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Glycobiology Advance Access originally published online on February 13, 2009
Glycobiology 2009 19(5):527-536; doi:10.1093/glycob/cwp016
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Comparative analysis of core-fucose-binding lectins from Lens culinaris and Pisum sativum using frontal affinity chromatography

Hiroaki Tateno, Sachiko Nakamura-Tsuruta and Jun Hirabayashi1

Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Central 2, 1-1-1 Umezono, Ibaraki 305-8568, Japan

1 To whom correspondence should be addressed: Tel: +81-29-861-3124; Fax: +81-29-861-3125; e-mail: jun-hirabayashi{at}aist.go.jp

Received on December 17, 2008; revised on February 1, 2009; accepted on February 5, 2009

Lens culinaris lectin (LCA) is a useful probe for the detection in serum of a core-fucosylated alpha-fetoprotein, called AFP-L3 fraction, which is a well-known marker for the diagnosis and prognosis of hepatocellular carcinoma. Here we performed a systematic quantitative interaction analysis of LCA and its close homolog, Pisum sativum lectin (PSA), by frontal affinity chromatography with 143 pyridylaminated (PA) glycans including a series of core-fucosylated glycans. Both lectins showed binding affinity to core-fucosylated, mono- and bi-antennary N-glycans, but not to their tri- and tetra-antennary forms, indicating that the addition of the GlcNAc residue at the N-acetylglucosaminyltransferase IV position abrogates the binding affinity. However, their specificities are distinguishable: while LCA showed the highest affinity to the core-fucosylated, agalactosylated, bi-antennary N-glycan (Ka = 1.1 x 105 M–1), PSA showed the highest affinity to the core-fucosylated, trimannosyl structure (Ka = 1.2 x 105 M–1). Glycan-binding specificities of LCA and PSA were also analyzed by glycoconjugate microarray compared to other core-fucose-binding lectins from Aspergillus oryzae (AOL) and Aleuria auratia (AAL). LCA and PSA bound specifically to core fucose, whereas AOL and AAL exhibited broad specificity to fucosylated glycans. These results explain why LCA is appropriate as a specific probe for AFP-L3, which mainly contains a core-fucosylated, biantennary N-glycan, but not its highly branched forms.

Key words: alpha-fetoprotein / core fucose / frontal affinity chromatography / lectin / specificity


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