Glycobiology Advance Access published online on March 15, 2006
Glycobiology, doi:10.1093/glycob/cwj102
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1 Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology, Chang-Gung University, Kwei-san, Tao-yuan, 333, Taiwan
* To whom correspondence should be addressed. Cell surface glycans are functional docking sites for tissue lectins such as the members of the galectin family. This interaction triggers a wide variety of responses; hence, there is a keen interest in defining its structural features. Toward this aim, we have used enzyme-linked lectinosorbent and inhibition assays with the proto-type rat galectin-5 and panels of free saccharides and glycoconjugates. Among 45 natural glycans tested for lectin binding, galectin-5 reacted best with glycoproteins (gps) presenting a high density of Gal
Received December 25, 2005
Revised March 10, 2006
Accepted March 12, 2006
Article
Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine-specificity and the effect of naturally clustered ligand presentation
Albert M. Wu 1 *,
Tanuja Singh 1,
June H. Wu 2,
Martin Lensch 3,
Sabine André 3,
and
Hans-Joachim Gabius 3
2 Department of Microbiology and Immunology, Chang-Gung University, Kwei-san, Tao-yuan, 333, Taiwan
3 Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstrasse 13, D-80539 Munich, Germany
Albert M. Wu, E-mail: amwu{at}mail.cgu.edu.tw
Abstract 
1-3/4GlcNAc (I/II) and multi-antennary N-glycans with II termini. Their reactivities, on a nanogram basis, were up to 4.3x102, 3.2x102, 2.5x102 and 1.7x104 times higher than monomeric Gal1-3/4GlcNAc (I/II), triantennary-II (Tri-II) and Gal, respectively. Galectin-5 also bound well to several blood-group type B (Gal
1-3Gal)- and A (GalNAc1-3Gal)-containing gps. It reacted weakly or not at all with tumor-associated Tn (GalNAc1-Ser/Thr) and sialylated gps. Among the mono-, di- and oligosaccharides and mammalian glycoconjugates tested, blood group B-active II (Gal1-3Gal1-4GlcNAc), B-active II1-3L (Gal1-3Gal1-4GlcNAc 1-3Gal1-4Glc) and Tri-II were the best. It is concluded that: (a) Gal1-3/4GlcNAc and other Gal1-related oligosaccharides with 1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (b) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted -galactoside, especially with -anomeric extension at the non-reducing end, e. g. human blood group B-active II and B-active II1-3L; (c) the preference within -anomeric positioning is Gal1-4 
Gal1-3 > Gal1-6; (d) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding. These results are an important step in the systematic comparison of ligand selection in this family of adhesion/growth-regulatory effectors with potential for medical applications.
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