Journal articles: 'Lectin Interactions'

1

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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4

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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5

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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6

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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7

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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10

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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11

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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Shang, Kun, Siyu Song, Yaping Cheng, Lili Guo, Yuxin Pei, Xiaomeng Lv, Teodor Aastrup, and Zhichao Pei. "Fabrication of Carbohydrate Chips Based on Polydopamine for Real-Time Determination of Carbohydrate–Lectin Interactions by QCM Biosensor." Polymers 10, no. 11 (November 16, 2018): 1275. http://dx.doi.org/10.3390/polym10111275.

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A novel approach for preparing carbohydrate chips based on polydopamine (PDA) surface to study carbohydrate–lectin interactions by quartz crystal microbalance (QCM) biosensor instrument has been developed. The amino-carbohydrates were immobilized on PDA-coated quartz crystals via Schiff base reaction and/or Michael addition reaction. The resulting carbohydrate-chips were applied to QCM biosensor instrument with flow-through system for real-time detection of lectin–carbohydrate interactions. A series of plant lectins, including wheat germ agglutinin (WGA), concanavalin A (Con A), Ulex europaeus agglutinin I (UEA-I), soybean agglutinin (SBA), and peanut agglutinin (PNA), were evaluated for the binding to different kinds of carbohydrate chips. Clearly, the results show that the predicted lectin selectively binds to the carbohydrates, which demonstrates the applicability of the approach. Furthermore, the kinetics of the interactions between Con A and mannose, WGA and N-Acetylglucosamine were studied, respectively. This study provides an efficient approach to preparing carbohydrate chips based on PDA for the lectin–carbohydrate interactions study.

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13

Jørndrup, S., and K. Buchmann. "Carbohydrate localization on Gyrodactylus salaris and G. derjavini and corresponding carbohydrate binding capacity of their hosts Salmo salar and S. trutta." Journal of Helminthology 79, no. 1 (March 2005): 41–46. http://dx.doi.org/10.1079/joh2004259.

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AbstractThe congeners Gyrodactylus salaris and G. derjavini are specific ectoparasites of Atlantic salmon Salmo salar and brown trout S. trutta, respectively. To elucidate the involvement of lectin–carbohydrate interactions in this host specificity, carbohydrates on the tegument of the two species and the corresponding lectin activity of their hosts have been studied. Carbohydrate composition on the tegument differed significantly between the two gyrodactylids. Three of four commercially available peroxidase-labelled lectins with primary affinity towards D-mannoside, D-GalNAc and L-fucose bound more strongly to G. derjavini than to G. salaris. Lectins with an affinity towards D-mannoside and D-GalNAc bound significantly stronger to the cephalic lobes on G. derjavini compared to the tegument and sheaths of the hamuli. One brown trout strain and three different salmon strains were tested for lectin activity in skin and plasma. Two Baltic salmon strains and one strain from the Atlantic region were included. Brown trout differed significantly from the salmon strains when skin samples were tested for D-GalNAc activity. Lectins binding to other carbohydrates showed trends for similar host differences. The implications of carbohydrate–lectin interactions for host specificity in gyrodactylids are discussed.

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14

Lee, W., A. M. C. De La Barca, D. Drake, and R. J. Doyle. "Lectin-Oral Streptococci Interactions." Journal of Medical Microbiology 47, no. 1 (January 1, 1998): 29–37. http://dx.doi.org/10.1099/00222615-47-1-29.

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15

Touhami, Ahmed, Barbara Hoffmann, Andrea Vasella, Frédéric A. Denis, and Yves F. Dufrêne. "Aggregation of yeast cells: direct measurement of discrete lectin–carbohydrate interactions." Microbiology 149, no. 10 (October 1, 2003): 2873–78. http://dx.doi.org/10.1099/mic.0.26431-0.

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Aggregation of microbial cells mediated by specific interactions plays a pivotal role in the natural environment, in medicine and in biotechnological processes. Here we used atomic force microscopy (AFM) to measure individual lectin–carbohydrate interactions involved in the flocculation of yeast cells, an aggregation event of crucial importance in fermentation technology. AFM probes functionalized with oligoglucose carbohydrates were used to record force-distance curves on living yeast cells at a rate of 0·5 μm s−1. Flocculating cells showed adhesion forces of 121±53 pN, reflecting the specific interaction between individual cell-surface lectins and glucose residues. Similar adhesion forces, 117±41 pN, were measured using probes functionalized with the lectin concanavalin A and attributed to specific binding to cell-surface mannose residues. By contrast, specific interaction forces were not observed in non-flocculating conditions, i.e. in the presence of mannose or when using non-flocculating cells, pointing to their involvement in yeast flocculation. The single molecule force spectroscopy measurements presented here provide a means to study a variety of cellular interactions at the molecular level, such as the adhesion of bacteria to animal and plant tissues.

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Sivaji, Nukathoti, Nikitha Harish, Samsher Singh, Amit Singh, Mamannamana Vijayan, and Avadhesha Surolia. "Mevo lectin specificity toward high-mannose structures with terminal αMan(1,2)αMan residues and its implication to inhibition of the entry of Mycobacterium tuberculosis into macrophages." Glycobiology 31, no. 8 (April 1, 2021): 1046–59. http://dx.doi.org/10.1093/glycob/cwab022.

