Relevant bibliographies by topics / Lectin Interactions

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Academic literature on the topic 'Lectin Interactions'

Author: Grafiati
Published: 25 June 2021
Last updated: 17 February 2022

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Journal articles on the topic "Lectin Interactions"

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Yamamoto, Kazuo. "Lectins: Structures and Lectin-Sugar Interactions." membrane 19, no. 1 (1994): 40–47. http://dx.doi.org/10.5360/membrane.19.40.

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Rhodes, Jonathan M., Barry J. Campbell, and Lu-Gang Yu. "Lectin–epithelial interactions in the human colon." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1482–86. http://dx.doi.org/10.1042/bst0361482.

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Similar changes in glycosylation occur in the colonic epithelium in inflammatory conditions such as ulcerative colitis and Crohn's disease and also in colon cancer and precancerous adenomatous polyps. They include reduced length of O-glycans, reduced sulfation, increased sialylation and increased expression of oncofetal carbohydrate antigens, such as sialyl-Tn (sialylα2-6GalNAc), and the TF antigen (Thomsen–Friedenreich antigen) Galβ1-3GalNAcα-Ser/Thr. The changes affect cell surface as well as secreted glycoproteins and mediate altered interactions between the epithelium and lectins of dietary, microbial or human origin. Different TF-binding lectins cause diverse effects on epithelial cells, reflecting subtle differences in binding specificities e.g. for sialylated TF; some of these interactions, such as with the TF-binding peanut lectin that resists digestion, may be biologically significant. Increased TF expression by cancer cells also allows interaction with the human galactose-binding lectin, galectin-3. This lectin has increased concentration in the sera of patients with metastatic cancer and binds TF on cancer cell surface MUC1 (mucin 1), causing clustering of MUC1 and revealing underlying adhesion molecules which promote adhesion to endothelium. This is likely to be an important mechanism in cancer metastasis and represents a valid therapeutic target. Tools are now available to allow fast and accurate elucidation of glycosylation changes in epithelial disease, characterization of their potential lectin ligands, whether dietary, microbial or human, and determination of the functional significance of their interactions. This should prove a very fruitful area for future research with relevance to infectious, inflammatory and cancerous diseases of the epithelia.
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Lerrer, Batia, and Nechama Gilboa-Garber. "Interactions of Pseudomonas aeruginosa PA-IIL lectin with quail egg white glycoproteins." Canadian Journal of Microbiology 47, no. 12 (December 1, 2001): 1095–100. http://dx.doi.org/10.1139/w01-124.

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Pseudomonas aeruginosa produces several lectins, including the galactophilic PA-IL and the fucose- and mannose-binding PA-IIL. The great advantage of these two lectins is their stability in purified preparations. Following observations that pigeon egg white blocks Escherichia coli P-fimbriae and PA-IL, we examined the interactions of diverse avian egg white components with PA-IIL. This lectin may represent both mannose- and fucose-specific microbial adhesins. For comparison, Con A (which also binds mannose) and Ulex europaeus lectin (UEA-I, which binds fucose) were analyzed in parallel. The lectin interactions with chicken, quail, and pigeon egg whites and several purified chicken egg white glycoproteins were examined by a hemagglutination inhibition test and Western blotting. Both analyses showed that like Con A and unlike UEA-I, which was not sensitive to any of these three egg whites, PA-IIL most strongly reacted with the quail egg white. However, in contrast with Con A, its interactions with the chicken egg white components, excluding avidin, were very poor. The results of this study might indicate the possibility that some of the egg white components that interacted with the above two mannose-binding lectins (exhibiting individual heterogeneity) might be associated with the innate immunity against mannose-specific microbial or viral adhesion during the fowl embryonic period.Key words: Pseudomonas aeruginosa, microbial lectin, PA-IIL lectin, avian egg white.
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Lis, Halina, and Nathan Sharon. "Lectin-carbohydrate interactions." Current Opinion in Structural Biology 1, no. 5 (October 1991): 741–49. http://dx.doi.org/10.1016/0959-440x(91)90173-q.

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Sharon, Nathan. "Lectin-microorganism interactions." FEBS Letters 363, no. 1-2 (April 17, 1995): 207. http://dx.doi.org/10.1016/0014-5793(95)90150-7.

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Jacobson, R. L., and R. J. Doyle. "Lectin-parasite interactions." Parasitology Today 12, no. 2 (February 1996): 55–61. http://dx.doi.org/10.1016/0169-4758(96)80655-7.

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Vilaró, Pilar, Carina Sampl, Gundula Teichert, Werner Schlemmer, Mathias Hobisch, Michael Weissl, Luis Panizzolo, Fernando Ferreira, and Stefan Spirk. "Interactions and Dissociation Constants of Galactomannan Rendered Cellulose Films with Concavalin A by SPR Spectroscopy." Polymers 12, no. 12 (December 18, 2020): 3040. http://dx.doi.org/10.3390/polym12123040.

