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Glycoconjugates and Glycomimetics for Targeting Lectins

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: closed (30 September 2021) | Viewed by 20436

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Special Issue Editors

Dr. Pavla Bojarová

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Guest Editor

1. Institute of Microbiology, Academy of Sciences of the Czech Republic, Laboratory of Biotransformation, National Centre of Biocatalysis and Biotransformation, Videnska 1083, CZ 142 20 Praha 4, Czech Republic
2. Faculty of Biomedical Engineering, Czech Technical University in Prague, Kladno, Czech Republic
Interests: biocatalysis and biotransformation by enzymes and whole cells; glycosidases; glycosyltransferases; sulfatases and sulfotransferases; nitrilases; site-directed mutagenesis and directed evolution of enzymes; engineering of enzymatic reactions; enzymatic synthesis of oligosaccharides; glycoconjugates; glycobiomaterials; glycopolymers; enzyme inhibitors and time-dependent inactivators; analysis of enzyme active site
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Prof. Dr. Vladimír Křen

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Institute of Microbiology, Academy of Sciences of the Czech Republic, Laboratory of Biotransformation, National Centre of Biocatalysis and Biotransformation, Videnska 1083, CZ 142 20 Praha 4, Czech Republic
Interests: biocatalysis and biotransformation; immobilized microbial cells, their use in production and biotransformation of natural products; biotransformation of natural products by enzymes and microorganisms; preparation of glycosidases of microbial origin and their use for glycosylation of natural compounds: glycoconjugates, multivalent compounds, ergot alkaloids, flavonoids, antioxidants and chemoprotectants
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Special Issue Information

Dear Colleagues,

Intercellular communication is often mediated by interactions between cell surface glycans and carbohydrate-binding proteins named lectins. Altered glycosylation may indicate and accompany major pathological processes in vivo. Therefore, carbohydrate–lectin interactions are attractive for diagnosis and therapy. Tailored glycomimetics (non-natural carbohydrate-based compounds) and multivalent glycoconjugates based on various scaffolds enable to master, modify, and control the interaction with lectins. Multivalency, mimicking nature´s design, may boost this interaction by several orders of magnitude. Important characteristics of efficient lectin ligands comprise selectivity, sensitivity, high affinity, favorable pharmacokinetics and pharmacodynamics, and biocompatibility.

The Special Issue " Glycoconjugates and glycomimetics for targeting lectins" aims to cover the research progress in the analysis, binding, or inhibition of biomedically attractive lectins using natural and artificial glycoconjugates, glycomimetics, and oligo- and polysaccharides. We are seeking contributions on new (bio)synthetic methods for glycoconjugates and glycomimetics, including the use of carbohydrate-active enzymes, innovative multivalency concepts, and methods of analyzing ligand interaction with lectins and the relationship between a ligand structure and its affinity. We welcome studies on structures prospective as diagnostic, therapeutic, or drug delivery agents.

Dr. Pavla Bojarová
Prof. Dr. Vladimír Křen
Guest Editors

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Keywords

Biomaterials and drug-targeting systems
Chemo-enzymatic modification and synthesis
Multivalent glycodendrimers and glycopolymers
Glycomimetics
Glycopeptides and glycoproteins
Glycosidases and glycosyltransferases
Structure–affinity relationship

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Published Papers (7 papers)

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Research

12 pages, 4733 KiB

Open AccessArticle

Identification of Multiple Domains of Entamoeba histolytica Intermediate Subunit Lectin-1 with Hemolytic and Cytotoxic Activities

by Kentaro Kato and Hiroshi Tachibana

Int. J. Mol. Sci. 2022, 23(14), 7700; https://doi.org/10.3390/ijms23147700 - 12 Jul 2022

