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Glycobiology Advance Access published online on February 13, 2009
Glycobiology, 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 Hirabayashi*

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

* To whom correspondence should be addressed: Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Central 2, 1-1-1 Umezono, Ibaraki 305-8568, Japan. E-mail: jun-hirabayashi{at}aist.go.jp, Phone: +81-29-861-3124, Fax: +81-29-861-3125

Received on December 17, 2008; 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 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: lectin / core-fucose / frontal affinity chromatography / specificity / alpha-fetoprotein


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