Prompt Chemoenzymatic Synthesis of Diverse Complex‐Type Oligosaccharides and Its Application to the Solid‐Phase Synthesis of a Glycopeptide with Asn‐Linked Sialyl‐undeca‐ and Asialo‐nonasaccharides

Kajihara, Yasuhiro; Suzuki, Yasuhiro; Yamamoto, Naoki; Sasaki, Ken; Sakakibara, Tohru; Juneja, Lekh Raj

doi:10.1002/chem.200305115

Cited by 161 publications

(117 citation statements)

References 66 publications

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“…The 1 H NMR resonances of the sugar part of compounds 1, 2, 3, H, E, and C (supplemental Fig. 4S) were in accordance with the published data (22). Depending on the pH and on counter ions, the resonances of the Asn moiety may vary.…”

Section: Synthesis Of Symmetrical and Asymmetrical Asn-linked N-glycanssupporting

confidence: 89%

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A Lectin from Platypodium elegans with Unusual Specificity and Affinity for Asymmetric Complex N-Glycans

Benevides

Ganne

Simoes

et al. 2012

Journal of Biological Chemistry

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Background: Legume lectins with new glycan specificity can be discovered in the Dalbergieae tribe. Results: We determined the sequence, specificity, and crystal structures of a new Man/Glc lectin (PELa) from Platypodium elegans seeds. Conclusion: The unusual affinity of PELa for asymmetrical complex N-glycans is related to the extended binding site and conformational constraints on oligosaccharides. Significance: Dalbergieae lectins are of interest for biotechnological applications.

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Section: Synthesis Of Symmetrical and Asymmetrical Asn-linked N-glycanssupporting

confidence: 89%

“…Synthesis of H-Nonasaccharide-Asn 1 was prepared from egg yolk by enzymatic hydrolysis of its disialylated derivative (22). 10.0 mg (5.7 mol) of nonasaccharide-Asn 1 were dissolved in 450 l of phosphate buffer (100 mM, pH 6.8, 30 mM MgCl 2 , 100 mM ␤-mercaptoethanol).…”

Section: Synthesis Of Asn-linked N-glycans H E and Cmentioning

confidence: 99%

A Lectin from Platypodium elegans with Unusual Specificity and Affinity for Asymmetric Complex N-Glycans

Benevides

Ganne

Simoes

et al. 2012

Journal of Biological Chemistry

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“…Preparation of NonasaccharideAsn 1-The protected compound Fmoc-1 was prepared from egg yolk by acid hydrolysis of the disialylated derivative of Fmoc-1 in analogy to the published procedures (22,23 (Fig. S1).…”

Section: Methodsmentioning

confidence: 99%

High Affinity Interaction between a Bivalve C-type Lectin and a Biantennary Complex-type N-Glycan Revealed by Crystallography and Microcalorimetry

Gourdine

Cioci

Miguet

et al. 2008

Journal of Biological Chemistry

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Codakine is an abundant 14-kDa mannose-binding C-type lectin isolated from the gills of the sea bivalve Codakia orbicularis. Binding studies using inhibition of hemagglutination indicated specificity for mannose and fucose monosaccharides. Further experiments using a glycan array demonstrated, however, a very fine specificity for N-linked biantennary complex-type glycans. An unusually high affinity was measured by titration microcalorimetry performed with a biantennary Asn-linked nonasaccharide. The crystal structure of the native lectin at 1.3 Å resolution revealed a new type of disulfide-bridged homodimer. Each monomer displays three intramolecular disulfide bridges and contains only one calcium ion located in the canonical binding site that is occupied by a glycerol molecule. The structure of the complex between Asn-linked nonasaccharide and codakine has been solved at 1.7 Å resolution. All residues could be located in the electron density map, except for the capping ␤1-4-linked galactosides. The ␣1-6-linked mannose binds to calcium by coordinating the O3 and O4 hydroxyl groups. The GlcNAc moiety of the ␣1,6 arm engages in several hydrogen bonds with the protein, whereas the GlcNAc on the other antenna is stacked against Trp 108 , forming an extended binding site. This is the first structural report for a bivalve lectin.Lectins are multivalent carbohydrate-binding proteins that play important roles in the social life of cells. A growing repertoire of lectins has been identified in invertebrates (1), where these molecules are involved in self/nonself recognition (2). For example, lectins play a role in aggregation mechanisms in corals and sponges (3) or in sperm-egg recognition in oysters (4). Lectin mediation of symbiosis with algae or bacteria has been observed in coral (5) and nematodes (6). Nevertheless, the most common function assessed for lectins in marine invertebrates is their role in innate immunity by specific binding of polysaccharide-coated pathogenic bacteria (7,8).Different lectins have been identified in bivalves and they most frequently belong to the C-type lectin family. Proteins from this group of calcium-dependent lectins have been reported in oysters (9, 10), scallops (11), and clams (12, 13). C-type lectins are characterized by a carbohydrate recognition domain (CRD) 3 with a conserved fold and the involvement of a calcium ion in carbohydrate binding (14). The crystal structure of mannose-binding protein was the first one to be described (15). The CRD belongs to a larger family sharing a common fold and is referred to as the C-type lectin-like domain (16).Codakine is a 14-kDa C-type lectin purified from the gill of the tropical clam Codakia orbicularis (Linné 1758) by affinity chromatography on a mannose-agarose column (17). It forms homodimers and heterodimers with isoforms 1 (NCBI accession number AAX19697) and 2 (NCBI accession number ABQ40396) (13). A 19-amino acid peptide signal suggests that the lectin travels through a secretory pathway. The 129-amino acid sequence of the mature ...