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Abstract Mannose-binding lectins can specifically recognize and bind complex glycan structures on pathogens and have potential as antiviral and antibacterial agents. We previously reported the structure of a lectin from an archaeal species, Mevo lectin, which has specificity toward terminal α1,2 linked manno-oligosaccharides. Mycobacterium tuberculosis expresses mannosylated structures including lipoarabinomannan (ManLAM) on its surface and exploits C-type lectins to gain entry into the host cells. ManLAM structure has mannose capping with terminal αMan(1,2)αMan residues and is important for recognition by innate immune cells. Here, we aim to address the specificity of Mevo lectin toward high-mannose type glycans with terminal αMan(1,2)αMan residues and its effect on M. tuberculosis internalization by macrophages. Isothermal titration calorimetry studies demonstrated that Mevo lectin shows preferential binding toward manno-oligosaccharides with terminal αMan(1,2)αMan structures and showed a strong affinity for ManLAM, whereas it binds weakly to Mycobacterium smegmatis lipoarabinomannan, which displays relatively fewer and shorter mannosyl caps. Crystal structure of Mevo lectin complexed with a Man7D1 revealed the multivalent cross-linking interaction, which explains avidity-based high-affinity for these ligands when compared to previously studied manno-oligosaccharides lacking the specific termini. Functional studies suggest that M. tuberculosis internalization by the macrophage was impaired by binding of Mevo lectin to ManLAM present on the surface of M. tuberculosis. Selectivity shown by Mevo lectin toward glycans with terminal αMan(1,2)αMan structures, and its ability to compromise the internalization of M. tuberculosis in vitro, underscore the potential utility of Mevo lectin as a research tool to study host-pathogen interactions.

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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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18

Kilpatrick, David C. "Lectin–glycoconjugate interactions in health and disease." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1453–56. http://dx.doi.org/10.1042/bst0361453.

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It is increasingly being acknowledged that complex carbohydrates mediate a huge variety of cellular interactions, permitting and regulating recognition and signalling events. This is achieved by the enormous range and complexity of branched structures in glycoconjugates and the ability of carbohydrate-binding proteins (lectins) to decipher this ‘glycocode’. Approx. 120 participants attended the 23rd International Lectin Meeting (Interlec-23) held at the Universities of Edinburgh (2 days) and Stirling (4 days) between 11 and 16 July 2008. These ‘Interlecs’ are truly international multi-disciplinary symposia, providing opportunities for scientists from different backgrounds, but with a common interest in some aspect of protein–carbohydrate interactions, to present their work in an informal and stimulating atmosphere. A major aim is always to induce cross-fertilization of ideas and concepts, and Interlec-23 was intended to have some bias towards lectins (galectins, collectins, selectins, siglecs etc.) and their ligands in human health and disease. Delegates from over 30 countries attended this meeting which was divided into seven oral sessions opened by a keynote speaker. This issue of Biochemical Society Transactions contains papers based on the keynote lectures and is therefore representative of the main themes of Interlec-23.

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19

Otten, L., and M. I. Gibson. "Discrimination between lectins with similar specificities by ratiometric profiling of binding to glycosylated surfaces; a chemical ‘tongue’ approach." RSC Advances 5, no. 66 (2015): 53911–14. http://dx.doi.org/10.1039/c5ra08857g.

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Glycan–lectin interactions drive infectious processes, but are characterized by relatively low specificity, especially for monosaccharides. Here we use multiplexed biosensing to discriminate between lectins (including cholera toxin).

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20

Karpova, I. S. "SPECIFIC INTERACTIONS BETWEEN LECTINS AND RED BLOOD CELLS OF CHORNOBYL CLEANUP WORKERS AS INDICATOR OF SOME LATE RADIATION EFFECTS." Experimental Oncology 38, no. 4 (December 22, 2016): 261–66. http://dx.doi.org/10.31768/2312-8852.2016.38(4):261-266.

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Aim: Growing interest in lectins is based on their diagnostic and pharmacological potential, especially the ability to inhibit proliferation and initiate apoptosis of cancer cells. In our research microplate lectinoassay able to detect carbohydrate containing structures (receptors) on erythrocyte surface have been proposed for Chornobyl cleanup workers (1986) monitoring. It was expected to reveal specific abnormalities associated with pathological condition arising as a result of late radiation effects. Materials and Methods: Red blood cell (RBC) specimens were taken from 171 persons distributed into the six cohorts: nonexposed donors (1); chronically exposed to the doses below (2) and over 50 cGy (3); exposed to acute radiation without (4) and with manifestation of acute radiation syndrome (5 and 6). Lectins from 24 species of medicinal plants were purified by ethanol fractionation and electrofocusing. Intensity of lectin-receptor interactions was determined in reaction of hemagglutination. Method of flow cytofluorometry was used to study B-cell counts. Hormone levels in blood serum were determined by radioimmunoassay. Results: An elevated ability of RBC to interact with the panel of lectins was found in all cohorts of exposed persons versus nonexposed donors, moreover, changes in the intensity of lectin-receptor binding depended on the dose of irradiation. Diagnostic value of specific RBC reactions with some individual lectins has been elucidated. Elevated intensity of RBC reaction with Zea mays lectin was accompanied by a decrease in serum content of thyroid hormones T4 and T3, as well as reduction of B-cell counts. In the case of Rubus caesius lectin the more intensive reaction with RBC, the higher level of hormone cortisol was observed. Conclusions: Deviations from donor’s norm in intensity of lectin — RBC interactions in radiation exposed men are supposed to carry information about negative changes in their health status following Chornobyl catastrophe and show the diagnostic potential. The most sensitive reactions have been associated primarily with shifts in endocrine and immune systems. This article is a part of a Special Issue entitled “The Chornobyl Nuclear Accident: Thirty Years After”.

