 23–31. http://dx.doi.org/10.1042/bj3100023.
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Endogenous and exogenous lectins have been found to activate the prophenoloxidase (proPO) system of the cockroach, Blaberus discoidalis, to the same extent as laminarin, a previously known microbial activator of proPO. The lectins can also further enhance this laminarin activation of the proPO system. Non-lectin proteins did not display any activation properties. The time course of proPO activation was studied after reconstitution of the reaction system using purified lectins, a trypsin-like enzyme, a trypsin inhibitor and partially purified lectin-binding proteins from the cockroach haemolymph. Lectin activation of the proPO system is probably not mediated by the lectin sugar-binding sites, as specific inhibitory sugars failed to abrogate the enhanced effect. The results suggest that alternative binding site(s) on the lectins may be involved in the proPO activation process. Evidence also suggests that several different lectins are involved in the regulation of the proPO system through separate receptors or binding molecules on the haemocytes, and that they exert their effects early in the sequence of events leading to conversion of proPO into its active form, possibly via regulation of serine proteases and protease inhibitors.
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Chikalovets, Irina, Alina Filshtein, Valentina Molchanova, Tatyana Mizgina, Pavel Lukyanov, Olga Nedashkovskaya, Kuo-Feng Hua, and Oleg Chernikov. "Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties." Molecules 25, no. 1 (December 30, 2019): 150. http://dx.doi.org/10.3390/molecules25010150.
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A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.
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Parkkinen, J. "Aberrant lectin-binding activity of immunoglobulin G in serum from rheumatoid arthritis patients." Clinical Chemistry 35, no. 8 (August 1, 1989): 1638–43. http://dx.doi.org/10.1093/clinchem/35.8.1638.
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Abstract Structural studies of oligosaccharide chains of immunoglobulin G (IgG) in serum have revealed a specific galactosylation deficiency associated with rheumatoid arthritis (RA). Using a two-site lectin-immunofluorometric assay, I studied the interaction of IgG with immobilized lectins. Compared with control IgG, IgG purified from RA patients' sera bound up to 40-fold more strongly to immobilized Bandeiraea simplicifolia agglutinin II, a lectin that specifically binds agalacto forms of other glycoproteins. However, inhibition studies and treatment of IgG with glycosidase suggested that only a minor part of this binding was mediated by agalacto oligosaccharides of IgG. Furthermore, these IgG samples bound even more intensively to some other immobilized lectins, including Ricinus communis agglutinin (RCA). The binding to RCA was not inhibited by lactose, a hapten sugar of RCA, whereas other lectin species in solution effectively inhibited it. Compared with intact RA IgG, isolated F(ab')2 fragments displayed only low RCA-binding activity. These results indicate the existence of a carbohydrate-nondependent interaction between RA IgG and different plant lectins. With use of immobilized RCA, the lectin-immunofluorometric assay was rapid and reproducible for measuring the aberrant lectin-binding activity of IgG directly in diluted serum samples.
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Vojdani, Aristo, Daniel Afar, and Elroy Vojdani. "Reaction of Lectin-Specific Antibody with Human Tissue: Possible Contributions to Autoimmunity." Journal of Immunology Research 2020 (February 11, 2020): 1–16. http://dx.doi.org/10.1155/2020/1438957.
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The aim of this study was to examine the direct reaction of specific lectin/agglutinin antibodies to different tissue antigens to confirm the theory that reactivity between them may contribute to autoimmunities. Lectins are carbohydrate-binding proteins found in nearly all fruits and vegetables. Undigested lectins can penetrate the gut barriers, provoking an immune response that results in the production of antibodies against them. Using an enzyme-linked immunosorbent assay, we reacted lectin-specific antibodies with 62 different tissue antigens. Wheat germ agglutinin-specific antibody was the most reactive with the tissue antigens (37 tissues out of 62), followed by red kidney bean phytohemagglutinin-specific antibody (20), soybean agglutinin-specific antibody (20), and peanut agglutinin-specific antibody (15). This reaction between anti-lectin antibodies and many human tissue antigens may be due to possible molecular mimicry and cross-reactivity. After our results confirmed that anti-lectin antibodies bind with human tissues, we wanted to determine the prevalence of these antibodies in the blood of 500 nominally healthy donors. The percentage elevation of antibodies against different lectins ranged from 12 to 16% (Immunoglobulin G), 9.7-14.7% (Immunoglobulin A), 12-18% (Immunoglobulin M), and 7.8-14.6% (Immunoglobulin E). Serial dilutions and inhibition study confirmed that these reactions were specific. Finally, we tested the lectin-specific antibody level in sera both negative and positive for RF and ANA and found that IgM anti-lectin antibody levels were highly correlated with RF but not with ANA level. The reaction of anti-lectin antibodies with human tissue components and their detection in RF-positive samples may describe mechanisms by which the production of antibodies against undigested lectins may contribute to the pathogenesis of some autoimmune diseases.
