Glycobiology Advance Access originally published online on March 15, 2006
Glycobiology 2006 16(6):524-537; doi:10.1093/glycob/cwj102
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Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine specificity and the effect of naturally clustered ligand presentation
2 Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology and 3 Department of Microbiology and Immunology, Chang-Gung University, Kwei-san, Tao-yuan, 333, Taiwan; and 4 Faculty of Veterinary Medicine, Institute of Physiological Chemistry, Ludwig-Maximilians-University, Veterinärstrasse 13, D-80539 Munich, Germany
1 To whom correspondence should be addressed; e-mail: amwu{at}mail.cgu.edu.tw
Received on December 25, 2005; revised on March 10, 2006; accepted on March 12, 2006
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 (ELLSA) and inhibition assays with the prototype 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 Galß1-3/4GlcNAc (I/II) and multiantennary N-glycans with II termini. Their reactivities, on a nanogram basis, were up to 4.3 x 102, 3.2 x 102, 2.5 x 102, and 1.7 x 104 times higher than monomeric Galß1-3/4GlcNAc (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 (Gal1-3Gal ß1-4GlcNAc), B-active IIß1-3L (Gal1-3Galß1-4GlcNAc ß1-3Galß1-4Glc), and Tri-II were the best. It is concluded that (1) Galß1-3/4GlcNAc and other Galß1-related oligosaccharides with 1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted ß-galactoside, especially with -anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIß1-3L); (3) the preference within ß-anomeric positioning is Galß1-4 
Galß1-3 > Galß1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding. These results are important for the systematic comparison of ligand selection in this family of adhesion/growth-regulatory effectors with potential for medical applications.
Key words: glycoprotein / lectin / N-glycans / O-glycans / sialylation
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