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Interactions of biomolecules at interfaces are important for a variety of physiological processes. Among these, interactions of lectins with monosaccharides have been investigated extensively in the past, while polysaccharide-lectin interactions have scarcely been investigated. Here, we explore the adsorption of galactomannans (GM) extracted from Prosopis affinis on cellulose thin films determined by a combination of multi-parameter surface plasmon resonance spectroscopy (MP-SPR) and atomic force microscopy (AFM). The galactomannan adsorbs spontaneously on the cellulose surfaces forming monolayer type coverage (0.60 ± 0.20 mg·m−2). The interaction of a lectin, Concavalin A (ConA), with these GM rendered cellulose surfaces using MP-SPR has been investigated and the dissociation constant KD (2.1 ± 0.8 × 10−8 M) was determined in a range from 3.4 to 27.3 nM. The experiments revealed that the galactose side chains as well as the mannose reducing end of the GM are weakly interacting with the active sites of the lectins, whereas these interactions are potentially amplified by hydrophobic effects between the non-ionic GM and the lectins, thereby leading to an irreversible adsorption.
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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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Jégouzo, Sabine A. F., Conor Nelson, Thomas Hardwick, S. T. Angel Wong, Noel Kuan Kiat Lau, Gaik Kin Emily Neoh, Rocío Castellanos-Rueda, et al. "Mammalian lectin arrays for screening host–microbe interactions." Journal of Biological Chemistry 295, no. 14 (February 24, 2020): 4541–55. http://dx.doi.org/10.1074/jbc.ra120.012783.

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Many members of the C-type lectin family of glycan-binding receptors have been ascribed roles in the recognition of microorganisms and serve as key receptors in the innate immune response to pathogens. Other mammalian receptors have become targets through which pathogens enter target cells. These receptor roles have often been documented with binding studies involving individual pairs of receptors and microorganisms. To provide a systematic overview of interactions between microbes and the large complement of C-type lectins, here we developed a lectin array and suitable protocols for labeling of microbes that could be used to probe this array. The array contains C-type lectins from cow, chosen as a model organism of agricultural interest for which the relevant pathogen–receptor interactions have not been previously investigated in detail. Screening with yeast cells and various strains of both Gram-positive and -negative bacteria revealed distinct binding patterns, which in some cases could be explained by binding to lipopolysaccharides or capsular polysaccharides, but in other cases they suggested the presence of novel glycan targets on many of the microorganisms. These results are consistent with interactions previously ascribed to the receptors, but they also highlight binding to additional sugar targets that have not previously been recognized. Our findings indicate that mammalian lectin arrays represent unique discovery tools for identifying both novel ligands and new receptor functions.
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Tetala, K. Kishore R., Marcel Giesbers, Gerben M. Visser, Ernst J. R. Sudhölter, and Teris A. van Beek. "Carbohydrate Microarray on Glass: A Tool for Carbohydrate-Lectin Interactions." Natural Product Communications 2, no. 4 (April 2007): 1934578X0700200. http://dx.doi.org/10.1177/1934578x0700200408.

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A simple method to immobilize carbohydrates on a glass surface to obtain a carbohydrate microarray is described. The array was used to study carbohydrate-lectin interactions. The glass surface was modified with aldehyde terminated linker groups of various chain lengths. Coupling of carbohydrates with an amino terminated alkyl spacer to the aldehyde terminated glass followed by reductive amination resulted in carbohydrate microarrays. Fluorescently labeled (FI-TC) lectins (concanavalin A and Arachis hypogaea) were used to study specific carbohydrate-lectin interactions. contact angle, atomic force microscopy (AFM) and confocal laser fluorescence microscopy (CLFM) techniques were used in this study to monitor the modification of the glass and the successful selective binding of lectins to the carbohydrate microarray.
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Dissertations / Theses on the topic "Lectin Interactions"

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Christou, Charita. "C-type lectin-like receptors and their interactions." Thesis, University of Oxford, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.509908.

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Simpson, Jonathan Robert Henry. "SERS-based nanoparticle biodetection using carbohydrate-lectin interactions." Thesis, University of Strathclyde, 2016. http://oleg.lib.strath.ac.uk:80/R/?func=dbin-jump-full&object_id=27026.