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Sivaji, N., K. V. Abhinav, and M. Vijayan. "Crystallization and biochemical characterization of an archaeal lectin fromMethanococcus voltaeA3." Acta Crystallographica Section F Structural Biology Communications 73, no. 5 (April 28, 2017): 300–304. http://dx.doi.org/10.1107/s2053230x17006173.
Full textAbstract:
A lectin fromMethanococcus voltaeA3 has been cloned, expressed, purified and characterized. The lectin appears to be specific for complex sugars. The protein crystallized in a tetragonal space group, with around 16 subunits in the asymmetric unit. Sequence comparisons indicate the lectin to have a β-prism I fold, with poor homology to lectins of known three-dimensional structure.
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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 12, no. 7 (September 30, 2013): 441–50. http://dx.doi.org/10.24297/jac.v12i7.6702.
Full textAbstract:
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 benign, non tumoral diseases, and healthy individuals. The conditions of the hemagglutination assay of serum lectin activity were optimized. They were Tris buffer of 20 mM and pH 7.4, 60 mM CaCl2, 800 µg of defatted serum, 30 ˚C for serum samples, 60 minutes for serum samples, and human blood of group A+ suspension with 1.4 optical density. The measurement of the specific hemagglutination activity of lectins demonstrated significant (p < 0.001) elevation in patients of malignant tumors when compared with those of other patients and healthy individuals. Lectin activity was pointed out to be significantly (r = 0.767 at p < 0.0005) positively correlated with stage of malignancies. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited by galactose, mannose, lactose, and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed N-Acetyl Galactosamine Binding Lectin (GalNAcBL). The purified folds and the yield was 178 with 32.4%. The polyacrylamide gel electrophoresis (PAGE) of purified lectin demonstrated one band consisted lectin activity. The approximate molecular weight of GalNAcBL was determined and found to be 63.83. Purified lectin was characterized through the assessment of the capability to agglutinate RBCs, inhibition by EDTA, pH dependency, thermal dependent, and carbohydrate contents. GalNAcBL were observed to be calcium dependence lectins (C-type). These results suggest that the diagnosis of the specific hemagglutination activity of lectin is promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers.
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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 (August 8, 2008): 441–50. http://dx.doi.org/10.24297/jac.v4i2.2705.
Full textAbstract:
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 benign, non tumoral diseases, and healthy individuals. The conditions of the hemagglutination assay of serum lectin activity were optimized. They were Tris buffer of 20 mM and pH 7.4, 60 mM CaCl2, 800 µg of defatted serum, 30 ˚C for serum samples, 60 minutes for serum samples, and human blood of group A+ suspension with 1.4 optical density. The measurement of the specific hemagglutination activity of lectins demonstrated significant (p < 0.001) elevation in patients of malignant tumors when compared with those of other patients and healthy individuals. Lectin activity was pointed out to be significantly (r = 0.767 at p < 0.0005) positively correlated with stage of malignancies. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited by galactose, mannose, lactose, and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed N-Acetyl Galactosamine Binding Lectin (GalNAcBL). The purified folds and the yield was 178 with 32.4%. The polyacrylamide gel electrophoresis (PAGE) of purified lectin demonstrated one band consisted lectin activity. The approximate molecular weight of GalNAcBL was determined and found to be 63.83. Purified lectin was characterized through the assessment of the capability to agglutinate RBCs, inhibition by EDTA, pH dependency, thermal dependent, and carbohydrate contents. GalNAcBL were observed to be calcium dependence lectins (C-type). These results suggest that the diagnosis of the specific hemagglutination activity of lectin is promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers.