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

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

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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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23

Drickamer, Kurt. "Multiplicity of lectin-carbohydrate interactions." Nature Structural & Molecular Biology 2, no. 6 (June 1995): 437–39. http://dx.doi.org/10.1038/nsb0695-437.

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Gupta, Dipti, Tarun K. Dam, Stefan Oscarson, and C. Fred Brewer. "Thermodynamics of Lectin-Carbohydrate Interactions." Journal of Biological Chemistry 272, no. 10 (March 7, 1997): 6388–92. http://dx.doi.org/10.1074/jbc.272.10.6388.

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Kéry, V. "Lectin-carbohydrate interactions in immunoregulation." International Journal of Biochemistry 23, no. 7-8 (January 1991): 631–40. http://dx.doi.org/10.1016/0020-711x(91)90031-h.

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SCHWARZ, Frederick P., Sandra MISQUITH, and Avadhesha SUROLIA. "Effect of substituent on the thermodynamics of d-glucopyranoside binding to concanavalin A, pea (Pisum sativum) lectin and lentil (Lens culinaris) lectin." Biochemical Journal 316, no. 1 (May 15, 1996): 123–29. http://dx.doi.org/10.1042/bj3160123.

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Titration calorimetry measurements of the binding of phenyl-α (αPhOGlu), 3-methoxy (3MeOGlu), fluorodeoxy and deoxy derivatives of α-D-glucopyranose (Glu) to concanavalin A (conA), pea lectin and lentil lectin were performed at approx. 10 and 25 °C in 0.01 M dimethylglutaric acid/NaOH buffer, pH 6.9, containing 0.15 M NaCl and Mn2+ and Ca2+ ions. Apparently the 3-deoxy, 4-deoxy and 6-deoxy as well as the 4-fluorodeoxy and 6-fluorodeoxy derivatives of Glu do not bind to the lectins because no heat release was observed on the addition of aliquots of solutions of these derivatives to the lectin solutions. The binding enthalpies, ∆H0b, and entropies, ∆S0b, determined from the measurements were compared with the same thermodynamic binding parameters for Glu, D-mannopyranoside and methyl-α-D-glucopyranoside (αMeOGlu). The binding reactions are enthalpically driven with little change in the heat capacity on binding, and exhibit enthalpy–entropy compensation. Differences between the thermodynamic binding parameters can be rationalized in terms of the interactions apparent in the known crystal structures of the methyl-α-D-mannopyranoside-conA [Derewenda, Yariv, Helliwell, Kalb (Gilboa), Dodson, Papiz, Wan and Campbell (1989) EMBO J. 8, 2189–2193] and pea lectin-trimannopyranoside [Rini, Hardman, Einspahr, Suddath and Carber (1993) J. Biol. Chem. 268, 10126–10132] complexes. Increases in the entropy change on binding are observed for αMeOGlu binding to pea and lentil lectin, for αPhOGlu binding to conA and pea lectin, and for 3MeOGlu binding to pea lectin relative to the entropy change for Glu binding, and imply that the phenoxy and methoxy substituents provide additional hydrophobic interactions in the complex. Increases in the binding enthalpy relative to that of Glu are observed for deoxy and fluoro derivatives in the C-1 and C-2 positions and imply that these substituents weaken the interaction with the surrounding water, thereby strengthening the interaction with the binding site.

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Lin, Borong, Xue Qing, Jinling Liao, and Kan Zhuo. "Role of Protein Glycosylation in Host-Pathogen Interaction." Cells 9, no. 4 (April 20, 2020): 1022. http://dx.doi.org/10.3390/cells9041022.

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Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate protein conformation, activity, and stability, etc. This review summarizes various roles of different glycoproteins during the interaction, which include: host glycoproteins prevent pathogens as barriers; pathogen glycoproteins promote pathogens to attack host proteins as weapons; pathogens glycosylate proteins of the host to enhance virulence; and hosts sense pathogen glycoproteins to induce resistance. In addition, this review also intends to summarize the roles of lectin (a class of protein entangled with glycoprotein) in host-pathogen interactions, including bacterial adhesins, viral lectins or host lectins. Although these studies show the importance of protein glycosylation in host-pathogen interaction, much remains to be discovered about the interaction mechanism.

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Sung, L. A., E. A. Kabat, and S. Chien. "Interaction energies in lectin-induced erythrocyte aggregation." Journal of Cell Biology 101, no. 2 (August 1, 1985): 652–59. http://dx.doi.org/10.1083/jcb.101.2.652.

