The Galβ-(syn)-gauche configuration is required for galectin-recognition disaccharides

Iwaki, Jun; Tateno, Hiroaki; Nishi, Nozomu; Minamisawa, Toshikazu; Nakamura‐Tsuruta, Sachiko; Ikoma, Yoko; Kominami, Junko; Urashima, Tadasu; Nakamura, Takanori; Hirabayashi, Jun

doi:10.1016/j.bbagen.2011.04.001

Cited by 36 publications

(39 citation statements)

References 65 publications

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“…The assay method is described in the legend to glycans found in the adsorbed fraction, having two non-sialylated lactosamine (or ␣-galactosylated lactosamine) units at the non-reducing end. This finding is consistent with the binding specificity of Gal-9 revealed on frontal affinity chromatography (4,34). The ␣-Gal epitope (Gal␣1-3Gal␤1-4GlcNAc-R) found in some glycans in the adsorbed fraction is not present in humans, but it is known to be present in many mammals, including mice.…”

Section: Discussionsupporting

confidence: 86%

Cooperative Interactions of Oligosaccharide and Peptide Moieties of a Glycopeptide Derived from IgE with Galectin-9

Nakakita¹,

Itoh²,

Nakakita³

et al. 2016

Journal of Biological Chemistry

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We previously showed that galectin-9 suppresses degranulation of mast cells through protein-glycan interaction with IgE. To elucidate the mechanism of the interaction in detail, we focused on identification and structural analysis of IgE glycans responsible for the galectin-9-induced suppression using mouse monoclonal IgE (TIB-141). TIB-141 in combination with the antigen induced degranulation of RBL-2H3 cells, which was almost completely inhibited by human and mouse galectin-9. Sequential digestion of TIB-141 with lysyl endopeptidase and trypsin resulted in the identification of a glycopeptide (H-Lys13-Try3; 48 amino acid residues) with a single N-linked oligosaccharide near the N terminus capable of neutralizing the effect of galectin-9 and another glycopeptide with two N-linked oligosaccharides (H-Lys13-Try1; 16 amino acid residues) having lower activity. Enzymatic elimination of the oligosaccharide chain from H-Lys13-Try3 and H-Lys13-Try1 completely abolished the activity. Removal of the C-terminal 38 amino acid residues of H-Lys13-Try3 with glutamyl endopeptidase, however, also resulted in loss of the activity. We determined the structures of N-linked oligosaccharides of H-Lys13-Try1. The galectin-9-binding fraction of pyridylaminated oligosaccharides contained asialo-and monosialylated bi/tri-antennary complex type oligosaccharides with a core fucose residue. The structures of the oligosaccharides were consistent with the sugar-binding specificity of galectin-9, whereas the nonbinding fraction contained monosialylated and disialylated biantennary complex type oligosaccharides with a core fucose residue. Although the oligosaccharides linked to H-Lys13-Try3 could not be fully characterized, these results indicate the possibility that cooperative binding of oligosaccharide and neighboring polypeptide structures of TIB-141 to galectin-9 affects the overall affinity and specificity of the IgElectin interaction.

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Section: Discussionsupporting

confidence: 86%

Cooperative Interactions of Oligosaccharide and Peptide Moieties of a Glycopeptide Derived from IgE with Galectin-9

Nakakita¹,

Itoh²,

Nakakita³

et al. 2016

Journal of Biological Chemistry

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“…specificities of several lectins, monoclonal antibodies or virus capsid proteins (14)(15)(16)(17)(18)(19)(20)(21). In this mini-review, we present a comprehensive dataset, in tabular form, of the chemical structures of HMOs that have been characterized to date, in order to provide a HMO database as a reference for future research on the sugar-binding specificities, inhibitors and biological functions of galectins.…”

Section: Se53mentioning

confidence: 99%

Human Milk Oligosaccharides as Essential Tools for Basic and Application Studies on Galectins