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Yuan, Hui Jun, Ai Mei Yang, Hui Ling Gong, Jing Hu, Jing Ting Bao, and Yi Jun Yuan. "Hemagglutination Characterization of Lectins from Four Traditional Chinese Medicines." Advanced Materials Research 634-638 (January 2013): 1309–12. http://dx.doi.org/10.4028/www.scientific.net/amr.634-638.1309.
Full textAbstract:
Hemagglutination titer of crude lectin from four traditional chinese medicine was detected. Lectins from Radix Polygalae and Saxifraga stolonifera agglutinated red blood cells of rabbit, rat and chook potently. Heteropappus hispidus (Thunb.) Less lectin also agglutinated the three kinds of red blood cells, but hemagglutination titer was lower. Hemagglutination effect of Lepisorus waltonii (Ching) Ching lectin only appeared in rat red blood cells.
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Mattox, Daniel E., and Chris Bailey-Kellogg. "Comprehensive analysis of lectin-glycan interactions reveals determinants of lectin specificity." PLOS Computational Biology 17, no. 10 (October 6, 2021): e1009470. http://dx.doi.org/10.1371/journal.pcbi.1009470.
Full textAbstract:
Lectin-glycan interactions facilitate inter- and intracellular communication in many processes including protein trafficking, host-pathogen recognition, and tumorigenesis promotion. Specific recognition of glycans by lectins is also the basis for a wide range of applications in areas including glycobiology research, cancer screening, and antiviral therapeutics. To provide a better understanding of the determinants of lectin-glycan interaction specificity and support such applications, this study comprehensively investigates specificity-conferring features of all available lectin-glycan complex structures. Systematic characterization, comparison, and predictive modeling of a set of 221 complementary physicochemical and geometric features representing these interactions highlighted specificity-conferring features with potential mechanistic insight. Univariable comparative analyses with weighted Wilcoxon-Mann-Whitney tests revealed strong statistical associations between binding site features and specificity that are conserved across unrelated lectin binding sites. Multivariable modeling with random forests demonstrated the utility of these features for predicting the identity of bound glycans based on generalized patterns learned from non-homologous lectins. These analyses revealed global determinants of lectin specificity, such as sialic acid glycan recognition in deep, concave binding sites enriched for positively charged residues, in contrast to high mannose glycan recognition in fairly shallow but well-defined pockets enriched for non-polar residues. Focused fine specificity analysis of hemagglutinin interactions with human-like and avian-like glycans uncovered features representing both known and novel mutations related to shifts in influenza tropism from avian to human tissues. As the approach presented here relies on co-crystallized lectin-glycan pairs for studying specificity, it is limited in its inferences by the quantity, quality, and diversity of the structural data available. Regardless, the systematic characterization of lectin binding sites presented here provides a novel approach to studying lectin specificity and is a step towards confidently predicting new lectin-glycan interactions.
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Nsayef Muslim, Sahira, Wafaa Hassan Muslem, Raghad J. Fayyad, Alaa Naseer Mohammed Al, and Mohamed Faraj Edbeib. "Extraction and purification of lectin from rice grains and using it as a novel prebiotic and inhibitor toward some gastrointestinal organisms." Bionatura 8, no. 2 (June 15, 2023): 1–9. http://dx.doi.org/10.21931/rb/2023.08.02.71.