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Endogenous biological processes including cellular recognition, motility and differentiation together with infection often result from carbohydrate-based interactions. Investigation into glycobiological interactions using sugar-coated nanoparticles are the basis for the research described herein. Metallic nanoparticles were coated with a variety of thiol-based linker molecules. Heterobifunctional PEG (carboxyl/thiol) molecules were found to be most successful in preventing non-specific aggregation. The carboxylic acid functionality of the PEG molecules used allowed for subsequent coupling of a variety of carbohydrates to the nanoparticle surface. This resulted in the production of glyconanoparticles with unique surface functionality, for example, glucose or galactose. Additionally, functionalising the particles with Raman reporter molecules (RRMs) resulted in the measurement of surface enhanced Raman scattering (SERS) signals. Aggregation of the glyconanoparticles in the presence of a variety of carbohydrate-binding proteins (lectins) was measured via changes in the extinction profile, size and the SERS response of those particles. Nanoparticle aggregation was used for the sensitive detection of plant lectins, including the Concanavalin A and Jacalin lectin and also bacterial lectins including cholera toxin B subunit (CTB). CTB was detected sensitively, selectively and rapidly by using glyconanoparticles coated in a mixture of different carbohydrates (mixed-monolayers of galactose and N-acetylneuraminic acid). Detection was possible in both buffer and synthetic freshwater conditions, demonstrating the use of these glyconanoparticles in detecting a target in complex samples. By exploiting the reversible nature of carbohydrate-lectin interactions, it was possible to use the glyconanoparticles together with the lectin ConA to develop a glucose sensor. This performed effectively across the physiological range and into the hypo/hyperglycaemic regions in buffer conditions. Finally, the glyconanoparticles were used for the detection of plant and bacterial lectins on glass substrates by initially developing a sandwich SERS assay with a view to eventually creating SERS-based carbohydrate microarrays.
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Bhatt, Veer Sandeep. "Non-lectin type Protein-carbohydrate Interactions: A Structural Perspective." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1306858684.

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Gou, Yanzi. "Synthesis of glycopolymers for the study of lectin-carbohydrate interactions." Thesis, University of Warwick, 2011. http://wrap.warwick.ac.uk/79688/.

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Saccharides act important roles in many biological processes as recognition molecules, signalling molecules and adhesion molecules. However, due to the complexity and diversity of oligosaccharides the direct synthetic approaches cannot fully meet the demands for all of the pure and well-defined oligosaccharides being studied in glycobiology. The efficient synthesis of glycomimetics, glycopolymers, offers an attractive route to solve this problem. Thus, the synthesis and application of glycopolymers of various architectures has been extensively investigated. Meanwhile, In order to explore the mechanism of the lectin-carbohydrate interactions and to get a better understanding of the structure-function relationship of oligosaccharides, the assays employed in studies of lectin-carbohydrate interactions become much more sophisticated and accurate with fast development of various analytical approaches. In this work, well-defined glycopolymers were prepared by the combination of CCTP and CuAAC click reactions. Alkyne-containing polymer scaffolds were synthesised by CCTP, followed by post-modification of the clickable polymer scaffolds with sugar azides. Moreover, a library of well-defined synthetic glycopolymers featuring the same macromolecular properties (architecture, polydispersity, valency, polarity, etc.) with difference only in the densities of different sugars (mannose, galactose and glucose) were employed to investigate the influence of different pendant epitopes on the interactions with a model lectin Con A by the traditional methods. Additionally, two powerful modem detection techniques QCM-D and SPR were also exploited to investigate the interactions of the lectin Con A, PNA, or DC-SIGN with a series of different glycopolymers. The diversities of binding properties contributed by different clustering parameters can make it possible to define the structures of the multivalent ligands and densities of binding epitopes for specific functions in the lectin-carbohydrate interactions. These conclusions can be employed as the springboard to develop new glycopolymeric drugs and therapeutic agents and to assess the mechanisms by which they work.
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Pourceau, Gwladys. "Mise au point de nouvelles méthodes de conjugaison oligonucléotide/sucre et développement d'un microsystème d'analyse des interactions lectine/sucre." Thesis, Montpellier 2, 2010. http://www.theses.fr/2010MON20224.

