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Glycobiology Advance Access originally published online on September 21, 2005
Glycobiology 2006 16(1):46-53; doi:10.1093/glycob/cwj038
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography

Kouichi Tachibana2, Sachiko Nakamura3, Han Wang2, Hiroko Iwasaki2,4, Kahori Tachibana2, Kanako Maebara2, Lamei Cheng2, J. Hirabayashi3 and H. Narimatsu1,2

2 Glycogene Function Team and 3 Gzlycostructure Analysis Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan; and 4 Amersham Biosciences KK, 3-25-1 Hyakunincho, Shinjuku-ku, Tokyo 169-0073, Japan

1 To whom correspondence should be addressed; e-mail: h.narimatsu{at}aist.go.jp

Received on June 3, 2005; revised on August 15, 2005; accepted on September 12, 2005

Jacalin, a lectin from the jackfruit Artocarpus integrifolia, has been known as a valuable tool for specific capturing of O-glycoproteins such as mucins and IgA1. Though its sugar-binding preference for T/Tn-antigens is well established, its detailed specificity has not been elucidated. In this study, we prepared a series of mucin-type glycopeptides using human glycosyltransferases, that is, ST6GalNAc1, Core1Gal-T1 and -T2, ß3Gn-T6, and Core2GnT1, and investigated their binding to immobilized Jacalin by frontal affinity chromatography (FAC). As a result, consistent with the previous observation, Jacalin showed high affinity for T-antigen (Core1) and Tn-antigen (alpha N-acetylgalactosamine)-attached peptides. Furthermore, we here show as novel findings that (1) Jacalin also showed significant affinity for Core3 and sialyl-T (ST)-attached peptides, but (2) Jacalin could not bind to Core2, Core6, and sialyl-Tn (STn)-attached peptides. The results were also confirmed by FAC using p-nitrophenyl (pNP)-derivatized saccharides. In conclusion, Jacalin binds to a GalNAc{alpha}1-peptide, in which C6-OH of {alpha}GalNAc is free (i.e., Core1, Tn, Core3, and ST), whereas it cannot recognize a GalNAc{alpha}1-peptide with a substitution at the C6 position (i.e., Core2, Core6, and STn). These findings provide useful information when applying jacalin for functional analysis of mucin-type glycoproteins and glycopeptides.

Key words: glycopeptide / Jacalin / mucin / O-glycan


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