Cited by 2 | Viewed by 1608

Abstract

Galactose and N-acetyl-D-galactosamine-inhibitable lectin of Entamoeba histolytica have roles in the pathogenicity of intestinal amoebiasis. Igl1, the intermediate subunit lectin-1 of E. histolytica, has been shown to have both hemolytic and cytotoxic activities that reside in the C-terminus of the protein. To identify the amino acid regions responsible for these activities, recombinant proteins were prepared and used in hemolytic and cytotoxic assays. The results revealed that Igl1 has multiple domains with hemolytic and cytotoxic activities and that amino acids 787-846, 968-1028 and 1029-1088 are involved in these activities. The hemolytic activities of the fragments were partly inhibited by mannose, galactose and N-acetylgalactosamine, and glucose showed lower or negligible inhibitory effects for the activities. This is the first report of a protozoan protein with hemolytic and cytotoxic activities in multiple domains. Full article

(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)

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17 pages, 2119 KiB

Open AccessArticle

Investigation of the Molecular Details of the Interactions of Selenoglycosides and Human Galectin-3

by Mária Raics, Álex Kálmán Balogh, Chandan Kishor, István Timári, Francisco J. Medrano, Antonio Romero, Rob Marc Go, Helen Blanchard, László Szilágyi, Katalin E. Kövér and Krisztina Fehér

Int. J. Mol. Sci. 2022, 23(5), 2494; https://doi.org/10.3390/ijms23052494 - 24 Feb 2022

Cited by 8 | Viewed by 2935

Abstract

Human galectin-3 (hGal-3) is involved in a variety of biological processes and is implicated in wide range of diseases. As a result, targeting hGal-3 for clinical applications has become an intense area of research. As a step towards the development of novel hGal-3 inhibitors, we describe a study of the binding of two Se-containing hGal-3 inhibitors, specifically that of di(β-D-galactopyranosyl)selenide (SeDG), in which two galactose rings are linked by one Se atom and a di(β-D-galactopyranosyl)diselenide (DSeDG) analogue with a diseleno bond between the two sugar units. The binding affinities of these derivatives to hGal-3 were determined by ¹⁵N-¹H HSQC NMR spectroscopy and fluorescence anisotropy titrations in solution, indicating a slight decrease in the strength of interaction for SeDG compared to thiodigalactoside (TDG), a well-known inhibitor of hGal-3, while DSeDG displayed a much weaker interaction strength. NMR and FA measurements showed that both seleno derivatives bind to the canonical S face site of hGal-3 and stack against the conserved W181 residue also confirmed by X-ray crystallography, revealing canonical properties of the interaction. The interaction with DSeDG revealed two distinct binding modes in the crystal structure which are in fast exchange on the NMR time scale in solution, explaining a weaker interaction with hGal-3 than SeDG. Using molecular dynamics simulations, we have found that energetic contributions to the binding enthalpies mainly differ in the electrostatic interactions and in polar solvation terms and are responsible for weaker binding of DSeDG compared to SeDG. Selenium-containing carbohydrate inhibitors of hGal-3 showing canonical binding modes offer the potential of becoming novel hydrolytically stable scaffolds for a new class of hGal-3 inhibitors. Full article

(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)

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19 pages, 3717 KiB

Open AccessArticle

Overcoming Microenvironment-Mediated Chemoprotection through Stromal Galectin-3 Inhibition in Acute Lymphoblastic Leukemia

by Somayeh S. Tarighat, Fei Fei, Eun Ji Joo, Hisham Abdel-Azim, Lu Yang, Huimin Geng, Khuchtumur Bum-Erdene, I. Darren Grice, Mark von Itzstein, Helen Blanchard and Nora Heisterkamp

Int. J. Mol. Sci. 2021, 22(22), 12167; https://doi.org/10.3390/ijms222212167 - 10 Nov 2021