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Les interactions entre les sucres et les lectines sont généralement l'étape clé dans de nombreux phénomènes biologiques et pathologiques. Malgré leu r importance cruciale, ces interactions sont paradoxalement caractérisées par des constantes d'affinité faibles et nécessite une multiprésentation des motifs saccharidiques pour être significatives. Cette augmentation est appelée "effet cluster". En outre, les techniques d'analyse actuellement utilisées en laboratoire nécessitent des quantités importantes de produits, ce qui est difficilement compatible avec les méthodes de synthèse actuelle. Pour pallier ces difficultés, une approche originale basée sur l'utilisation conjointe de glycooligonucléotide et de puces à ADN a été proposée. Les glycoconjugués basés sur des squelettes phosphodiesters et couplés à des séquences d'ADN ont été synthétisés en utilisant la chimie des oligonucléotides, couplée à la "click chemistry". La séquence d'ADN quant à elle a permis l'ancrage sur une puce à ADN et donc la mesure de leur affinité vis-à-vis de différentes lectines. Ce manuscrit rapporte le développement des nouvelles méthodologies de synthèse des glycooligonucléotides ainsi que la préparation de nombreux glycoconjugués originaux, dont l'affinité pour différentes lectines a été mesurée via l'utilisation de la puce à ADN. L'influence de plusieurs paramètres a été étudiée: le nombre de résidus, l'arrangement spatial, la lipophilie etc. Il s'avère que l'arrangement spatial semble être l'un des points les plus importants dans la mise au point d'un glycoconjugué
The interactions between carbohydrates and lectins are generally the "key step" in many biological and pathological phenomena. Despite their importance, these interactions are paradoxically characterized by low affinity constants and requires multipresence of saccharide to be significant. This increase is called "cluster effect". In addition, the analysis techniques currently used in the laboratory requires large quantities of products, which is hardly compatible with the current methods of synthesis. To circumvent these difficulties, a original approach based on the combined use of glycooligonucleotides and DNA microarrays has been proposed. Glycoconjugates based on phosphodiester skeletons linked to DNA sequences have been synthesized using the chemistry of oligonucleotides, coupled with the "click chemistry". The DNA sequence has allowed the anchoring on a DNA chip and therefore the measurement of their affinity versus different lectins.This manuscript reports the development of new synthetic methodologies for the glycooligonucleotides synthesis and the preparation of many original glycoconjugates, whose affinity for various lectins was measured through the use of DNA microarray. The influence of several parameters was studied: the number of residues, the spatial arrangement, etc. lipophilicity. The spatial arrangement appears to be one of the most important parameters in the development of a glycoconjugate
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Miller, A. "Complement-carbohydrate interactions : studies of mannose binding lectin and complement factor H." Thesis, University College London (University of London), 2012. http://discovery.ucl.ac.uk/1338984/.

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The complement system is a fundamental component of innate immunity that orchestrates complex immunological and inflammatory processes. Complement comprises over 30 proteins that eliminates invading microorganisms while maintaining host cell integrity. Protein-carbohydrate interactions play critical roles in both the activation and regulation of complement. Mannose binding lectin (MBL) activates the lectin pathway of complement via the recognition of sugar arrays on pathogenic surfaces. X-ray scattering and AUC combined with constrained modelling were used to identify a bent structure for the MBL monomer in terms of crystal structures for its carbohydrate-recognition domain and its triple helical region. Near-planar solution structures were determined for the MBL dimer, trimer and tetramer. These solution structures clarified how MBL binds to pathogenic surfaces and provides a template for the binding and autoactivation of the MASP protease to initiate the lectin pathway of complement activation. Factor H (FH) with 20 short complement regulator (SCR) domains regulates the alternative pathway of complement by facilitating the breakdown of the central component C3b. FH binds to heparan sulphate (HS) and to heparin (a HS analogue) on host cell surfaces where it regulates C3b activity and protects these cells from complement attack. A Tyr402His polymorphism in SCR-7 is a major risk factor for the development of age-related macular degeneration (AMD), and is involved in heparin binding. Both the Tyr402 and His402 allotypes of the SCR-6/8 fragment of FH were cloned and expressed in an E. coli system. X-ray scattering, analytical ultracentrifugation and surface plasmon resonance were used to characterise the interactions of FH Tyr402 and His402 with heparin and HS. These polyanions induce the strong self-association of FH SCR-6/8, the extent of which was found to be dependent on the length of the polyanion and the presence of the His402 allotype. The formation of large FH-heparin aggregates may provide a molecular explanation for the link between the Tyr402His polymorphism and the initial formation of drusen deposits in AMD.
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Wing, James Badger. "The effect of mannose-binding lectin on the cellular interactions of Neisseria gonorrhoeae." Thesis, University of Sheffield, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.444921.

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Wang, Xin. "Synthesis and Characterization of Glyconanomaterials, and Their Applications in Studying Carbohydrate-Lectin Interactions." PDXScholar, 2011. https://pdxscholar.library.pdx.edu/open_access_etds/626.

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This dissertation focuses on the synthesis and characterization of glyconanomaterials, as well as their applications in studying carbohydrate-protein interactions. A new and versatile method for coupling underivatized carbohydrates to nanomaterials including gold and silica nanoparticles was developed via the photochemically induced coupling reaction of perfluorophenylazide (PFPA). A wide range of carbohydrates including mono-, oligo- and poly-saccharides were conjugated to the nanoparticles with high yields and efficiency. New analytical methods were developed to determine the binding affinities of glyconanoparticles (GNPs) with lectins; these include fluorescence-based competition assay, dynamic light scattering (DLS) and isothermal titration calorimetry (ITC). Results showed that the multivalent presentation of carbohydrate ligands significantly enhanced the binding affinity of GNPs by several orders of magnitude compared to the free ligands. Systematic studies were carried out to investigate the impact of ligand presentation, i.e., the type and length of spacer linkage, the ligand density and the nanoparticle size on the binding affinity of the resulting glyconanoparticles. We used gold GNPs to study interactions with anti-HIV lectin cyanovirin-N (CV-N), and dye-doped silica nanoparticles for labeling glyans and developing high-throughput screening technique.
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Ligeour, Caroline. "Synthèse de nouveaux glycooligonucléotides et glycoclusters : étude de leurs affinités avec les lectines I et II de Pseudomonas aeruginosa et la lectine de Burkholderia ambifaria." Thesis, Montpellier 2, 2013. http://www.theses.fr/2013MON20211/document.

