Specificities of<i>Ricinus communis</i>agglutinin 120 interaction with sulfated galactose

Wang, Yufeng; Yu, Guangli; Han, Zhangrun; Yang, Bo; Hu, Yan-Nan; Zhao, Xia; Wu, Jiandong; Lv, Yanna; Chai, Wengang

doi:10.1016/j.febslet.2011.10.035

Cited by 34 publications

(22 citation statements)

References 36 publications

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“…RCA promotes binding and agglutination of polysaccharides and glycoproteins in addition to liposomes and micelles containing glycolipids with galactosyl residues [80], [81]. Furthermore, the specificities of interactions of RCA with neutral and sialylated oligosaccharides have been well established and is consistent with our results as summarized in Table S11 [82].…”

Section: Resultssupporting

confidence: 90%

Community-Based Network Study of Protein-Carbohydrate Interactions in Plant Lectins Using Glycan Array Data

Malik

Lee

2014

PLoS ONE

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Lectins play major roles in biological processes such as immune recognition and regulation, inflammatory responses, cytokine signaling, and cell adhesion. Recently, glycan microarrays have shown to play key roles in understanding glycobiology, allowing us to study the relationship between the specificities of glycan binding proteins and their natural ligands at the omics scale. However, one of the drawbacks in utilizing glycan microarray data is the lack of systematic analysis tools to extract information. In this work, we attempt to group various lectins and their interacting carbohydrates by using community-based analysis of a lectin-carbohydrate network. The network consists of 1119 nodes and 16769 edges and we have identified 3 lectins having large degrees of connectivity playing the roles of hubs. The community based network analysis provides an easy way to obtain a general picture of the lectin-glycan interaction and many statistically significant functional groups.

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Section: Resultssupporting

confidence: 90%

Community-Based Network Study of Protein-Carbohydrate Interactions in Plant Lectins Using Glycan Array Data

Malik

Lee

2014

PLoS ONE

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“…Both lectins are sensitive to sulfate substitution on the Gal ring. For RCA, binding is enhanced by 2‐O ‐ or 6‐ O ‐sulfation but abolished by 4‐ O ‐sulfation (41). In contrast, the presence of sulfates generally reduces the binding affinity of PNA to terminal Gal (42) whereas or 6‐O ‐ or 3‐ O ‐sulfation or sialation of the Gal residue in Galβ1,3GalNAc can almost abolish PNA binding (43).…”

Section: Discussionmentioning

confidence: 99%

Mining the “glycocode”—exploring the spatial distribution of glycans in gastrointestinal mucin using force spectroscopy

et al. 2013

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Mucins are the main components of the gastrointestinal mucus layer. Mucin glycosylation is critical to most intermolecular and intercellular interactions. However, due to the highly complex and heterogeneous mucin glycan structures, the encoded biological information remains largely encrypted. Here we have developed a methodology based on force spectroscopy to identify biologically accessible glycoepitopes in purified porcine gastric mucin (pPGM) and purified porcine jejunal mucin (pPJM). The binding specificity of lectins Ricinus communis agglutinin I (RCA), peanut (Arachis hypogaea) agglutinin (PNA), Maackia amurensis lectin II (MALII), and Ulex europaeus agglutinin I (UEA) was utilized in force spectroscopy measurements to quantify the affinity and spatial distribution of their cognate sugars at the molecular scale. Binding energy of 4, 1.6, and 26 aJ was determined on pPGM for RCA, PNA, and UEA. Binding was abolished by competition with free ligands, demonstrating the validity of the affinity data. The distributions of the nearest binding site separations estimated the number of binding sites in a 200-nm mucin segment to be 4 for RCA, PNA, and UEA, and 1.8 for MALII. Binding site separations were affected by partial defucosylation of pPGM. Furthermore, we showed that this new approach can resolve differences between gastric and jejunum mucins.—Gunning, A. P., Kirby, A. R., Fuell, C., Pin, C., Tailford L. E., Juge, N. Mining the “glycocode”—exploring the spatial distribution of glycans in gastrointestinal mucin using force spectroscopy.

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“…[8][9][10][11] Recently, there has been increasing evidence showing that numerous biological functions are closely related to specific oligosaccharide sequences, leading more and more researchers to study oligosaccharides and then to understand glycan-protein interactions. [12][13][14][15][16] In the past decade, a highly sensitive mass spectrometry technique, particularly electrospray ionization mass spectrometry (ESI-MS), has been successfully used in the structural analysis of both neutral [17,18] and acidic oligosaccharides, such as carrageenan, [19,20] alginate, [21] and glycosaminoglycan-derived oligomers. [22,23] With respect to the oligosaccharides derived from fucoidan, several laboratories [24 -28] have confirmed the structure of oligosaccharides from linear sulfated fucoidan/fucan by mass spectrometry.…”

Section: Introductionmentioning

confidence: 99%

Structural Study of Sulfated Fuco-Oligosaccharide Branched Glucuronomannan fromKjellmaniella crassifoliaby ESI-CID-MS/MS

Liu

et al. 2015

Journal of Carbohydrate Chemistry

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303Downloaded by [University of Otago] at 07:05 18 July 2015 304 J. Wu et al.A polysaccharide was purified from brown alga Kjellmaniella crassifolia, and its precise structure was deduced on the basis of sequence analysis of oligosaccharide fragments obtained from mildly and strongly acidic hydrolysis of the polysaccharide. Electrospray ionization collision-induced dissociation tandem mass spectrometry (ESI-CID-MS/MS) was used to identify the structural features of the resultant oligosaccharides. The side chain oligosaccharides were composed of α-1,3-linked 4-O-sulfated fucose and α-1,3-linked 2,4-O-disulfated fucose, while the backbone oligosaccharides consisted of the disaccharide repeating unit of β-1,4-linked glucuronic acid and α-1,2-linked mannose. Thus, the fucoidan was determined to be a sulfated fuco-oligosaccharide branched glucuronomannan.

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Specificities ofRicinus communisagglutinin 120 interaction with sulfated galactose

Cited by 34 publications

References 36 publications

Community-Based Network Study of Protein-Carbohydrate Interactions in Plant Lectins Using Glycan Array Data

Community-Based Network Study of Protein-Carbohydrate Interactions in Plant Lectins Using Glycan Array Data

Mining the “glycocode”—exploring the spatial distribution of glycans in gastrointestinal mucin using force spectroscopy

Structural Study of Sulfated Fuco-Oligosaccharide Branched Glucuronomannan fromKjellmaniella crassifoliaby ESI-CID-MS/MS

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