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Two N-acetylgalactosamine-reactive lectins, Helix pomatia (HPA) and Dolichos biflorus (DBA), were used to study the energies involved in cell-cell interactions through the specific binding of these lectins to their membrane receptors on genotype AO human erythrocytes (red blood cells) (RBCs). The energy required to dissociate a unit of aggregated membrane area (gamma d) of two RBCs bridged by lectin molecules was determined from the shear force needed to dissociate two-cell aggregates in a flow channel. When HPA were used as bridging molecules, gamma d (0.4 X 10(-4) to 3.8 X 10(-4) dyn/cm) was proportional to the density (D = 175 to 1,060 molecules/micron 2) of HPA molecules bound on the RBC membrane. A similar gamma d/D ratio was also obtained for DBA. These results indicate that the number of lectin molecules bound on the interface plays an important role in determining the energy required for cell-cell dissociation. The aggregation energy per unit membrane area (gamma a) in lectin-induced aggregates was calculated from the degree of encapsulation of a lectin-bound, heat-sphered human RBC by a normal discoid RBC. A minimum of approximately 1,800 HPA molecules/micron 2 on the spheres was required to form stable aggregates with the RBC. By using spheres having a surface HPA density of 1,830 to 2,540 molecules/micron 2, or 1.1-1.5 X 10(12) combining sites/cm2, the gamma a value for HPA-induced aggregation was found to be 2.2 X 10(-3) dyn/cm. This higher value of gamma a than gamma d has been explained on the basis of several differences in aggregation and disaggregation processes. The gamma a value for DBA-induced aggregation was not obtainable by the sphere encapsulation method because of the relative low D values. A comparison of the present results with the published value of the free energy change of 5 kcal/mol for the interactions of HPA and DBA with their ligands suggests that only a small fraction of the lectin molecules bound to RBC surface participate in the bridging of adjacent cells.

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Tiemeyer, M., and C. S. Goodman. "Gliolectin is a novel carbohydrate-binding protein expressed by a subset of glia in the embryonic Drosophila nervous system." Development 122, no. 3 (March 1, 1996): 925–36. http://dx.doi.org/10.1242/dev.122.3.925.

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Interactions between embryonic neural cells generate the specific patterns of connectivity observed in nervous systems. Cell surface carbohydrates have been proposed to function in cellular recognition events guiding such interactions. Carbohydrate-binding proteins (lectins) that recognize specific oligosaccharide ligands in embryonic neural tissue provide a molecular mechanism for carbohydrate-mediated cell-cell interactions in neural development. Therefore, we have screened an embryonic Drosophila melanogaster cDNA library, expressed in COS1 cells, for carbohydrate-binding activity. COS1 cells expressing putative Drosophila lectins were identified and recovered based on their adhesion to immobilized preparations of neutral and zwitterionic glycolipids extracted from Drosophila embryos. We have identified an endogenous lectin expressed during Drosophila embryogenesis. The cloned lectin, designated ‘gliolectin’, possesses a novel protein sequence with a calculated molecular mass of 24,993. When expressed in Drosophila S2 cells, the lectin mediates heterophilic cellular aggregation. In embryos, gliolectin is expressed by a subset of glial cells found at the midline of the developing nervous system. Expression is highest during the formation of the Drosophila embryonic axonal commissures, a process requiring midline glial cell funcion. Immunoprecipitation with a monoclonal antibody against gliolectin yields a protein of Mr=46,600 from Drosophila embryonic membranes, suggesting that post-translational modification of gliolectin is extensive. Epitope- tagged chimericproteins composed of the amino terminal one-half of gliolectin and the Fc region of human IgG bind a small subset of the total glycolipids extracted from Drosophila embryos, demonstrating that the lectin activity of gliolectin can discriminate between oligosaccharide structures. The presence of gliolectin in the developing Drosophila embryonic nervous system further supports a role for cell surface carbohydrates in cell-cell recognition and indicates that the molecular diversity of animal lectins is not yet completely defined.

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dos Santos, Marinalva Cardoso, Thais Kroetz, Cristiana Lima Dora, Fernando Carlos Giacomelli, Tiago Elias Allievi Frizon, Claus Tröger Pich, Luciano da Silva Pinto, et al. "Elucidating Bauhinia variegata lectin/phosphatidylcholine interactions in lectin-containing liposomes." Journal of Colloid and Interface Science 519 (June 2018): 232–41. http://dx.doi.org/10.1016/j.jcis.2018.02.028.

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Chen, Yanan, Harindra Vedala, Gregg P. Kotchey, Aymeric Audfray, Samy Cecioni, Anne Imberty, Sébastien Vidal, and Alexander Star. "Detection of Lectins using Glyco-Functionalized Nanosensors." MRS Proceedings 1451 (2012): 191–96. http://dx.doi.org/10.1557/opl.2012.1291.