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Aims: Lectins are carbohydrates with structure usually binding with proteins. The isolation of lectins from local and inexpensive sources, such as rice, considered one of the chief cereal crops, is necessary due to its broad application. Methods: Lectin was extracted from a novel source, Oryza sativa grains, with solvent (hexane) of ratios (1:5 w/v) for 15 minutes. The extract solution was fractionated with ammonium sulfate at 25-65% saturation concentrations and then applied to a DEAE-cellulose column followed by a Sephadex G-100 column. SDS-PAGE has been done to vitrify from lectin purity. An enhancement and inhibition activities were calculated to detect the effect of lectin on lactic acid bacteria and pathogenic bacterial growth. The extracted lectin from three types of Oryza sativa grains showed various levels of erythrocyte agglutination from 8 to 32U/ml. Then, the specimen was loaded into a DEAE-cellulose column followed by gel using Sephadex G-100 column with a final specific activity of 246.15U/mg, 24.15 fold of purification and 70% yield of lectin. Findings: Lectin SDS-PAGE result revealed a single protein band with 43 k Da. The purified lectin exhibited a substantial prebiotic property of lactic acid bacteria growth enhancement while exhibiting apparent growth inhibition against tested pathogenic bacteria. Typically, prebiotic properties should inhibit the growth of pathogens and enhance the growth of beneficial and desirable bacteria like Lactobacillus reuteri. Conclusion: The lectin may be used in animal diet to improve digestibility and support gastrointestinal tract health. Keywords: Inhibitor agent; lectin; prebiotic; purification; Phyto hemagglutinins; rice grains.
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WRIGHT, Lisa M., Els J. M. VAN DAMME, Annick BARRE, Anthony K. ALLEN, Fred VAN LEUVEN, Colin D. REYNOLDS, Pierre ROUGE, and Willy J. PEUMANS. "Isolation, characterization, molecular cloning and molecular modelling of two lectins of different specificities from bluebell (Scilla campanulata) bulbs." Biochemical Journal 340, no. 1 (May 10, 1999): 299–308. http://dx.doi.org/10.1042/bj3400299.
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Two lectins have been isolated from bluebell (Scilla campanulata) bulbs. From their isolation by affinity chromatography, they are characterized as a mannose-binding lectin (SCAman) and a fetuin-binding lectin (SCAfet). SCAman preferentially binds oligosaccharides with α(1,3)- and α(1,6)-linked mannopyranosides. It is a tetramer of four identical protomers of approx. 13 kDa containing 119 amino acid residues; it is not glycosylated. The fetuin-binding lectin (SCAfet), which is not inhibited by any simple sugars, is also unglycosylated. It is a tetramer of four identical subunits of approx. 28 kDa containing 244 residues. Each 28 kDa subunit is composed of two 14 kDa domains. Both lectins have been cloned from a cDNA library and sequenced. X-ray crystallographic analysis and molecular modelling studies have demonstrated close relationships in sequence and structure between these lectins and other monocot mannose-binding lectins. A refined model of the molecular evolution of the monocot mannose-binding lectins is proposed.
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Hirabayashi, Jun, and Ryoichi Arai. "Lectin engineering: the possible and the actual." Interface Focus 9, no. 2 (February 15, 2019): 20180068. http://dx.doi.org/10.1098/rsfs.2018.0068.
Full textAbstract:
Lectins are a widespread group of sugar-binding proteins occurring in all types of organisms including animals, plants, bacteria, fungi and even viruses. According to a recent report, there are more than 50 lectin scaffolds (∼Pfam), for which three-dimensional structures are known and sugar-binding functions have been confirmed in the literature, which far exceeds our view in the twentieth century (Fujimoto et al. 2014 Methods Mol. Biol. 1200 , 579–606 ( doi:10.1007/978-1-4939-1292-6_46 )). This fact suggests that new lectins will be discovered either by a conventional screening approach or just by chance. It is also expected that new lectin domains including those found in enzymes as carbohydrate-binding modules will be generated in the future through evolution, although this has never been attempted on an experimental level. Based on the current state of the art, various methods of lectin engineering are available, by which lectin specificity and/or stability of a known lectin scaffold can be improved. However, the above observation implies that any protein scaffold, including those that have never been described as lectins, may be modified to acquire a sugar-binding function. In this review, possible approaches to confer sugar-binding properties on synthetic proteins and peptides are described.
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Fang, R., M. Mantle, and H. Ceri. "Characterization of quail intestinal mucin as a ligand for endogenous quail lectin." Biochemical Journal 293, no. 3 (August 1, 1993): 867–72. http://dx.doi.org/10.1042/bj2930867.