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“…4. According to this strategy, over 35 kinds of diverse oligosaccharides can be prepared 42) (Figs. 5, 6).…”

Section: Synthesis Of N-linked Oligosaccharidementioning

confidence: 99%

Synthesis of Diverse Asparagine Linked Oligosaccharides

Kajihara

2005

J. Appl. Glycosci.

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Oligosaccharides are linked to the protein surface and play roles in a number of biological events.1,2) Therefore, much attention is being paid to research to investigate the function of the oligosaccharides. For post and co translational modification, attaching of oligosaccharides onto the proteins is thought to have a large effect on protein working. Recently, the human genome has been almost decoded, so that post genome research also requires a scrupulous study of the function of oligosaccharides on a protein.Oligosaccharides on glycoprotein are roughly divided into two groups, O linked and N linked types. In the case of the O linked type, a small oligosaccharide attaches to the alcohol of serine or threonine by an N acetyl D galactosaminyl linkage. The sequences of the small oligosaccharides are classified into 8 groups. On the other hand, the N linked type is a large branched oligosaccharide, which is further divided into three types: complex, hybrid, and high mannose type (Fig. 1). All oligosaccharides are linked to the nitrogen of asparagine by an N glycosyl linkage. Biosynthesis of this N linked oligosaccharide has been extensively studied. Recently, research for quality control of glycoprotein in the Endoplasmic reticulum has proved that a chaperon, calnexin calreticurin, monitors the folding process of protein recognizing high mannose type oligosaccharide on its protein surface and unfolded glycoproteins are then transported into a cytosol for digestion. 3)In order to prove the function of N glycan on the protein surface, a convenient synthetic method for N glycan and its glycopeptide should be developed. In this paper, we introduce recent synthetic developments focusing on the enzymatic synthesis of N linked oligosaccharides. Synthesis of N-linked oligosaccharide.During the synthesis of N linked oligosaccharide, several synthetic hindrances should be overcome such as stereo specific glycoside formation, and the reduction of repetitive protection and deprotection steps. In the case of glycosylation, formation of mannosyl and sialyl linkages, which is difficult, should be performed. Both glyco-* Fax. 81 45 787 2413, E mail: kajihara@yokohama cu.ac.jp J. Appl. Glycosci., 52, 177 182 (2005) ! C 2005 The Japanese Society of Applied Glycoscience Proceedings of the Symposium on Amylases and Related Enzymes, 2004Synthesis of Diverse Asparagine Linked Oligosaccharides (Received December 17, 2004) Yasuhiro KajiharaGraduate School of Integrated Science, Yokohama City University (22 2, Seto, Kanazawa ku, Yokohama 236 0027, Japan) Abstract: Oligosaccharides are linked to the protein surface and play roles in a number of biological events. Therefore, much attention is being paid to research to investigate the function of the oligosaccharides. In order to investigate the function of oligosaccharides, many synthetic approaches have been examined by synthesizing N-linked oligosaccharides. In this paper, we introduce recent synthetic developments focusing on the synthesis of N-linked oligosaccharides.

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Prompt Chemoenzymatic Synthesis of Diverse Complex‐Type Oligosaccharides and Its Application to the Solid‐Phase Synthesis of a Glycopeptide with Asn‐Linked Sialyl‐undeca‐ and Asialo‐nonasaccharides

Cited by 161 publications

References 66 publications

A Lectin from Platypodium elegans with Unusual Specificity and Affinity for Asymmetric Complex N-Glycans

A Lectin from Platypodium elegans with Unusual Specificity and Affinity for Asymmetric Complex N-Glycans

High Affinity Interaction between a Bivalve C-type Lectin and a Biantennary Complex-type N-Glycan Revealed by Crystallography and Microcalorimetry

Synthesis of Diverse Asparagine Linked Oligosaccharides

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