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Glycobiology Advance Access originally published online on February 6, 2003
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Glycobiology, 2003, Vol. 13, No. 6 479-486
© 2003 Oxford University Press

Studies on Gal{alpha}3-binding proteins: comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin

Susann Teneberg1,2, Björn Alsén2, Jonas Ångström2, Harry C. Winter3 and Irwin J. Goldstein3

2 Institute of Medical Biochemistry, Göteborg University, P.O. Box 440, SE 405 30 Göteborg, Sweden
3 Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606, USA

Received on December 6, 2002; revised on January 16, 2003; accepted on January 21, 2003

The carbohydrate binding preferences of the Gal{alpha}3Galß4 GlcNAc-binding lectins from Marasmius oreades and Euonymus europaeus were examined by binding to glycosphingolipids on thin-layer chromatograms and in microtiter wells. The M. oreades lectin bound to Gal{alpha}3-terminated glycosphingolipids with a preference for type 2 chains. The B6 type 2 glycosphingolipid (Gal{alpha}3[Fuc{alpha}2]Galß4GlcNAcß3Galß4Glcß1Cer) was preferred over the B5 glycosphingolipid (Gal{alpha}3Galß4GlcNAcß3Galß4Glcß1Cer), suggesting that the {alpha}2-linked Fuc is accommodated in the carbohydrate binding site, providing additional interactions. The lectin from E. europaeus had broader binding specificity. The B6 type 2 glycosphingolipid was the best ligand also for this lectin, but binding to the B6 type 1 glycosphingolipid (Gal{alpha}3[Fuc{alpha}2]Galß3GlcNAcß3Galß4Glcß1Cer) was also obtained. Furthermore, the H5 type 2 glycosphingolipid (Fuc{alpha}2Galß4GlcNAcß3Galß4Glcß1Cer), devoid of a terminal {alpha}3-linked Gal, was preferred over the the B5 glycosphingolipid, demonstrating a significant contribution to the binding affinity by the {alpha}2-linked Fuc. The more tolerant nature of the lectin from E. europaeus was also demonstrated by the binding of this lectin, but not the M. oreades lectin, to the x2 glycosphingolipid (GalNAcß3Galß4GlcNAcß3Galß4Glcß1Cer) and GlcNAcß3Galß4GlcNAcß3Galß4Glcß1Cer. The A6 type 2 glycosphingolipid (GalNAc{alpha}3[Fuc{alpha}2]Galß4GlcNAcß3Galß4Glcß1Cer) and GalNAc{alpha}3Galß4GlcNAcß3Galß4Glcß1-Cer were not recognized by the lectins despite the interaction with B6 type 2 glycosphingolipid and the B5 glycosphingolipid. These observations are explained by the absolute requirement of a free hydroxyl in the 2-position of Gal{alpha}3 and that the E. europaea lectin can accommodate a GlcNAc acetamido moiety close to this position by reorienting the terminal sugar, whereas the M. oreades lectin cannot.

1 To whom correspondence should be addressed; e-mail: susann.teneberg{at}medkem.gu.se


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