Specificities of Ricinus communis agglutinin 120 interaction with sulfated galactose

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• 作者：Yufeng  ; Wang^a ; Guangli  ; Yu^a ;   ; ^{glyu@ouc.edu.cn} ; Zhangrun  ; Han^a ; Bo  ; Yang^a ; Yannan  ; Hu^a ; Xia  ; Zhao^a ; Jiandong  ; Wu^a ; Youjing  ; Lv^a ; Wengang  ; Chai^a ;   ; ^b ;   ; ^{w.chai@imperial.ac.uk}
• 关键词：Galactan oligosaccharide ; Neoglycolipid ; Carbohydrate microarray ; Ricinus communis agglutinin I
• 刊名：FEBS Letters
• 出版年：2011
• 出版时间：15 December 2011
• 年：2011
• 卷：585
• 期：24
• 页码：3927-3934
• 全文大小：793 K

文摘

Lectins are used extensively as research tools to detect and target specific oligosaccharide sequences. Ricinus communis agglutinin I (RCA₁₂₀) recognizes non-reducing terminal ¦Â-d-galactose (Gal¦Â) and its specificities of interactions with neutral and sialylated oligosaccharides have been well documented. Here we use carbohydrate arrays of sulfated Gal¦Â-containing oligosaccharide probes, prepared from marine-derived galactans, to investigate their interactions with RCA₁₂₀. Our results showed that RCA₁₂₀ binding to Gal¦Â1? 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 Gal¦Â-binding protein but it cannot accommodate any sulfation on Gal¦Â.