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Journal articles on the topic 'Carbohydrate-lectin interactions'

Author: Grafiati

Published: 4 June 2021

Last updated: 27 April 2022

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1

Lis, Halina, and Nathan Sharon. "Lectin-carbohydrate interactions." Current Opinion in Structural Biology 1, no. 5 (1991): 741–49. http://dx.doi.org/10.1016/0959-440x(91)90173-q.

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2

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

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3

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

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4

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

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5

Shang, Kun, Siyu Song, Yaping Cheng, et al. "Fabrication of Carbohydrate Chips Based on Polydopamine for Real-Time Determination of Carbohydrate–Lectin Interactions by QCM Biosensor." Polymers 10, no. 11 (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

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6

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 (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 fo

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7

Tan, Yih Horng, Kohki Fujikawa, Papapida Pornsuriyasak, et al. "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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8

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 c

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9

Scheibe, Christian, and Oliver Seitz. "PNA–sugar conjugates as tools for the spatial screening of carbohydrate–lectin interactions." Pure and Applied Chemistry 84, no. 1 (2011): 77–85. http://dx.doi.org/10.1351/pac-con-11-08-07.

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Multivalent carbohydrate–lectin interactions are essential for a multitude of biological recognition events. Much effort has been spent in the synthesis of potent multivalent scaffolds in order to mimic or inhibit biological carbohydrate–protein interactions. However, the defined spatial presentation of carbohydrates remained a challenging task. Peptide nucleic acid (PNA)- and DNA-based double helices are useful scaffolds that enable the controlled display of carbohydrate ligands in a modular approach. The hybridization of PNA-sugar conjugates with complementary DNA strands provides multivalen

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10

Duverger, E. "Carbohydrate-lectin interactions assessed by surface plasmon resonance." Biochimie 85, no. 1-2 (2003): 167–79. http://dx.doi.org/10.1016/s0300-9084(03)00060-9.

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11

Scheibe, Christian, Alexander Bujotzek, Jens Dernedde, Marcus Weber, and Oliver Seitz. "DNA-programmed spatial screening of carbohydrate–lectin interactions." Chemical Science 2, no. 4 (2011): 770. http://dx.doi.org/10.1039/c0sc00565g.

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12

Elgavish, Sharona, and Boaz Shaanan. "Lectin-carbohydrate interactions: different folds, common recognition principles." Trends in Biochemical Sciences 22, no. 12 (1997): 462–67. http://dx.doi.org/10.1016/s0968-0004(97)01146-8.

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13

Navarra, Giulio, Pascal Zihlmann, Roman P. Jakob, et al. "Carbohydrate-Lectin Interactions: An Unexpected Contribution to Affinity." ChemBioChem 18, no. 6 (2017): 539–44. http://dx.doi.org/10.1002/cbic.201600615.

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14

Scharenberg, Meike, Xiaohua Jiang, Lijuan Pang, et al. "Kinetic Properties of Carbohydrate-Lectin Interactions: FimH Antagonists." ChemMedChem 9, no. 1 (2013): 78–83. http://dx.doi.org/10.1002/cmdc.201300349.

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15

Kauscher, Ulrike, and Bart Jan Ravoo. "Mannose-decorated cyclodextrin vesicles: The interplay of multivalency and surface density in lectin–carbohydrate recognition." Beilstein Journal of Organic Chemistry 8 (September 17, 2012): 1543–51. http://dx.doi.org/10.3762/bjoc.8.175.

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Cyclodextrin vesicles are versatile models for biological cell membranes since they provide a bilayer membrane that can easily be modified by host–guest interactions with functional guest molecules. In this article, we investigate the multivalent interaction of the lectin concanavalin A (ConA) with cyclodextrin vesicles decorated with mannose–adamantane conjugates with one, two or three adamantane units as well as one or two mannose units. The carbohydrate–lectin interaction in this artificial, self-assembled glycocalyx was monitored in an agglutination assay by the increase of optical density

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16

Sundhoro, Madanodaya, Hui Wang, Scott T. Boiko, et al. "Fabrication of carbohydrate microarrays on a poly(2-hydroxyethyl methacrylate)-based photoactive substrate." Organic & Biomolecular Chemistry 14, no. 3 (2016): 1124–30. http://dx.doi.org/10.1039/c5ob01417d.

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17

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 (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 specifi

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18

Euzen, Ronan, and Jean-Louis Reymond. "Glycopeptide dendrimers: tuning carbohydrate–lectin interactions with amino acids." Mol. BioSyst. 7, no. 2 (2011): 411–21. http://dx.doi.org/10.1039/c0mb00177e.