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Les interactions sucre-lectine jouent un rôle très important dans de nombreux processus biologiques comme les infections par des virus ou des bactéries. Toutefois, ces interactions étant faibles, la présentation de manière multivalente des résidus saccharidiques est nécessaire pour obtenir une augmentation significative des constantes d'association. Une technique basée sur l'utilisation de glycooligonucléotides et d'une puce à ADN utilisée comme plateforme d'ancrage a permis d'étudier l'affinité d'un grand nombre de composés envers les lectines PA-IL et PA-IIL de Pseudomonas aeruginosa et la lectine BambL de Burkholderia ambifaria. Les glycooligonucléotides ont été synthétisés, à partir de blocs de construction synthétisés en aval, en utilisant la chimie des acides nucléiques supportée et automatisée (phosphoramidites et H-phosphonate) ainsi que des réactions de « click chemistry » (la cycloaddition 1,3-dipolaire catalysée par le cuivre (I) ou le couplage thiol par addition de type Michael ou par substitution nucléophile d'un dérivé bromoacetamide).Les glycoclusters ayant montrés une bonne affinité envers les lectines cibles ont été sélectionnés et resynthétisés en solution sans l'étiquette ADN à l'échelle de la centaine de milligrammes. Les glycoclusters ainsi synthétisés en deux ou trois étapes avec une seule purification ont pu être évalués par quatre techniques d'analyse des interactions (HIA, ELLA, SPR et ITC) en présence des lectines PA-IL, PA-IIL et BambL. Nous avons trouvé un tétragalactocluster et un tétrafucocluster possédant une forte affinité envers la lectine PA-IL et BambL respectivement avec des valeurs de Kd de 157 nM et 43 nM
Carbohydrate-lectin interactions play a key role in various biological processes such as infection by viruses or bacteria. As these interactions are weak, the multivalent association of carbohydrate is necessary to increase the binding constant. We used glycooligonucleotide and DNA chip to study the affinity of diverse compounds to PA-IL and PA-IIL lectins of Pseudomonas aeruginosa and Bambl lectin of Burkholderia ambifaria. Glycooligonucleotides were synthesized with previously prepared building blocks, using automated supported nucleic acid chemistry (phosphoramidites and H-phosphonate) and “Click chemistry” (copper (I) catalyzed 1,3-dipolar cycloaddition, thiol coupling by Michael addition and nucleophilic substitution of bromoacetamide derivative).Glycoclusters showing the better affinities toward the lectins have been synthesized to a hundred milligrams scale in solution without the DNA tag. The synthesis processes in two or three steps and only one final purification. Their interactions with the lectins PA-IL, PA-IIL and BambL were studied by several assays (HIA, ELLA, SPR and ITC). A tetragalactocluster and a tetrafucocluster showed high affinity toward respectively the lectin PA-IL (Kd = 157 nM) and the lectin BambL (Kd = 43 nM)
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Roussel, Francis. "Interactions cellulaires et couples lectine-sucre." Rouen, 1994. http://www.theses.fr/1994ROUE5071.

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L'expression de sucres de membrane (insolubles) par certaines cellules peut aller de pair avec l'expression de lectines endogènes (insolubles) par d'autres cellules. La complémentarité des deux réactifs solubles utilisés pour les mettre en évidence (lectines végétales, néoglycoprotéines) définit un couple lectine-sucre. L'interaction fonctionnelle ou plus banalement la complémentarité anatomique de ces deux cellules porteuses pose le problème de l'implication du couple lectine-sucre dans leur mise en place spécifique. Cette problématique a été explorée 1) au niveau de la voie sensitive douloureuse où un couple lactose et/ou galactose est impliqué. 2) Au niveau des interactions hôte parasite Trichomonas vaginalis-cellule MacCoy qui sont modulables in vitro, et donc régulables in vivo, par des inhibiteurs solubles, révélant un couple mannose/N Acétyl Glucosamine. 3) Au niveau des cellules cancéreuses qui représentent un exemple typique de désorganisation des relations intercellulaires et qui ont montré des déséquilibres dans le couple fucose. Elles ont perdu la notion d'organe en devenant aptes à former des métastases grâce aux interactions qu'elles contractent avec les cellules endothéliales qui expriment beaucoup de fucose et qui constituent leur porte d'entrée dans le reste de l'organisme. Ces anomalies des couples lectine-sucre qui atteignent au plus profond la spécificité d'organe apparaissent liées à la dissémination métastatique. Les couples lectine-sucre définiraient la notion d'organe et seraient indispensables au maintien de la cohérence de l'organisme. L'utilisation de réactifs complémentaires, lectines et néoglycoprotéines, de spécificité de plus en plus fine, de pouvoir discriminant équilibré entre eux, la détection systématique d'éventuels compétiteurs solubles, en particulier dans le domaine du fucose, devraient permettre de progresser dans l'analyse du processus métastatique qui fait la gravité du cancer
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Books on the topic "Lectin Interactions"

