Specificities of Ricinus communis agglutinin 120 interaction with sulfated galactose.

Yufeng Wang, Guangli Yu, Zhangrun Han, Bo Yang, Yannan Hu, Xia Zhao, Jiandong Wu, Youjing Lv, Wengang Chai

Shandong Provincial Key Laboratory of Glycoscience and Glycoengineering, and Key Laboratory of Marine Drugs, Ministry of Education, Ocean University of China, Qingdao, China.

FEBS letters 2011 Dec 15

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Lectins are used extensively as research tools to detect and target specific oligosaccharide sequences. Ricinus communis agglutinin I (RCA(120)) 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 RCA(120). Our results showed that RCA(120) 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. Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Yufeng Wang, Guangli Yu, Zhangrun Han, Bo Yang, Yannan Hu, Xia Zhao, Jiandong Wu, Youjing Lv, Wengang Chai. Specificities of Ricinus communis agglutinin 120 interaction with sulfated galactose. FEBS letters. 2011 Dec 15;585(24):3927-34