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ABSTRACTWe have used single-walled carbon nanotube field-effect transistor (SWNT-FET) and chemically converted graphene field-effect transistor (CCG-FET) devices to probe the interactions between carbohydrates and their recognition lectins. Porphyrin- and pyrene-based glycoconjugates were used as receptor molecules and the target lectins were two bacterial lectins that present different carbohydrate preference, namely PA-IL, PA-IIL from Pseudomonas aeruginosa and a plant lectin Concanavalin A. The specific binding between lectin and carbohydrate can be transduced to the change in FET device conductance. An initial study with SWNT-FET noncovalently functionalized with porphyrin-based glycoconjugates showed both good selectivity and sensitivity. To compare SWNT and CCG performance, pyrene- and porphyrin-based glycoconjugates were functionalized noncovalently on the surface of CCG-FET and SWNT-FET devices, which were then treated with non-specific and specific lectins. The responses were compared and rationalized using computer-aided models of carbon nanostructure/glycoconjugate interactions. Fluorescence microscopy, atomic force microscopy, UV-vis-NIR spectroscopy and Isothermal titration microcalorimetry (ITC) measurements were used to confirm the electrical results.

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Jayaprakash, Nisha Grandhi, Amrita Singh, Rahul Vivek, Shivender Yadav, Sanmoy Pathak, Jay Trivedi, Narayanaswamy Jayaraman, Dipankar Nandi, Debashis Mitra, and Avadhesha Surolia. "The barley lectin, horcolin, binds high-mannose glycans in a multivalent fashion, enabling high-affinity, specific inhibition of cellular HIV infection." Journal of Biological Chemistry 295, no. 34 (July 7, 2020): 12111–29. http://dx.doi.org/10.1074/jbc.ra120.013100.

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N-Linked glycans are critical to the infection cycle of HIV, and most neutralizing antibodies target the high-mannose glycans found on the surface envelope glycoprotein-120 (gp120). Carbohydrate-binding proteins, particularly mannose-binding lectins, have also been shown to bind these glycans. Despite their therapeutic potency, their ability to cause lymphocyte proliferation limits their application. In this study, we report one such lectin named horcolin (Hordeum vulgare lectin), seen to lack mitogenicity owing to the divergence in the residues at its carbohydrate-binding sites, which makes it a promising candidate for exploration as an anti-HIV agent. Extensive isothermal titration calorimetry experiments reveal that the lectin was sensitive to the length and branching of mannooligosaccharides and thereby the total valency. Modeling and simulation studies demonstrate two distinct modes of binding, a monovalent binding to shorter saccharides and a bivalent mode for higher glycans, involving simultaneous interactions of multiple glycan arms with the primary carbohydrate-binding sites. This multivalent mode of binding was further strengthened by interactions of core mannosyl residues with a secondary conserved site on the protein, leading to an exponential increase in affinity. Finally, we confirmed the interaction of horcolin with recombinant gp120 and gp140 with high affinity and inhibition of HIV infection at nanomolar concentrations without mitogenicity.

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Cagnoni, Alejandro J., Emiliano D. Primo, Sebastián Klinke, María E. Cano, Walter Giordano, Karina V. Mariño, José Kovensky, Fernando A. Goldbaum, María Laura Uhrig, and Lisandro H. Otero. "Crystal structures of peanut lectin in the presence of synthetic β-N- and β-S-galactosides disclose evidence for the recognition of different glycomimetic ligands." Acta Crystallographica Section D Structural Biology 76, no. 11 (October 13, 2020): 1080–91. http://dx.doi.org/10.1107/s2059798320012371.

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Carbohydrate–lectin interactions are involved in important cellular recognition processes, including viral and bacterial infections, inflammation and tumor metastasis. Hence, structural studies of lectin–synthetic glycan complexes are essential for understanding lectin-recognition processes and for the further design of promising chemotherapeutics that interfere with sugar–lectin interactions. Plant lectins are excellent models for the study of the molecular-recognition process. Among them, peanut lectin (PNA) is highly relevant in the field of glycobiology because of its specificity for β-galactosides, showing high affinity towards the Thomsen–Friedenreich antigen, a well known tumor-associated carbohydrate antigen. Given this specificity, PNA is one of the most frequently used molecular probes for the recognition of tumor cell-surface O-glycans. Thus, it has been extensively used in glycobiology for inhibition studies with a variety of β-galactoside and β-lactoside ligands. Here, crystal structures of PNA are reported in complex with six novel synthetic hydrolytically stable β-N- and β-S-galactosides. These complexes disclosed key molecular-binding interactions of the different sugars with PNA at the atomic level, revealing the roles of specific water molecules in protein–ligand recognition. Furthermore, binding-affinity studies by isothermal titration calorimetry showed dissociation-constant values in the micromolar range, as well as a positive multivalency effect in terms of affinity in the case of the divalent compounds. Taken together, this work provides a qualitative structural rationale for the upcoming synthesis of optimized glycoclusters designed for the study of lectin-mediated biological processes. The understanding of the recognition of β-N- and β-S-galactosides by PNA represents a benchmark in protein–carbohydrate interactions since they are novel synthetic ligands that do not belong to the family of O-linked glycosides.