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Okolo, C. J. Studies on lectin binding sites of Glossina in relation to host parasite interactions with particular reference to Glossina trypanosome systems. Salford: University of Salford, 1991.

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Rosenfeld, Henning. Interaction investigations of lectins to glycoproteins and glycolipids with regard to their application in affinity separation processes. Hamburg: Helmut-Schmidt-Universität, 2005.

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Rosenfeld, Henning. Interaction investigations of lectins to glycoproteins and glycolipids with regard to their application in affinity separation processes. Hamburg: Helmut-Schmidt-Universität, 2005.

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Carbohydrate recognition: Biological problems, methods, and applications. Hoboken, N.J: Wiley, 2011.

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J, Doyle Ronald, and Slifkin Malcolm, eds. Lectin-microorganism interactions. New York: M. Dekker, 1994.

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C, Lee Y., and Lee Reiko T, eds. Recognition of carbohydrates in biological systems: Edited by Yuan C. Lee, Reiko T. Lee. San Diego, Calif: Academic Press, 2003.

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Lee, Y. C., and Reiko T. Lee. Recognition of Carbohydrates in Biological Systems, Part A : General Procedures, Volume 362 (Methods in Enzymology). Academic Press, 2003.

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Lee, Y. C., and Reiko T. Lee. Recognition of Carbohydrates in Biological Systems, Part A : General Procedures, Volume 362 (Methods in Enzymology). Academic Press, 2003.

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Book chapters on the topic "Lectin Interactions"

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Evers, David L., and Kevin G. Rice. "Mammalian Carbohydrate-Lectin Interactions." In Glycoscience: Chemistry and Chemical Biology I–III, 1779–816. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-56874-9_41.

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Evers, David L., and Kevin G. Rice. "Mammalian Carbohydrate-Lectin Interactions." In Glycoscience, 1779–816. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-11893-1_17.

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Mariethoz, Julien, Khaled Khatib, Matthew P. Campbell, Nicolle H. Packer, Elaine Mullen, and Frederique Lisacek. "SugarBindDB SugarBindDB : Resource of Pathogen Pathogen Lectin-Glycan Interactions Lectin-glycan interactions." In Glycoscience: Biology and Medicine, 275–82. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_28.

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Mandal, D. K., and C. F. Brewer. "Lectin-Glycoconjugate Cross-Linking Interactions." In Lectins and Glycobiology, 117–28. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77944-2_12.

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de Bentzmann, Sophie, Annabelle Varrot, and Anne Imberty. "Monitoring Lectin Interactions with Carbohydrates." In Methods in Molecular Biology, 403–14. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0473-0_32.

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Rudd, Pauline, Farida Fortune, Thomas Lehner, Raj Parekh, Thakor Patel, Mark Wormald, Rajneesh Malhotra, Robert Sim, and Raymond Dwek. "Lectin-Carbohydrate Interactions in Disease." In Advances in Experimental Medicine and Biology, 147–52. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1885-3_13.

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Sharon, N. "Molecular basis of lectin-carbohydrate interactions." In Lectins and Cancer, 1–12. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76739-5_1.

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Duverger, Eric, Nathalie Lamerant-Fayel, Natacha Frison, and Michel Monsigny. "Carbohydrate–Lectin Interactions Assayed by SPR." In Methods in Molecular Biology, 157–78. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-670-2_10.

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Sharon, Nathan. "Carbohydrate—Lectin Interactions in Infectious Disease." In Toward Anti-Adhesion Therapy for Microbial Diseases, 1–8. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0415-9_1.

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Brewer, C. Fred. "Lectin Cross-Linking Interactions with Multivalent Carbohydrates." In The Molecular Immunology of Complex Carbohydrates —2, 17–25. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1267-7_2.