Cited by 10 | Viewed by 2511

Abstract

Environmentally-mediated drug resistance in B-cell precursor acute lymphoblastic leukemia (BCP-ALL) significantly contributes to relapse. Stromal cells in the bone marrow environment protect leukemia cells by secretion of chemokines as cues for BCP-ALL migration towards, and adhesion to, stroma. Stromal cells and BCP-ALL cells communicate through stromal galectin-3. Here, we investigated the significance of stromal galectin-3 to BCP-ALL cells. We used CRISPR/Cas9 genome editing to ablate galectin-3 in stromal cells and found that galectin-3 is dispensable for steady-state BCP-ALL proliferation and viability. However, efficient leukemia migration and adhesion to stromal cells are significantly dependent on stromal galectin-3. Importantly, the loss of stromal galectin-3 production sensitized BCP-ALL cells to conventional chemotherapy. We therefore tested novel carbohydrate-based small molecule compounds (Cpd14 and Cpd17) with high specificity for galectin-3. Consistent with results obtained using galectin-3-knockout stromal cells, treatment of stromal-BCP-ALL co-cultures inhibited BCP-ALL migration and adhesion. Moreover, these compounds induced anti-leukemic responses in BCP-ALL cells, including a dose-dependent reduction of viability and proliferation, the induction of apoptosis and, importantly, the inhibition of drug resistance. Collectively, these findings indicate galectin-3 regulates BCP-ALL cell responses to chemotherapy through the interactions between leukemia cells and the stroma, and show that a combination of galectin-3 inhibition with conventional drugs can sensitize the leukemia cells to chemotherapy. Full article

(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)

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8 pages, 904 KiB

Open AccessCommunication

Quantification and Topographical Distribution of Terminal and Linked Fucose Residues in Human Spermatozoa by Using Field Emission Scanning Electron Microscopy (FE-SEM)

by Laura Robles-Gómez, Paula Sáez-Espinosa, Eliana Marina López-Viloria, Andrea López-Botella, Jon Aizpurua and María José Gómez-Torres

Int. J. Mol. Sci. 2021, 22(21), 11947; https://doi.org/10.3390/ijms222111947 - 4 Nov 2021

Cited by 2 | Viewed by 1815

Abstract

The modification of sperm glycocalyx is an essential process during sperm capacitation. The presence and redistribution of terminal and linked fucose have been described during in vitro capacitation in humans. However, the influence of the capacitation time on the quantification and localization of terminal and linked fucose is still unknown. In this study, the quantitative and qualitative changes in fucosyl residues during different in vitro capacitation times (1 and 4 h), are simultaneously characterized by using Aleuria aurantia (AAA) lectin–gold labelling and high-resolution field emission scanning electron microscopy (FE-SEM) in human sperm. A significant decrease was found in the number of terminal fucose registered in the whole sperm head during the in vitro capacitation. Nevertheless, the quantification of fucose residues after 1 h of in vitro capacitation was very similar to those found after 4 h. Therefore, the changes observed in terminal and linked fucose during capacitation were not time-dependent. Furthermore, the comprehensive analysis of the topographic distribution showed the preferential fucosyl location in the acrosomal region and the presence of distinct clusters distributed over the head in all the studied conditions. Overall, these findings corroborate the validity of FE-SEM combined with gold labelling to register changes in surface molecules during in vitro sperm capacitation. Full article

(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)

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9 pages, 2166 KiB

Open AccessArticle

Reversible Lectin Binding to Glycan-Functionalized Graphene

by Tereza Koukalová, Petr Kovaříček, Pavla Bojarová, Valentino L. P. Guerra, Vladimír Vrkoslav, Lukáš Navara, Ivan Jirka, Marek Cebecauer, Vladimír Křen and Martin Kalbáč

Int. J. Mol. Sci. 2021, 22(13), 6661; https://doi.org/10.3390/ijms22136661 - 22 Jun 2021

Cited by 2 | Viewed by 3154

Abstract

The monolayer character of two-dimensional materials predestines them for application as active layers of sensors. However, their inherent high sensitivity is always accompanied by a low selectivity. Chemical functionalization of two-dimensional materials has emerged as a promising way to overcome the selectivity issues. Here, we demonstrate efficient graphene functionalization with carbohydrate ligands—chitooligomers, which bind proteins of the lectin family with high selectivity. Successful grafting of a chitooligomer library was thoroughly characterized, and glycan binding to wheat germ agglutinin was studied by a series of methods. The results demonstrate that the protein quaternary structure remains intact after binding to the functionalized graphene, and that the lectin can be liberated from the surface by the addition of a binding competitor. The chemoenzymatic assay with a horseradish peroxidase conjugate also confirmed the intact catalytic properties of the enzyme. The present approach thus paves the way towards graphene-based sensors for carbohydrate–lectin binding. Full article