Full textAbstract:
The S-type lectins have been shown to be components of mucosal scrapings, and in avian systems these lectins have been localized immunohistochemically to the mucosal surface and goblet cells of the intestine. The interaction of lectin specifically with purified mucin has not, however, been established. Quail intestinal mucin was purified by two subsequent isopycnic density-gradient centrifugations in CsCl and chromatography on Sepharose Cl-2B. Purified mucin, obtained from the void volume of the Sepharose column, was characterized by SDS/PAGE, amino acid and carbohydrate analyses, sensitivity to thiol reduction, and cross-reactivity with antibody preparations to rat and human intestinal mucins on Western blots. Antibody raised against purified quail mucin partially cross-reacts with purified rat, rabbit and human intestinal mucins, and specifically labels the mucosal surface and goblet cells of quail intestine by the immunoperoxidase technique. Protein eluted by lactose from an affinity matrix composed of quail intestinal mucin possessed the same molecular mass on SDS/PAGE as intestinal lectin and reacted on Western blots with a lectin-specific antibody. The data clearly demonstrate the co-localization of lectin and mucin in the quail intestine and also the ability of the lectin to specifically interact with the purified mucin, raising the question of the role of endogenous lectins in secretions.
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Kawsar, Sarkar M. Abe, Imtiaj Hasan, Sultana Rajia, Yasuhiro Koide, Yuki Fujii, Ryuhei Hayashi, Masao Yamada, and Yasuhiro Ozeki. "Diverse Localization Patterns of an R-Type Lectin in Marine Annelids." Molecules 26, no. 16 (August 7, 2021): 4799. http://dx.doi.org/10.3390/molecules26164799.
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Lectins facilitate cell–cell contact and are critical in many cellular processes. Studying lectins may help us understand the mechanisms underlying tissue regeneration. We investigated the localization of an R-type lectin in a marine annelid (Perinereis sp.) with remarkable tissue regeneration abilities. Perinereis nuntia lectin (PnL), a galactose-binding lectin with repeating Gln-X-Trp motifs, is derived from the ricin B-chain. An antiserum was raised against PnL to specifically detect a 32-kDa lectin in the crude extracts from homogenized lugworms. The antiserum detected PnL in the epidermis, setae, oblique muscle, acicula, nerve cord, and nephridium of the annelid. Some of these tissues and organs also produced Galactose (Gal) or N-acetylgalactosamine (GalNAc), which was detected by fluorescent-labeled plant lectin. These results indicated that the PnL was produced in the tissues originating from the endoderm, mesoderm, and ectoderm. Besides, the localizing pattern of PnL partially merged with the binding pattern of a fluorescent-labeled mushroom lectin that binds to Gal and GalNAc. It suggested that PnL co-localized with galactose-containing glycans in Annelid tissue; this might be the reason PnL needed to be extracted with haptenic sugar, such as d-galactose, in the buffer. Furthermore, we found that a fluorescein isothiocyanate-labeled Gal/GalNAc-binding mushroom lectin binding pattern in the annelid tissue overlapped with the localizing pattern of PnL. These findings suggest that lectin functions by interacting with Gal-containing glycoconjugates in the tissues.
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Ghanimi Fard, Mina, Zahra Khabir, Philipp Reineck, Nicole M. Cordina, Hiroshi Abe, Takeshi Ohshima, Sagar Dalal, Brant C. Gibson, Nicolle H. Packer, and Lindsay M. Parker. "Targeting cell surface glycans with lectin-coated fluorescent nanodiamonds." Nanoscale Advances 4, no. 6 (2022): 1551–64. http://dx.doi.org/10.1039/d2na00036a.
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Nanodiamonds were coated in lectins to target glycan receptors on astrocytes, neurons and microglia. The uptake in each cell type was variable depending on their coating of Aleuria aurantia lectin, wheat germ agglutinin or tomato lectin.
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Kulkarni, S. R., and V. J. Tayade. "Bacteriostatic activity of con a lectin from Canavalia ensiformis." Indian Journal of Pharmaceutical and Biological Research 1, no. 04 (December 31, 2013): 59–63. http://dx.doi.org/10.30750/ijpbr.1.4.11.