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Conference papers on the topic "Lectin Interactions"

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Wang, Deyu, Duxiao Jiang, and Chunwei Yuan. "Spectral characters of lectin saccharide interaction." In International Symposium on Biomedical Optics, edited by Qingming Luo, Britton Chance, Lihong V. Wang, and Steven L. Jacques. SPIE, 1999. http://dx.doi.org/10.1117/12.364383.

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Lian, E. C. Y., and F. A. Siddigui. "BINDING OF 37-DKa PLATELET AGGLUTINATING PROTEIN TO HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643976.

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We have previously reported the purification of a 37-KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura. using 125I-labeled p37, the properties of its binding to platelets were studied. The binding of p37 to washed human platelets from 4 normal subjects and two TTP patients after recovery was specific, concentration dependent and saturable. The Scatchard analysis revealed that the binding sites for p37 was about 100,000 per platelet with a dissociation constant of 48 × 10−9 M. The binding of p37 to erythrocytes was very little and non-specific. Stimulation of platelets by thrombin or ADP did not have any effect on the binding of p37 to platelets. The monoclonal antibodies to platelet GP lb (6D1) and GP Ilb-llla (10E5)(A gift of Dr. Barry coller) did not inhibit the binding of p37 to platelets. Fibrinogen (1 mg/ml) and FVIII/vWF (250 ug/ml) reduced the binding slightly. The polyclonal antibodies to p37 as well as concanavalin-A inhibited the binding of p37 to platelets through their direct interaction with p37. Other lectins such as phytohemagglutinin, potato lectin and helix pomatia lectin did not have any effect. At 40 mM, sialic acid, α-D-(+)-glucose, D-(+)-mannose and D-fructose caused 91%,44%,79%, and 63% inhibition of p37 binding respectively. D-(+)-galactose did not interfere with the binding. It is concluded that p37 binds to platelets on the sites other than GP lb and Gp IIb-IIIa and its binding to platelets is inhibited by certain sugars.
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Aihara, M., S. Morimoto, Y. Sawada, A. Kimura, Y. Chiba, and Y. Yoshida. "A ROLE OF PLATELET MEMBRANE COMPONENTS IN THE INTERACTION OF PLATELET-COLLAGEN-VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644480.

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To determine a role of platelet membrane components on the interaction of platelet-collagen-von Willebrand factor(vWF), several experimental approaches were used. The adhesion of human fixed washed platelets(FWP) to collagen was decreased after the treatment with Serratia marcescens protease(100 ug/ml), but the collagen cofactor activity(COo) of vWF that enhances the adhesion of FWP to collagen was still present after the digestion. Although the platelet adhesion in the absence of normal plasma was not changed by the addition of monoclonal antibody(M-ab) against platelet membrane glycoprotein(GP) IIb/lIIa(1 0E5, BS Coller), the adhesion was decreased by 30-50% after the treatment of the platelets with 10-100 ug/ml anti-GPIb(6D1, BS Coller). The adhesion of FWP to collagen was inhibited by lectins;the adhesion was 58-75% in the presence of 100-400 ug/ml L. culinaris lectin or weat germ agglutinin and the adhesion was nil in the presence of 100 ug/ml Ricinus communis agglutinin I or 200 ug/ml concanavalin A. By the crossed aff ino-immunoelectrophoresis, the binding of GP Ilb/lIIa in Triton-solubilized platelet supernatant to the collagen spacer gel was observed. When CHAPSO solubilized platelet was applied to the collagen column and the fractions containing adhesion inhibitor were eluated by 0.3M NaCl, Mr of 240K, 220K, 21 OK, 116K, 61K, 54K, 50K and 45K proteins were identified besides the proteins which correspond to thrombospondin, GPIb, GP lib or Ilia by SDS-PAGE(7.5% gel, silver stain). GOo in normal plasma was not changed by anti-GPIIb/lIIa but was decreased to 32-38%by anti-GPIb. M-ab against vWF, CLB-RAg 35(van Mourik), that inhibits the binding of vWF to platelet by ristocetin decreased COo in normal plasma by 70% and CLB-RAg 201 (van Mourik) that inhibits the binding of vWF to collagen did completely inhibit the COo in normal plasma. In conclusion, our data suggest that (1) GPIb is partly involved in the platelet adhesion to collagen; (2) the binding of vWF to collagen is required for the expression of CCo; (3) CCo of vWF is partly mediated though GPIb; and (4) several platelet membrane protein(s) besides GPIb or GPIIb/lIIa may be also involved in both the adhesion of platelets to collagen and CCo of vWF.
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Verma, Anamika, Mitchell R. White, Kazue Takahashi, Stephan Thiel, and Kevan Hartshorn. "Interaction Of Ficolins And Mannose Binding Lectins With Seasonal And Pandemic Influenza." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2750.