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19

Vedala, Harindra, Yanan Chen, Samy Cecioni, Anne Imberty, Sébastien Vidal, and Alexander Star. "Nanoelectronic Detection of Lectin-Carbohydrate Interactions Using Carbon Nanotubes." Nano Letters 11, no. 1 (2011): 170–75. http://dx.doi.org/10.1021/nl103286k.

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20

Di Maio, Antonio, Anna Cioce, Silvia Achilli, et al. "Controlled density glycodendron microarrays for studying carbohydrate–lectin interactions." Organic & Biomolecular Chemistry 19, no. 34 (2021): 7357–62. http://dx.doi.org/10.1039/d1ob00872b.

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21

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 (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 boun

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22

Jayaprakash, Nisha Grandhi, Amrita Singh, Rahul Vivek, et al. "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 (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 i

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23

Vornholt, Wolfgang, Markus Hartmann, and Michael Keusgen. "SPR studies of carbohydrate–lectin interactions as useful tool for screening on lectin sources." Biosensors and Bioelectronics 22, no. 12 (2007): 2983–88. http://dx.doi.org/10.1016/j.bios.2006.12.021.

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24

Cagnoni, Alejandro J., Emiliano D. Primo, Sebastián Klinke та ін. "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, № 11 (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-gal

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25

Tronchin, Guy, Karine Esnault, Myriam Sanchez, Gerald Larcher, Agnes Marot-Leblond, and Jean-Philippe Bouchara. "Purification and Partial Characterization of a 32-Kilodalton Sialic Acid-Specific Lectin from Aspergillus fumigatus." Infection and Immunity 70, no. 12 (2002): 6891–95. http://dx.doi.org/10.1128/iai.70.12.6891-6895.2002.

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ABSTRACT Adherence of the opportunistic fungus Aspergillus fumigatus to the extracellular matrix components is considered a crucial step in the establishment of the infection. Given the high carbohydrate content of these glycoproteins and the role of carbohydrate-protein interactions in numerous adherence processes, the presence of a lectin in A. fumigatus was investigated. Different fungal extracts obtained by sonication or grinding in liquid nitrogen from resting or swollen conidia, as well as from germ tubes and mycelium, were tested by hemagglutination assays using rabbit erythrocytes. A l

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26

Chen, Chen, Huang Xu, Yue-Cheng Qian, and Xiao-Jun Huang. "Glycosylation of polyphosphazenes by thiol-yne click chemistry for lectin recognition." RSC Advances 5, no. 21 (2015): 15909–15. http://dx.doi.org/10.1039/c4ra14012e.

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27

Sakurai, Kaori. "Photoaffinity Labeling Approaches toward Identification of Carbohydrate^|^#x2013;Lectin Interactions." Trends in Glycoscience and Glycotechnology 27, no. 153 (2015): 1–12. http://dx.doi.org/10.4052/tigg.27.1.

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28

Dam, Tarun K., and C. Fred Brewer. "Thermodynamic Studies of Lectin−Carbohydrate Interactions by Isothermal Titration Calorimetry." Chemical Reviews 102, no. 2 (2002): 387–430. http://dx.doi.org/10.1021/cr000401x.

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29

Weimar, Thomas, Bernd Haase, and Thies Köhli. "Low Affinity Carbohydrate Lectin Interactions Examined with Surface Plasmon Resonance." Journal of Carbohydrate Chemistry 19, no. 8 (2000): 1083–89. http://dx.doi.org/10.1080/07328300008544136.

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30

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 (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 f

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31

Bowen, B. R., C. Fennie, and L. A. Lasky. "The Mel 14 antibody binds to the lectin domain of the murine peripheral lymph node homing receptor." Journal of Cell Biology 110, no. 1 (1990): 147–53. http://dx.doi.org/10.1083/jcb.110.1.147.

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Murine and human leukocytes express surface glycoproteins, termed homing receptors (HRs), containing lectin-like, EGF-like (egf), and complement binding-like domains, that apparently endow these cells with the ability to home to peripheral lymph nodes (pln's) by virtue of an adhesive interaction with the pln postcapillary venule endothelium. The murine pln HR was initially characterized with a rat monoclonal antibody, Mel 14, that was specific for the murine form of the receptor. This work demonstrated that Mel 14 blocked the binding of murine lymphocytes to pln endothelium both in vitro and i

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32

Perduca, Massimiliano, Laura Destefanis, Michele Bovi, et al. "Structure and properties of the oyster mushroom (Pleurotus ostreatus) lectin." Glycobiology 30, no. 8 (2020): 550–62. http://dx.doi.org/10.1093/glycob/cwaa006.