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The aim of this work was to explore the therapeutic applications of Con A lectin from Canavalia ensiformis and to explore its antibacterial activity. Activity of lectin was quantified by their ability to agglutinate erythrocytes using Hemagglutination assay. Characterization and purity of Con A lectin was evaluated by using SDS-PAGE analysis. The reversal of hemagglutination activity of lectin was evaluated by using the sugars namely; mannose, galactose, lactose, fructose, glucose. The antibacterial activity of lectins was tested against Streptococcus mutans, Staphylococcus aureus, Bacillus subtilis, Escherichia coli using pour plate method. Amoxycillin was used as standard. At 250mg/ml concentration Con A lectin showed good bacteriostatic activity.
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Lakhtin, M., V. Lakhtin, V. Alyoshkin, and S. Afanasyev. "Lectins of beneficial microbes: system organisation, functioning and functional superfamily." Beneficial Microbes 2, no. 2 (June 1, 2011): 155–65. http://dx.doi.org/10.3920/bm2010.0014.
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In this review our last results and proposals with respect to general aspects of lectin studies are summarised and compared. System presence, organisation and functioning of lectins are proposed, and accents on beneficial symbiotic microbial lectins studies are presented. The proposed general principles of lectin functioning allows for a comparison of lectins with other carbohydrate-recognition systems. A new structure-functional superfamily of symbiotic microbial lectins is proposed and its main properties are described. The proposed superfamily allows for extended searches of the biological activities of any microbial member. Prospects of lectins of beneficial symbiotic microorganisms are discussed.
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Shruthishree D. Padiyappa, Hemavathi Avalappa, Yeldur P. Venkatesh, Nagaraj Parisara, B. T. Prabhakar, and Pramod.S.N. "Characterization of antioxidant, anti-cancer, and immunomodulatory functions of partially purified garlic (Allium sativum L.) lectin." Biomedicine 42, no. 4 (September 12, 2022): 703–12. http://dx.doi.org/10.51248/.v42i4.1862.
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Introduction and Aim: The metabolic and oxidative stress induces highly reactive free radicals that are known to harm normal physiology and play a role in the development of cancer. Elevated levels of these free radicals contribute to excessive neovascularization leading to angiogenesis mediated cancer progression. Targeting these free radicals through dietary source is important strategy in regulation of cancer. Allium sativum L. (AsL) garlic has important multi pharmacological properties. On the other hand, dietary lectins are proven to be the best anti-cancer molecules. The study presents investigation that focus to assess the antioxidant, immunomodulatory and anticancer activities of partially purified garlic lectin (PPAsL). Materials and Methods: Fresh garlic bulbs were processed and evaluated for lectin induced HA activity. Further the garlic lectins (AsL) were partially purified by ammonium sulphate precipitation and dialysis and analyzed through SDS-PAGE. Further lectins were characterized by producing Anti-AsL polyclonal antibodies and purification by affinity chromatography. Pharmacological evaluations of the lectins were assessed through antioxidant, anti-proliferative and antiangiogenic mediated anti-cancer activity. Results: Lectin positive activity was confirmed by HA activity and partial purification lectin identified ?12kDa protein having Glc/Man glycan specificity. The polyclonal antibodies raised against PPAsL, confirmed that it has potent immunogen. Pharmacological evaluation confirmed that PPAsL has potent antioxidant, antiangiogenic and antiproliferative effect both in-vitro and in-vivo. Conclusion: PPAsL is potent antioxidant, anti-proliferative and anti-cancer molecule. The dietary recommendation of the garlic lectin is an important therapeutic strategy against the cancer.
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Poirier, F., and E. J. Robertson. "Normal development of mice carrying a null mutation in the gene encoding the L14 S-type lectin." Development 119, no. 4 (December 1, 1993): 1229–36. http://dx.doi.org/10.1242/dev.119.4.1229.
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The L14 lectin is a 14 × 10(3) M(r) carbohydrate binding protein belonging to the family of S-type lectins. The pattern of expression of this protein during mouse embryogenesis suggests that it may have multiple roles during pre- and post-implantation development. Using the technique of homologous recombination in embryonic stem cells, we have introduced a null mutation in the gene encoding the L14 lectin and generated a strain of mice carrying the mutant allele. We report here that homozygous mutant animals that lack the L14 lectin develop normally and are viable and fertile. The absence of any major phenotypic abnormalities in these mutant animals suggests that other protein(s) potentially compensate for the absence of the L14 lectin. Here we show that a related protein termed L30, a lectin that has carbohydrate binding specificity similar to that of L14, is present in the same embryonic cell populations as L14 at the time of implantation, suggesting that the two S-type lectins may be capable of functional substitution at this early stage of embryogenesis.
