Journal of Biochemistry Advance Access originally published online on July 25, 2007
Journal of Biochemistry 2007 142(4):459-469; doi:10.1093/jb/mvm153
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© 2007 The Japanese Biochemical Society.
Systematic Comparison of Oligosaccharide Specificity of Ricinus communis Agglutinin I and Erythrina Lectins: a Search by Frontal Affinity Chromatography
1Lectin Application and Analysis Team, Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Central 2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568; 2Fine Chemical & Foods Laboratories, J-Oil Mills, Inc., 11, Kagetoricho, Totsuka-ku, Yokohama 245-0064, Japan; 3Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel and 4Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa 229-0195, Japan
*To whom correspondence should be addressed. Lectin Application and Analysis Team, Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Central 2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568, Japan. Tel: +81-29-861-3124, Fax: +81-29-861-3125, E-mail: jun-hirabayashi{at}aist.go.jp
Received June 18, 2007; Accepted July 20, 2007
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Abstract |
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Ricinus communis agglutinin I (RCA120) is considered a versatile tool for the detection of galactose-containing oligosaccharides. However, possible contamination by the highly toxic isolectin ‘ricin’ has become a critical issue for RCA120's continued use. From a practical viewpoint, it is necessary to find an effective substitute for RCA120. For this purpose, we examined by means of frontal affinity chromatography over 100 lectins which have similar sugar-binding specificities to that of RCA120. It was found that Erythrina cristagalli lectin (ECL) showed the closest similarity to RCA120. Both lectins prefer Galß1-4GlcNAc (type II) to Galß1-3GlcNAc (type I) structures, with increased affinity for highly branched N-acetyllactosamine-containing N-glycans. Their binding strength significantly decreased following modification of the 3-OH, 4-OH and 6-OH of the galactose moiety of the disaccharide, as well as the 3-OH of its N-acetylglucosamine residue. Several differences were also observed in the affinity of the two lectins for various other ligands, as well as effects of bisecting GlcNAc and terminal sialylation. Although six other Erythrina-derived lectins have been reported with different amino acid sequences, all showed quite similar profiles to that of ECL, and thus, to RCA120. Erythrina lectins can therefore serve as effective substitutes for RCA120, taking the above differences into consideration.
Key Words: Erythrina lectins, frontal affinity chromatography, galactose-binding lectin, Ricinus communis agglutinin, sugar-binding specificity
Abbreviations: ASF, asialofetuin; ASL, Asialolactoferrin; ECafL, Erythrina caffra lectin; ECL, commercial Erythrina cristagalli lectin; ECorL, Erythrina corallodendron lectin; ECriL, Erythrina cristagalli lectin; EFlaL, Erythrina flabelliformis lectin; ELysL, Erythrina lysistemon lectin; EVesL, Erythrina verseptillo lectin; FAC, frontal affinity chromatography; PA, pyridylaminated; pNP, p-nitrophenyl; RCA120, Ricinus communis agglutinin I; SBA, Glycine max agglutinin
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