(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)

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17 pages, 4729 KiB

Open AccessArticle

Cross-Linking Effects Dictate the Preference of Galectins to Bind LacNAc-Decorated HPMA Copolymers

by Sara Bertuzzi, Ana Gimeno, Ane Martinez-Castillo, Marta G. Lete, Sandra Delgado, Cristina Airoldi, Marina Rodrigues Tavares, Markéta Bláhová, Petr Chytil, Vladimír Křen, Nicola G. A. Abrescia, Ana Ardá, Pavla Bojarová and Jesús Jiménez-Barbero

Int. J. Mol. Sci. 2021, 22(11), 6000; https://doi.org/10.3390/ijms22116000 - 1 Jun 2021

Cited by 7 | Viewed by 3562

Abstract

The interaction of multi-LacNAc (Galβ1-4GlcNAc)-containing N-(2-hydroxypropyl) methacrylamide (HPMA) copolymers with human galectin-1 (Gal-1) and the carbohydrate recognition domain (CRD) of human galectin-3 (Gal-3) was analyzed using NMR methods in addition to cryo-electron-microscopy and dynamic light scattering (DLS) experiments. The interaction with individual LacNAc-containing components of the polymer was studied for comparison purposes. For Gal-3 CRD, the NMR data suggest a canonical interaction of the individual small-molecule bi- and trivalent ligands with the lectin binding site and better affinity for the trivalent arrangement due to statistical effects. For the glycopolymers, the interaction was stronger, although no evidence for forming a large supramolecule was obtained. In contrast, for Gal-1, the results indicate the formation of large cross-linked supramolecules in the presence of multivalent LacNAc entities for both the individual building blocks and the polymers. Interestingly, the bivalent and trivalent presentation of LacNAc in the polymer did not produce such an increase, indicating that the multivalency provided by the polymer is sufficient for triggering an efficient binding between the glycopolymer and Gal-1. This hypothesis was further demonstrated by electron microscopy and DLS methods. Full article

(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)

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26 pages, 4009 KiB

Open AccessArticle

Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells

by Antonín Sedlář, Martina Trávníčková, Pavla Bojarová, Miluše Vlachová, Kristýna Slámová, Vladimír Křen and Lucie Bačáková

Int. J. Mol. Sci. 2021, 22(10), 5144; https://doi.org/10.3390/ijms22105144 - 13 May 2021

Cited by 25 | Viewed by 3651

Abstract

Galectin-3 (Gal-3) is a β-galactoside-binding protein that influences various cell functions, including cell adhesion. We focused on the role of Gal-3 as an extracellular ligand mediating cell-matrix adhesion. We used human adipose tissue-derived stem cells and human umbilical vein endothelial cells that are promising for vascular tissue engineering. We found that these cells naturally contained Gal-3 on their surface and inside the cells. Moreover, they were able to associate with exogenous Gal-3 added to the culture medium. This association was reduced with a β-galactoside LacdiNAc (GalNAcβ1,4GlcNAc), a selective ligand of Gal-3, which binds to the carbohydrate recognition domain (CRD) in the Gal-3 molecule. This ligand was also able to detach Gal-3 newly associated with cells but not Gal-3 naturally present on cells. In addition, Gal-3 preadsorbed on plastic surfaces acted as an adhesion ligand for both cell types, and the cell adhesion was resistant to blocking with LacdiNAc. This result suggests that the adhesion was mediated by a binding site different from the CRD. The blocking of integrin adhesion receptors on cells with specific antibodies revealed that the cell adhesion to the preadsorbed Gal-3 was mediated, at least partially, by β1 and αV integrins—namely α5β1, αVβ3, and αVβ1 integrins. Full article

(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)

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