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

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Marine bioresources produce a great variety of specific and potent bioactive molecules including natural organic compounds such as fatty acids, polysaccharides, polyether, peptides, proteins, and enzymes. Lectins are also one of the promising candidates for useful therapeutic agents because they can recognize the specific carbohydrate structures such as proteoglycans, glycoproteins, and glycolipids, resulting in the regulation of various cells via glycoconjugates and their physiological and pathological phenomenon through the host-pathogen interactions and cell-cell communications. Here, we review the multiple lectins from marine resources including fishes and sea invertebrate in terms of their structure-activity relationships and molecular evolution. Especially, we focus on the unique structural properties and molecular evolution of C-type lectins, galectin, F-type lectin, and rhamnose-binding lectin families.

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Sung, L. A., E. A. Kabat, and S. Chien. "Interaction of lectins with membrane receptors on erythrocyte surfaces." Journal of Cell Biology 101, no. 2 (August 1, 1985): 646–51. http://dx.doi.org/10.1083/jcb.101.2.646.

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The interactions of human genotype AO erythrocytes (red blood cells) (RBCs) with N-acetylgalactosamine-reactive lectins isolated from Helix pomatia (HPA) and from Dolichos biflorus (DBA) were studied. Binding curves obtained with the use of tritium-labeled lectins showed that the maximal numbers of lectin molecules capable of binding to human genotype AO RBCs were 3.8 X 10(5) and 2.7 X 10(5) molecules/RBC for HPA and DBA, respectively. The binding of one type of lectin may influence the binding of another type. HPA was found to inhibit the binding of DBA, but not vice versa. The binding of HPA was weakly inhibited by a beta-D-galactose-reactive lectin isolated from Ricinus communis (designated RCA1). Limulus polyphemus lectin (LPA), with specificity for N-acetylneuraminic acid, did not influence the binding of HPA but enhanced the binding of DBA. About 80% of LPA receptors (N-acetylneuraminic acid) were removed from RBC surfaces by neuraminidase treatment. Neuraminidase treatment of RBCs resulted in increases of binding of both HPA and DBA, but through different mechanisms. An equal number (7.6 X 10(5) of new HPA sites were generated on genotypes AO and OO RBCs by neuraminidase treatment, and these new sites accounted for the enhancement (AO cells) and appearance (OO cells) of hemagglutinability by HPA. Neuraminidase treatment did not generate new DBA sites, but increased the DBA affinity for the existing receptors; as a result, genotype AO cells increased their hemagglutinability by DBA, while OO cells remained unagglutinable. The use of RBCs of different genotypes in binding assays with 3H-labeled lectins of known specificities provides an experimental system for studying cell-cell recognition and association.

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Baricevic, Ivona, Ljiljana Vicovac-Panic, Vesna Marinovic, and Margita Cuperlovic. "Investigations of asialoglycoprotein receptor glycosylation by lectin affinity methods." Journal of the Serbian Chemical Society 67, no. 5 (2002): 331–38. http://dx.doi.org/10.2298/jsc0205331b.

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The asialoglycoprotein receptor belongs to the family of calcium-dependent (C-type) animal lectins. The purified receptor is a glycoprotein in which 10 % of the dry weight consists of sialic acid, galactose, N-acetylglucosamine and mannose. The carbohydrate content of the asialoglycoprotein receptor was investigated by lectin affinity methods. The usefulness of plant lectin affinity methods in the characterization of the saccharide content of the asialoglycoprotein receptor, as an animal lectin, is demonstrated. RCA I ConA, PHA, SNA I and WGA showed greater affinity toward the asialoglycoprotein receptor, while PSL, AAA and PNA showed negligible interactions with the asialoglycoprotein receptor. The obtained results correlated well with the carbohydrate content of the asialoglycoprotein receptor as determined by chemical methods.

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Francis, Frederic, Julian Chen, Liu Yong, and Emilie Bosquee. "Aphid Feeding on Plant Lectins Falling Virus Transmission Rates: A Multicase Study." Journal of Economic Entomology 113, no. 4 (June 9, 2020): 1635–39. http://dx.doi.org/10.1093/jee/toaa104.

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Abstract Aphids are insect vectors that have piercing–sucking mouthparts supporting diversified patterns of virus–vector interactions. Aphids primarily retain circulative viruses in the midgut/hindgut, whereas noncirculative viruses tend to be retained in the stylet. Most viruses, and many proteins from animals, have carbohydrate or carbohydrate-binding sites. Lectins vary in their specificity, of which some are able to bind to viral glycoproteins. To assess the potential competition between lectins and viral particles in virus transmission by aphids, this study examined how feeding plant lectins to aphids affects the transmission efficiency of viruses. Sitobion avenae (F, 1794) (Homoptera: Aphididae) aphids fed with Pisum sativum lectin (PSL) transmitted Barley yellow dwarf virus with significantly lower efficiency (four-fold ratio). Pea enation mosaic virus was significantly reduced in Acyrthosiphon pisum Harris (Homoptera: Aphididae) aphids fed with the lectin Concanavalin A. In comparison, the transmission of Potato virus Y was significantly reduced when Myzus persicae Sultzer (Homoptera: Aphididae) aphids were fed with PSL. Thus, lectin could be used as a blocking agent of plant viruses, facilitating an alternative approach for crop protection.

