The epitope of the H-type 2 trisaccharide recognized by Erythrina corallodendron lectin. Evidence for both attractive polar and strong hydrophobic interactions for complex formation involving a lectin

Lemieux, Raymond U, Ling, Chang-Chun, Sharon, Nathan and Streicher, Hansjorg (2000) The epitope of the H-type 2 trisaccharide recognized by Erythrina corallodendron lectin. Evidence for both attractive polar and strong hydrophobic interactions for complex formation involving a lectin. Israel Journal of Chemistry, 40 (3-4). pp. 167-176. ISSN 0021-2148

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Abstract

Erythrina corallodendron lectin (ECorL), originally regarded as specific for N-acetyllactosamine (LacNAc), shows preferential binding of the II-type 2 human blood group determinant (alpha -L-Fuc-(1-2)-beta -D-Gal-(1-4)-beta -D-GlcNAc-OH). In the present study, various deoxy- and mono-O-methyl derivatives of beta -H-type 2 methyl glycoside and beta -LacNAc methyl glycoside were employed in an enzyme-linked lectin assay to further examine the specificity requirements of ECorL and the contribution of the fucose moiety to the binding of the trisaccharide to the lectin. Based on the relative affinities of the ligands, the X-ray structure of the ECorL/ LacNAc complex, and the site-directed mutagenesis studies of the lectin, the epitope of the II-type 2 trisaccharide recognized by ECorL has been delineated. The fucose moiety is shown to provide a strong hydrophobic interaction at its 2-OH, most likely with Trp 135 of the lectin combining site, in addition to the polar interactions of the key hydroxyl groups at positions 3 and 4 of the galactose and the stacking of the latter residue on Phe131. Comparison of the epitopes of H-type-2-OMe recognized by three other legume lectins, from Galactia tenuiflora, Psophocarpus tetragonolobus, and Ulex europaeus, shows that all four are different, in spite of the high similarity between their tertiary structures. Our findings provide a striking illustration of how a single oligosaccharide can carry different messages for communication with different recognition molecules.

Item Type: Article
Schools and Departments: School of Life Sciences > Chemistry
Depositing User: Hans Streicher
Date Deposited: 06 Feb 2012 19:50
Last Modified: 25 Apr 2012 14:08
URI: http://sro.sussex.ac.uk/id/eprint/22474
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