Glycobiology Advance Access published online on February 6, 2003
Glycobiology, doi:10.1093/glycob/cwg049
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© 2003 Oxford University Press
ORIGINAL ARTICLES
1 Institute of Medical Biochemistry, Göteborg University, P.O. Box 440, SE 405 30 Göteborg, Sweden The carbohydrate binding preferences of the Gal 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 The A6 type 2 glycosphingolipid (GalNAc
Revised on January 16, 2003
Accepted on January 21, 2003
Studies on Gal
3-binding proteins: Comparison of the glycosphingolipid binding specificities of Marasmius oreades lectin and Euonymus europaeus lectin
2 Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606
3Gal
4GlcNAc binding lectins from Marasmius oreades and Euonumus europaeus were examined by binding to glycosphingolipids on thin-layer chromatograms and in microtiter wells. The M. oreades lectin bound to Gal3-terminated glycosphingolipids with a preference for type 2 chains. The B6 type 2 glycosphingolipid (Gal3(Fuc2)Gal4GlcNAc3Gal4Glc1Cer) was preferred over the B5 glycosphingolipid (Gal3Gal4GlcNAc3Gal4Glc1Cer), suggesting that the 2-linked Fuc is accommodated in the carbohydrate binding site providing additional interactions.3(Fuc2)Gal3GlcNAc3Gal4Glc1Cer) was also obtained. Furthermore, the H5 type 2 glycosphingolipid (Fuc2Gal4GlcNAc3Gal4Glc1Cer), devoid of a terminal 3-linked Gal, was preferred over the the B5 glycosphingolipid, demonstrating a significant contribution to the binding affinity by the 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 (GalNAc3Gal4GlcNAc3Gal4Glc1Cer) and GlcNAc3Gal4GlcNAc3Gal4Glc1Cer.3(Fuc2)Gal4GlcNAc3Gal4Glc1Cer or GalNAc3Gal4GlcNAc3Gal4Glc1Cer 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 Gal3 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.
Marasmius oreades lectin, Euonymus europaeus lectin, glycosphingolipid binding, Gal3Gal epitope
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