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

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

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Prado Acosta, Mariano, and Bernd Lepenies. "Bacterial glycans and their interactions with lectins in the innate immune system." Biochemical Society Transactions 47, no. 6 (November 14, 2019): 1569–79. http://dx.doi.org/10.1042/bst20170410.

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Bacterial surfaces are rich in glycoconjugates that are mainly present in their outer layers and are of great importance for their interaction with the host innate immune system. The innate immune system is the first barrier against infection and recognizes pathogens via conserved pattern recognition receptors (PRRs). Lectins expressed by innate immune cells represent an important class of PRRs characterized by their ability to recognize carbohydrates. Among lectins in innate immunity, there are three major classes including the galectins, siglecs, and C-type lectin receptors. These lectins may contribute to initial recognition of bacterial glycans, thus providing an early defence mechanism against bacterial infections, but they may also be exploited by bacteria to escape immune responses. In this review, we will first exemplify bacterial glycosylation systems; we will then describe modes of recognition of bacterial glycans by lectins in innate immunity and, finally, we will briefly highlight how bacteria have found ways to exploit these interactions to evade immune recognition.

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Monsigny, Michel, Roger Mayer, and Annie-Claude Roche. "ChemInform Abstract: Sugar-Lectin Interactions: Sugar Clusters, Lectin Multivalency and Avidity." ChemInform 32, no. 6 (February 6, 2001): no. http://dx.doi.org/10.1002/chin.200106266.

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Antonik, Paweł M., Ahmed M. Eissa, Adam R. Round, Neil R. Cameron, and Peter B. Crowley. "Noncovalent PEGylation via Lectin–Glycopolymer Interactions." Biomacromolecules 17, no. 8 (July 19, 2016): 2719–25. http://dx.doi.org/10.1021/acs.biomac.6b00766.

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Kirkeby, Svend, and Dennis Moe. "Lectin interactions with α-galactosylated xenoantigens." Xenotransplantation 9, no. 4 (June 7, 2002): 260–67. http://dx.doi.org/10.1034/j.1399-3089.2002.01078.x.

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Suzuki, Yoshio. "Development of Lectin Modified Fluorescent Magnetic Particles for Highly Sensitive Detection of Glycoconjugates." Sensors 21, no. 16 (August 17, 2021): 5512. http://dx.doi.org/10.3390/s21165512.

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I conducted this study to develop an improved method for glycome detection using fluorescent magnetic beads, whose surfaces were modified using lectins, for the highly sensitive detection of saccharides or glycoproteins via fluorescence quenching using a novel fluorescence emitter and quencher pair. The emitter (Cy3 fluorophore) was incorporated into magnetic beads, and a fluorescence quencher (cyanopyranyl group) was bound to glycomes via covalent bonding. The fluorescence intensities of fluorescent magnetic beads containing lectins decreased specifically in the presence of glycomes, which was a result of fluorescence quenching from Cy3 to cyanopyranyl groups due to the formation of a stable complex between lectins and glycome. Fluorescence intensities were plotted as a function of glycoprotein concentration, and good linear relationships were observed. This method enabled the fluorescent reading-out of a series of lectin-glycome interactions on the basis of recognition selectivity and affinity of immobilized lectins without tedious washing processes. Moreover, a simple profiling process was performed using this assay for diverse glycoconjugates, which not only included simple saccharides but also glycoproteins and glycome in cell lysates. These results clearly indicate that the combination of magnetic beads with the novel emitter-quencher pair enabled the highly sensitive detection of lectin-glycome interactions.

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Raposo, Cláudia D., André B. Canelas, and M. Teresa Barros. "Human Lectins, Their Carbohydrate Affinities and Where to Find Them." Biomolecules 11, no. 2 (January 29, 2021): 188. http://dx.doi.org/10.3390/biom11020188.

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Lectins are a class of proteins responsible for several biological roles such as cell-cell interactions, signaling pathways, and several innate immune responses against pathogens. Since lectins are able to bind to carbohydrates, they can be a viable target for targeted drug delivery systems. In fact, several lectins were approved by Food and Drug Administration for that purpose. Information about specific carbohydrate recognition by lectin receptors was gathered herein, plus the specific organs where those lectins can be found within the human body.

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Tang, Jo Sing Julia, Sophia Rosencrantz, Lucas Tepper, Sany Chea, Stefanie Klöpzig, Anne Krüger-Genge, Joachim Storsberg, and Ruben R. Rosencrantz. "Functional Glyco-Nanogels for Multivalent Interaction with Lectins." Molecules 24, no. 10 (May 15, 2019): 1865. http://dx.doi.org/10.3390/molecules24101865.

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Interactions between glycans and proteins have tremendous impact in biomolecular interactions. They are important for cell–cell interactions, proliferation and much more. Here, we emphasize the glycan-mediated interactions between pathogens and host cells. Pseudomonas aeruginosa, responsible for a huge number of nosocomial infections, is especially the focus when it comes to glycan-derivatives as pathoblockers. We present a microwave assisted protecting group free synthesis of glycomonomers based on lactose, melibiose and fucose. The monomers were polymerized in a precipitation polymerization in the presence of NiPAm to form crosslinked glyco-nanogels. The influence of reaction parameters like crosslinker type or stabilizer amount was investigated. The gels were characterized in lectin binding studies using model lectins and showed size and composition-dependent inhibition of lectin binding. Due to multivalent presentation of glycans in the gel, the inhibition was clearly stronger than with unmodified saccharides, which was compared after determination of the glycan loading. First studies with Pseudomonas aeruginosa revealed a surprising influence on the secretion of virulence factors. Functional glycogels may be in the future potent alternatives or adjuvants for antibiotic treatment of infections based on glycan interactions between host and pathogen.