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Ravishankar, R., K. Suguna, A. Surolia, and M. Vijayan. "Structures of the complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins." Acta Crystallographica Section D Biological Crystallography 55, no. 8 (August 1, 1999): 1375–82. http://dx.doi.org/10.1107/s0907444999006587.
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The crystal structures of complexes of peanut lectin with methyl-β-galactose and N-acetyllactosamine have been determined at 2.8 and 2.7 Å, respectively. These, and the complexes involving lactose and the T-antigenic disaccharide reported previously, permit a detailed characterization of peanut-lectin–carbohydrate association and the role of water molecules therein. The water molecules in the combining site are substantially conserved in the four complexes. The role of interacting sugar hydroxyl groups, when absent, are often mimicked by ordered water molecules not only at the primary combining site, but also at the site of the second sugar ring. The similarity of peanut-lectin–sugar interactions with those in other galactose/N-acetylgalactosamine-specific lectins also extend to a substantial degree to water bridges. The comparative study provides a structural explanation for the exclusive specificity of peanut lectin for galactose at the monosaccharide level, compared with that of the other lectins for galactose as well as N-acetylgalactosamine. The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars.
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Catt, J. W., F. L. Harrison, and J. S. Carleton. "Distribution of an endogenous beta-galactoside-specific lectin during foetal and neonatal rabbit development." Journal of Cell Science 87, no. 5 (June 1, 1987): 623–33. http://dx.doi.org/10.1242/jcs.87.5.623.
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The tissue concentration of an endogenous beta-galactoside-specific lectin is developmentally regulated in rabbit tissues during foetal and neonatal development. Immunoassay data and localization studies both indicate that the lectin is particularly associated with late embryonic and early postnatal development. No lectin could be detected in embryos prior to 21 days of gestation, whereas many tissues showed an increase in lectin around the time of birth. It is likely that in most tissues the high concentrations of lectin are largely due to increased synthesis by fibroblasts, which are particularly abundant and active in connective tissue during the extensive tissue reorganization taking place at this time. The lectin appears to be synthesized by other differentiated cell types also, notably myoblasts, alveolar cells and erythroblasts. The peak of lectin concentration seen in foetal liver probably reflects lectin associated with foetal erythropoiesis. The rabbit lectin has a low specific activity but its tissue concentration is correspondingly higher than lectin concentrations in other mammals. This conservation of total lectin activity suggests a fundamental role for the lectin dependent upon its saccharide binding activity. This and other indirect evidence suggests that these lectins are involved in the synthesis, secretion or organization of extracellular matrix components.
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Cammue, B. P., B. Peeters, and W. J. Peumans. "Isolation and partial characterization of an N-acetylgalactosamine-specific lectin from winter-aconite (Eranthis hyemalis) root tubers." Biochemical Journal 227, no. 3 (May 1, 1985): 949–55. http://dx.doi.org/10.1042/bj2270949.
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A lectin was isolated from root tubers of winter aconite (Eranthis hyemalis) by affinity chromatography on fetuin-agarose, and it was partially characterized with respect to its biochemical, physicochemical and carbohydrate-binding properties. The Eranthis hyemalis lectin is a dimeric protein (Mr 62000) composed of two different subunits of Mr 30000 and 32000, held together by disulphide bonds. It is especially rich in asparagine/aspartic acid, glutamine/glutamic acid and leucine, and contains 5% covalently bound carbohydrate. Hapten inhibition assays indicated that the winter-aconite lectin is specific for N-acetylgalactosamine. In addition, the lectin exhibits a pronounced specificity towards blood-group-O erythrocytes. The winter-aconite lectin is the first lectin to be isolated from a species belonging to the plant family Ranunculaceae. It appears to be different from all previously described plant lectins.
