Specificities of Ricinus communis agglutinin 120 interaction with sulfated galactose |
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Authors: | Wang Yufeng Yu Guangli Han Zhangrun Yang Bo Hu Yannan Zhao Xia Wu Jiandong Lv Youjing Chai Wengang |
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Affiliation: | aShandong Provincial Key Laboratory of Glycoscience and Glycoengineering, and Key Laboratory of Marine Drugs, Ministry of Education, Ocean University of China, Qingdao 266003, China;bGlycosciences Laboratory, Department of Medicine, Imperial College London, Northwick Park & St Mark’s Campus, Harrow, Middlesex HA1 3UJ, United Kingdom |
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Abstract: | Lectins are used extensively as research tools to detect and target specific oligosaccharide sequences. Ricinus communis agglutinin I (RCA120) recognizes non-reducing terminal β-d-galactose (Galβ) and its specificities of interactions with neutral and sialylated oligosaccharides have been well documented. Here we use carbohydrate arrays of sulfated Galβ-containing oligosaccharide probes, prepared from marine-derived galactans, to investigate their interactions with RCA120. Our results showed that RCA120 binding to Galβ1–4 was enhanced by 2-O- or 6-O-sulfation but abolished by 4-O-sulfation. The results were corroborated with competition experiments. Erythrina cristagalli lectin is also a Galβ-binding protein but it cannot accommodate any sulfation on Galβ. |
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Keywords: | Abbreviations: RCA120, Ricinus communis agglutinin ECL, Erythrina cristagalli lectin DHPE, 1,2-dihexadecyl-sn-glycero-3-phosphoethanolamine NGL, neoglycolipid Gal, galactose Glc, glucose GlcNAc, N-acetylglucosamine GalNAc, N-acetylgalactosamine Fuc, fucose NeuAc, N-acetylneuaminic acid anGal, 3,6-anhydro-α-galactopyranose LNnT, lacto-N-neotetraose LNT, lacto-N-tetraose G4, galactotetraose LSTc, LS-tetrasaccharide C A4, neoagar-tetrasaccharide dsK, desulfatedκ&part -carrageenan dsL, desulfated λ-carrageenan HBS, HEPES buffered solution HBST, HBS containing 0.05% Tween 20 |
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