Urashima

Hirabayashi

Sato

et al. 2018

Trends in Glycoscience and Glycotechnology

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130

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It is now recognized that human milk oligosaccharides (HMOs) can function both as prebiotics and as decoy receptors that inhibit the attachment of pathogenic microorganisms to the colonic mucosa. They can also act as immune modulators and as colonic maturation stimulators in breast-fed infants. These functions could be mediated by biological interaction between a variety of HMOs and lectins including galectins, selectins and siglecs. There are more than 100 HMOs; they have structural units such as H type 1: Fucα1-2Galβ1-3GlcNAc, Lewis a: Galβ1-3(Fucα1-4)GlcNAc, Lewis b: Fucα1-2Galβ1-3(Fucα1-4)GlcNAc, Lewis x: Galβ1-4(Fuc α1-3)GlcNAc, sialyl Lewis a: Neu5Acα2-3Galβ1-3(Fucα1-4)GlcNAc, and sialyl Lewis x: Neu5Acα2-3Galβ1-4(Fucα1-3)GlcNAc. It can be expected that these units may be utilized as tools for studies on the sugar-binding specificities of lectins including galectins, monoclonal antibodies, virus capsid proteins and bacterial toxins. This mini-review presents the dataset of comprehensive HMO structures, including recently clarified ones, in tabular form, for its utilization in such studies, including those of carbohydratebinding specificity of galectins. In addition, this review introduces recent in vivo and clinical studies, which may be relevant to the biological functions and future utilization of HMOs.

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“…This linkage shift may affect the biological functions of endogenous lectins, such as galectins and siglecs. The binding activity of galectins is greatly diminished when LacNAc chains are capped with α2,6-linked Sia (106,107).…”

Section: Differentiated Cell Sialylated N-glycansmentioning

confidence: 99%

Cell Surface Sialylated N-Glycan Alterations during Development

Karaçalı¹

2017

Eur J Biol

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This brief survey focuses on the comparison of sialylated N-glycans of embryonic stem cells (ESCs), induced pluripotent stem cells (iPSCs), mesenchymal stem cells (MSCs) and of differentiated cells. In addition, the impact of sialic acid (Sia) deficiency on cell surfaces during development is summarized. The most common Sia is N-acetylneuraminic acid (Neu5Ac). The branched structures of complex-and hybrid-type N-glycans are the carrier for Sia. Transmembrane adhesive proteins, voltage-gated ion channels and many ligand-activated receptors are some examples of heavily sialylated N-glycan bearing membrane proteins. Their oligosaccharide extensions provide an important contribution to glycocalyx glycans. ESCs and iPSCs are characterized with high mannose-type and biantennary complex-type core structures. Two branches terminate with α2,6-linked Sia. MSCs contain high mannose, hybrid-and complex-type N-glycans. Linear poly-N-acetyllactosamine (poly-Galβ1-4GlcNAc, poly-LacNAc) chains are the characteristic structures. Both α2,3-and α2,6-linked Sias are seen in a species-specific manner in MSCs. α2,6-linked Sia is probably a marker associated with the multipotency of human MSCs. Differentiated healthy cells contain the most abundant 2-branched complex structures. The bisecting branch on the core structure appears as a differentiation marker. poly-LacNAc chains are terminated with α2,3-and α2,6-linked Sia, with the former being higher. poly-LacNAc sequences have a high affinity for β-galactoside recognizing lectin and galectin. Galectin forms a lattice structure with the N-glycans of glycoproteins anchored to the plasma membrane. The impact of N-glycangalectin complexes in cell biology is summarized. Finally, the effect of reduced Sia on clearance of aged cells is explained. Experimental evidence for the masking role of Sia in the regulation of histolysis in aged cells is revealed.

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The Galβ-(syn)-gauche configuration is required for galectin-recognition disaccharides

Cited by 36 publications

References 65 publications

Cooperative Interactions of Oligosaccharide and Peptide Moieties of a Glycopeptide Derived from IgE with Galectin-9

Cooperative Interactions of Oligosaccharide and Peptide Moieties of a Glycopeptide Derived from IgE with Galectin-9

Human Milk Oligosaccharides as Essential Tools for Basic and Application Studies on Galectins

Cell Surface Sialylated N-Glycan Alterations during Development

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