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Delbaere, Louis T. J., Margaret Vandonselaar, Lata Prasad, J. Wilson Quail, Joyce R. Pearlstone, Michael R. Carpenter, Lawrence B. Smillie, Pandurang V. Nikrad, Ulrike Spohr, and Raymond U. Lemieux. "Molecular recognition of a human blood group determinant by a plant lectin." Canadian Journal of Chemistry 68, no. 7 (July 1, 1990): 1116–21. http://dx.doi.org/10.1139/v90-172.

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The lectin IV of Griffoniasimplicifolia (GS4) specifically binds the terminal tetrasaccharide unit of the Lewis b human blood group determinant (Leb). The single crystal X-ray analysis of the complex with Leb-OMe has demonstrated that the binding site on the lectin is a shallow depression with a negatively charged aspartate side chain at the bottom of the cavity. In addition to this aspartate, a serine and an asparagine side chain provide the polar groups that hydrogen bond to the three hydroxyl groups of Leb, which has been termed the key polar grouping for complex formation. A notable characteristic of the binding site is that five aromatic amino acid side chains (one Phe, two Tyr, and two Trp residues) surround these polar interactions and make van der Waals contacts with the tetrasaccharide. Thus, as predicted from previous solution binding studies, extensive nonpolar interactions are involved, which contribute importantly both to the specificity of the reaction and the stability of the noncovalent complex that is formed. These results represent the first structural example of the molecular recognition of a human blood group determinant by the receptor site of a protein. Extensive sequence homology exists between GS4 and the concanavalin A (Con A), pea, and favin lectins. The main hydrophilic groups of the carbohydrate-binding site of GS4 and Con A are aspartate, asparagine, and serine residues; the homology suggests that the serine is replaced by asparagine in the case of the pea and favin lectins. It appears probable that these two latter lectins possess very similar, if not identical, specificities. Keywords: lectin, carbohydrate, molecular recognition, binding.

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Padilla-Vaca, Felipe, Serge Ankri, Rivka Bracha, Lucy Anna Koole, and David Mirelman. "Down Regulation of Entamoeba histolytica Virulence by Monoxenic Cultivation with Escherichia coli O55 Is Related to a Decrease in Expression of the Light (35-Kilodalton) Subunit of the Gal/GalNAc Lectin." Infection and Immunity 67, no. 5 (May 1, 1999): 2096–102. http://dx.doi.org/10.1128/iai.67.5.2096-2102.1999.

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ABSTRACT Entamoeba histolytica virulence is related to a number of amebic components (lectins, cysteine proteinases, and amebapore) and host factors, such as intestinal bacterial flora. Trophozoites are selective in their interactions with bacteria, and the parasite recognition of glycoconjugates plays an important role in amebic virulence. Long-term monoxenic cultivation of pathogenic E. histolyticatrophozoites, strains HK-9 or HM-1:IMSS, with Escherichia coli serotype O55, which binds strongly to the Gal/GalNAc amebic lectin, markedly reduced the trophozoites’ adherence and cytopathic activity on cell monolayers of baby hamster kidney (BHK) cells. Specific probes prepared from E. histolytica lectin genes as well as antibodies directed against the light (35-kDa) and heavy (170-kDa) subunits of the Gal/GalNAc lectin revealed a decrease in the transcription and expression of the light subunit in trophozoites grown monoxenically with E. coli O55. This effect was not observed when E. histolyticawas grown with E. coli 346, a mannose-binding type I pilated bacteria. Our results suggest that the light subunit of the amebic lectin is involved in the modulation of parasite adherence and cytopathic activity.

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Dai, Zong, Abdel-Nasser Kawde, Yun Xiang, Jeffrey T. La Belle, Jared Gerlach, Veer P. Bhavanandan, Lokesh Joshi, and Joseph Wang. "Nanoparticle-Based Sensing of Glycan−Lectin Interactions." Journal of the American Chemical Society 128, no. 31 (August 2006): 10018–19. http://dx.doi.org/10.1021/ja063565p.

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Crouzier, Thomas, Colin H. Beckwitt, and Katharina Ribbeck. "Mucin Multilayers Assembled through Sugar–Lectin Interactions." Biomacromolecules 13, no. 10 (September 18, 2012): 3401–8. http://dx.doi.org/10.1021/bm301222f.

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Tan, Yih Horng, Kohki Fujikawa, Papapida Pornsuriyasak, Allan J. Alla, N. Vijaya Ganesh, Alexei V. Demchenko, and Keith J. Stine. "Lectin–carbohydrate interactions on nanoporous gold monoliths." New Journal of Chemistry 37, no. 7 (2013): 2150. http://dx.doi.org/10.1039/c3nj00253e.

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Journal articles on the topic 'Lectin Interactions'

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