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Abstract Pleurotus ostreatus Lectin (POL) is a 353 amino acid chain lectin that can be purified from the fruiting bodies of the very well-known and widely diffused edible oyster mushrooms (P. ostreatus). The lectin has been partially characterized by different groups and, although it was crystallized about 20 years ago, its 3D structure and the details of its interactions with carbohydrates are still unknown. This paper reports the 3D structure and ligand-binding properties of POL. We have determined the X-ray structure of the apo-protein purified from the fruiting bodies of the mushroom and t

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33

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 asialoglycoprote

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34

Krugluger, W., W. Lill, A. Nell, S. Katzensteiner, W. Sperr, and O. Forster. "Lectin binding to chronic inflammatory gingival tissue: possible adhesion mechanisms based on lectin-carbohydrate interactions." Journal of Periodontal Research 28, no. 2 (1993): 145–51. http://dx.doi.org/10.1111/j.1600-0765.1993.tb01062.x.

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35

Maierhofer, Caroline, Katja Rohmer, and Valentin Wittmann. "Probing multivalent carbohydrate–lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates." Bioorganic & Medicinal Chemistry 15, no. 24 (2007): 7661–76. http://dx.doi.org/10.1016/j.bmc.2007.08.063.

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36

Liyanage, Sajani H., and Mingdi Yan. "Quantification of binding affinity of glyconanomaterials with lectins." Chemical Communications 56, no. 88 (2020): 13491–505. http://dx.doi.org/10.1039/d0cc05899h.

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This Feature Article discusses the techniques to determine the binding affinity glyconanomaterials, which is critical for the evaluation of nanomaterials as multivalent scaffolds in enhancing carbohydrate–lectin interactions.

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37

Zlocowski, Natacha, Virginia Lorenz, Eric P. Bennett, Henrik Clausen, Gustavo A. Nores, and Fernando J. Irazoqui. "An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferase-2." Biological Chemistry 394, no. 1 (2013): 69–77. http://dx.doi.org/10.1515/hsz-2012-0191.

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Abstract Polypeptide GalNAc-transferases (ppGalNAc-Ts) are a family of enzymes that catalyze the initiation of mucin-type O-glycosylation. All ppGalNAc-T family members contain a common (QXW)3 motif, which is present in the R-type lectin group. The acetylation site K521 is part of the QKW motif of β-trefoil in the lectin domain of ppGalNAc-T2. We used a combination of acetylation and site-directed mutagenesis approaches to examine the functional role of K521 in ppGalNAc-T2. Binding assays of non-acetylated and acetylated forms of the mutant ppGalNAc-T2K521Q to various naked and αGalNAc-glycosy

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38

Ahmed, Hafiz, and Dina M. M. Alsadek. "Galectin-3 as a Potential Target to Prevent Cancer Metastasis." Clinical Medicine Insights: Oncology 9 (January 2015): CMO.S29462. http://dx.doi.org/10.4137/cmo.s29462.

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Interactions between two cells or between cell and extracellular matrix mediated by protein–carbohydrate interactions play pivotal roles in modulating various biological processes such as growth regulation, immune function, cancer metastasis, and apoptosis. Galectin-3, a member of the β-galactoside-binding lectin family, is involved in fibrosis as well as cancer progression and metastasis, but the detailed mechanisms of its functions remain elusive. This review discusses its structure, carbohydrate-binding properties, and involvement in various aspects of tumorigenesis and some potential carbo

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39

Bakkers, Mark J. G., Qinghong Zeng, Louris J. Feitsma, et al. "Coronavirus receptor switch explained from the stereochemistry of protein–carbohydrate interactions and a single mutation." Proceedings of the National Academy of Sciences 113, no. 22 (2016): E3111—E3119. http://dx.doi.org/10.1073/pnas.1519881113.

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Hemagglutinin-esterases (HEs) are bimodular envelope proteins of orthomyxoviruses, toroviruses, and coronaviruses with a carbohydrate-binding “lectin” domain appended to a receptor-destroying sialate-O-acetylesterase (“esterase”). In concert, these domains facilitate dynamic virion attachment to cell-surface sialoglycans. Most HEs (type I) target 9-O-acetylated sialic acids (9-O-Ac-Sias), but one group of coronaviruses switched to using 4-O-Ac-Sias instead (type II). This specificity shift required quasisynchronous adaptations in the Sia-binding sites of both lectin and esterase domains. Previ

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40

Wang, Chao, Brian Sanders, and David C. Baker. "Synthesis of a glycodendrimer incorporating multiple mannosides on a glucoside core." Canadian Journal of Chemistry 89, no. 8 (2011): 959–63. http://dx.doi.org/10.1139/v11-069.