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Lim, Anita WW, André A. Neves, Sarah Lam Shang Leen, Pierre Lao-Sirieix, Elizabeth Bird-Lieberman, Naveena Singh, Michael Sheaff, Tony Hollingworth, Kevin Brindle, and Peter Sasieni. "Lectins in Cervical Screening." Cancers 12, no. 7 (July 16, 2020): 1928. http://dx.doi.org/10.3390/cancers12071928.
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Cervical screening in low-resource settings remains an unmet need. Lectins are naturally occurring sugar-binding glycoproteins whose binding patterns change as cancer develops. Lectins discriminate between dysplasia and normal tissue in several precancerous conditions. We explored whether lectins could be developed for cervical screening via visual inspection. Discovery work comprised lectin histochemistry using a panel of candidate lectins on fixed-human cervix tissue (high-grade cervical intraepithelial neoplasia (CIN3, n = 20) or normal (n = 20)), followed by validation in a separate cohort (30 normal, 25 CIN1, 25 CIN3). Lectin binding was assessed visually according to staining intensity. To validate findings macroscopically, near-infra red fluorescence imaging was conducted on freshly-resected cervix (1 normal, 7 CIN3), incubated with topically applied fluorescently-labelled lectin. Fluorescence signal was compared for biopsies and whole specimens according to regions of interest, identified by the overlay of histopathology grids. Lectin histochemistry identified two lectins—wheat germ agglutinin (WGA) and Helix pomatia agglutinin (HPA)—with significantly decreased binding to CIN3 versus normal in both discovery and validation cohorts. Findings at the macroscopic level confirmed weaker WGA binding (lower signal intensity) in CIN3 vs. normal for biopsies (p = 0.0308) and within whole specimens (p = 0.0312). Our findings confirm proof-of-principle and indicate that WGA could potentially be developed further as a probe for high-grade cervical disease.
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Assreuy, A. M. S., M. D. Shibuya, G. J. Martins, M. L. P. De Souza, B. S. Cavada, R. A. Moreira, J. T. A. Oliveira, R. A. Ribeiro, and C. A. Flores. "Anti-inflammatory effect of glucose—mannose binding lectins isolated from Brazilian beans." Mediators of Inflammation 6, no. 3 (1997): 201–10. http://dx.doi.org/10.1080/09629359791695.
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Selectins are essential for leukocyte recruitment in inflammation. Because of a lectin domain present in the selectin structure, we investigated the anti-inflammtory activity of six mannose–glucose binding lectins from brazilian beans:Dioclea guianensis-DguiL;D. grandiflora-DgL;Cratylia floribunda-CfL;D. violacea-D.vL;D. virgata-DvirL andCanavalia brasiliensis-ConBr. The lectins were injected intravenously (i.v.) into rats (0.1 and 1.0 mg/kg; 30 min before irritants) and its activities compared toE. coliendotoxin (LPS,30 μg/kg i.v.). Three lectins (DvL, CfL and DguiL), although less intense than LPS, inhibited the neutrophil migration induced by carrageenan (Cg, 300 μg) in a dose-dependent manner (0.1 and 1.0 mg/kg). DvL activity was reversed by 0.1 M α-D-methyl-mannoside (α-CH3), but not by 0.1 M α-D-galactose. The fMLP (44 ng)-induced neutrophil migration was also reduced by these lectins. Endotoxin contamination of lectin samples could be excluded since α-CH3 treatment reversed the DvL effect, but did not modify LPS inhibitory activity. Carrageenan (300 μg)-induced paw oedema was also reduced by LPS or lectin treatments. Conversely, none of the tested lectins inhibited dextran (Dex, 300 μg)-induced paw oedema, a classical leukocyte independent model, or zymosan (Zy, 1.0 mg)-induced peritonitis and paw oedema. LPS showed no effect upon Dex-induced paw oedema and barely reduced (25%) the oedematogenic effects of zymosan. As proposed for LPS, the lectin inhibitory activity was better observed on neutrophil-mediated inflammatory reactions. We speculate that the plant lectin antiinflammatory activity is probably due to a competitive blockage of a common leukocyte and/or endothelial selectin carbohydrate ligand.