Journal of Biochemistry Advance Access originally published online on July 11, 2006
Journal of Biochemistry 2006 140(2):285-291; doi:10.1093/jb/mvj148
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© 2006 The Japanese Biochemical Society.
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Comparative Analysis by Frontal Affinity Chromatography of Oligosaccharide Specificity of GlcNAc-Binding Lectins, Griffonia simplicifolia Lectin-II (GSL-II) and Boletopsis leucomelas Lectin (BLL)
1 Glycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, AIST Tsukuba Central 2, 1-1-1, Umezono, Tsukuba, Ibaraki 305-8568; 2 Fine Chemical & Foods Laboratories, J-OIL MILLS, INC., 11, Kagetoricho, Totsuka-ku, Yokohama 245-0064; and 3 Cellular biochemistry, School of Food and Nutritional Sciences, University of Shizuoka, 52-1, Yada, Shizuoka 422-8526
* To whom correspondence should be addressed. Tel: +81-29-861-3124, Fax: +81-29-861-3125, E-mail: jun-hirabayashi{at}aist.go.jp
Lectin-based structural glycomics requires a search for useful lectins and their biochemical characterization to profile complex features of glycans. In this paper, two GlcNAc-binding lectins are reported with their detailed oligosaccharide specificity. One is a classic plant lectin, Griffonia simplicifolia lectin-II (GSL-II), and the other is a novel fungal lectin, Boletopsis leucomelas lectin (BLL). Their sugar-binding specificity was analyzed by frontal affinity chromatography using 146 glycans (125 pyridylaminated and 21 p-nitrophenyl saccharides). As a result, it was found that both GSL-II and BLL showed significant affinity toward complex-type N-glycans, which are either partially or completely agalactosylated. However, their branch-specific features differed significantly: GSL-II strongly bound to agalacto-type, tri- or tetra-antennary N-glycans with its primary recognition of a GlcNAc residue transferred by GlcNAc-transferase IV, while BLL preferred N-glycans with fewer branches. In fact, the presence of a GlcNAc residue transferred by GlcNAc-transferase V abolishes the binding of BLL. Thus, GSL-II and BLL forms a pair of complementally probes to profile a series of agalacto-type N-glycans.
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