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The synthesis of a glycodendrimer by incorporating repetitive mannoside units onto a glucoside core was carried out to multivalently probe fundamental carbohydrate–protein interactions. The dendritic structure was constructed by a modified procedure that utilized multiple glycosylations between a thioether glycosyl donor and five elongated spacer arms of a glycosyl acceptor. The completed dendrimer bears a full carbohydrate structure, and thus should find its potential application in the study of mannose–lectin interactions.

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41

Kilpatrick, David C. "Lectin–glycoconjugate interactions in health and disease." Biochemical Society Transactions 36, no. 6 (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-discipli

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42

Köber, Mariana, Maria Moros, Laura Franco Fraguas, et al. "Nanoparticle-Mediated Monitoring of Carbohydrate–Lectin Interactions Using Transient Magnetic Birefringence." Analytical Chemistry 86, no. 24 (2014): 12159–65. http://dx.doi.org/10.1021/ac503122y.

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43

Lee, Reiko T., Yasuro Shinohara, Yukio Hasegawa, and Yuan C. Lee. "Lectin-Carbohydrate Interactions: Fine Specificity Difference Between Two Mannose-Binding Proteins." Bioscience Reports 19, no. 4 (1999): 283–92. http://dx.doi.org/10.1023/a:1020546307825.

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Two types of rat mannose-binding proteins (MBPs), MBP-A (serum type) and MBP-C (liver type), have similar binding specificity for monosaccharide and similar binding site construct according to the X-ray structure, but exhibit different affinity toward natural oligosaccharides and glycoproteins. To understand the basis for this phenomenon, we used cloned fragment of MBP-A and -C (entire carbohydrate-recognition domain and a short connecting piece) that exists as stable trimers in various binding studies. Binding of a number of mannose-containing di- and tri-saccharides and high-mannose type oli

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44

Garcia-Hernandez, E., R. A. Zubillaga, A. Rodriguez-Romero, and A. Hernandez-Arana. "Stereochemical metrics of lectin-carbohydrate interactions: comparison with protein-protein interfaces." Glycobiology 10, no. 10 (2000): 993–1000. http://dx.doi.org/10.1093/glycob/10.10.993.

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45

Sato, Yukari, Kyoko Yoshioka, Teiichi Murakami, Soichiro Yoshimoto, and Osamu Niwa. "Design of Biomolecular Interface for Detecting Carbohydrate and Lectin Weak Interactions." Langmuir 28, no. 3 (2012): 1846–51. http://dx.doi.org/10.1021/la2030044.

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46

Becer, C. Remzi. "The Glycopolymer Code: Synthesis of Glycopolymers and Multivalent Carbohydrate-Lectin Interactions." Macromolecular Rapid Communications 33, no. 9 (2012): 742–52. http://dx.doi.org/10.1002/marc.201200055.

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47

Zhang, Xiaojuan, and Vamsi K. Yadavalli. "Functionalized self-assembled monolayers for measuring single molecule lectin carbohydrate interactions." Analytica Chimica Acta 649, no. 1 (2009): 1–7. http://dx.doi.org/10.1016/j.aca.2009.07.027.

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48

Cooper, Oren, Hoang-Phuong Phan, Tom Fitzpatrick, et al. "Picomolar detection of carbohydrate-lectin interactions on piezoelectrically printed microcantilever array." Biosensors and Bioelectronics 205 (June 2022): 114088. http://dx.doi.org/10.1016/j.bios.2022.114088.

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49

Wharton, D. A., and D. S. Murray. "Carbohydrate/lectin interactions between the nematophagous fungus,Arthrobotrys oligospora, and the infective juveniles ofTrichostrongylus colubriformis(Nematoda)." Parasitology 101, no. 1 (1990): 101–6. http://dx.doi.org/10.1017/s0031182000079804.

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SUMMARYRemoval of the sheath of the ensheathed infective juvenile ofTrichostrongylus colubriformisprevents capture by the nematophagous fungusArthrobotrys oligospora. Exposure of the trap hyphae to a variety of saccharides, which may block a recognition system based on lectin/carbohydrate binding, failed to prevent capture but some saccharides did inhibit penetration and invasion by the fungus. Capture and penetration thus appear to be two distinct processes with capture being less specific than penetration. Carbohydrate residues were absent from the outer surface of the cuticle and the sheath

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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 (2008): 1482–86. http://dx.doi.org/10.1042/bst0361482.

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Abstract:

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 dietar

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