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NAKAMURA, Shin, Yukio SUZUKI, Takayuki HARADA, Shigeru MORIKAWA, Shunichiro KAWABATA, and Sadaaki IWANAGA. "TISSUE FACTOR OF A HUMAN CELL LINE, RET-1: ITSPRODUCTION, PURIFICATION AND PROPERTIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643287.

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A dendritic cell-like cell line, HIN-Ret-1(RET-1), was found to produce the highest level of tissue factor (TF) among several established cell lines from human lymphoma or leukemia. The TF level expressed by this cell line exceeded 5.6 times that expressed by a monocyte-like cell line, U-937. Unlike other TF producing cell line, i.e. RET-2, HL-60, ML-3, and U-937, the TF expression by RET-1 was spontaneous and unaffected with TP A, PHA, LPS, or MAF. The TF activity of RET-1 was markedly inhibited by Con A as well as that produced by LPS-stimulated monkey monocytes, whereas the TF activity of monkey brain and lung was hardly inhibited by the lectin. Hence, the RET-1 cell lysate solubilized in Triton X-100 was subjected to affinity chromatography on a Con A-Sepharose column, and TF-apoprotein (TF-Apo) was completely bound to the column and eluted with TBS containing 0.15 M α(-methylglucoside and 0.1 % Triton X-100. Further purification of this material was performed with combination of FPLC on a DEAE-5PW column and affinity chromatography using a factor VII-Sepharose column. By these methods, TF-Apo preparation with purification-fold of 9,400 and over-all yield of 7 % was obtained. Its apparent molecular weight was estimated to be 120 kDa by gel filtration in TBS containing 0.1 % Triton X-100. SDS-PAGE gave the value of 47 kDa, which was almost compatible with that of TF-Apo from brain or placenta. TF-Apo frcm the monocytes also bound to the lectin column, suggesting that the apoprotein of these macrophage-related cells has an oligosaccharide chain interacting with the lectin. RET-1 TF-Apo was unstable under acidic condition (<pH 4.0) or in organic solvents such as isopropanol (>18 %) and acetonitrile (>8 %).
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Tanimoto, Toshiko, Yuko Kishimoto, Akiko Ikuta, Yuki Nishi, and Keishiro Miyake. "PREPARATION AND CHARACTERIZATION OF BRANCHED BETA-CYCLODEXTRINS HAVING MANNOOLIGOSACCHARIDES IN SIDE CHAINS AND STUDY OF THEIR INTERACTION WITH LECTINS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.564.

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Tandon, N. N., and G. A. Jamieson. "ROLE OF PLATELET MEMBRANE GLYCOPROTEIN IV IN PLATELET-COLLAGEN INTERACTION: A MICROTITER ASSAY TO STUDY PLATELET ADHERENCE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643906.

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The role of platelet glycoprotein IV (GPIV) in platelet function has not been elucidated. We have now isolated GPIV (Mr 88,000) from platelet membranes in homogeneous form by a series of steps involving (i) phase partitioning in Triton X-114, (ii) ion exchange chromatography on DEAE-cellulose, (iii) lectin affinity chromatography on WGA-Sepharose, and (iv) size exclusion chromatography on Ultrogel AcA44. Purified GPIV inhibited platelet shape change and aggregation induced by collagen (2 ug/ml; 7 nM as tropocollagen) in a dose-dependent fashion (ID50 ∼ 1 ug/ml; 10 nM) but did not affect aggregation induced by thrombin, ADP, epinephrine, arachidonate or ionophore A23187. To study the role of GPIV in platelet interaction with collagen we have developed a microtiter assay involving (i) coating acid soluble or fibrillar Type I collagen onto microtiter plates, (ii) incubation of coated collagen with 51Cr-labeled platelets and (iii) quantitation of platelet adherence by analysing the radioactivity of the SDS lysate of the adhered platelets. In this assay system, Fab fragments of anti-GPIV antibody inhibited platelet adherence by 75% to both acid soluble and fibrillar Type I collagen while nonimmune serum was without effect. Fab fragments also inhibited collagen-induced aggregation and secretion (ID∼ 10 ug/ml; 200 nM) and, slightly less effectively, aggregation by ADP and epinephrine (ID∼ 300 NM), but did not affect platelet activation by thrombin, arachidonate or ionophore. Fab fragments also inhibited platelet attachment to collagen-Sepharose columns by 80%. These results suggest a role for GPIV in the interaction of platelets with collagen, probably at the level of primary platelet adherence.
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Reports on the topic "Lectin Interactions"

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Wang, Xin. Synthesis and Characterization of Glyconanomaterials, and Their Applications in Studying Carbohydrate-Lectin Interactions. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.626.

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Deutscher, Susan. Radiolabeled Peptide Scaffolds for PET/SPECT - Optical in Vivo Imaging of Carbohydrate-Lectin Interactions. Office of Scientific and Technical Information (OSTI), September 2014. http://dx.doi.org/10.2172/1158790.

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