Polyvalency of Tn (GalNAcα1→Ser/Thr) glycotope as a critical factor for Vicia villosa B4 and glycoprotein interactions
- 26 March 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 562 (1-3) , 51-58
- https://doi.org/10.1016/s0014-5793(04)00180-2
Abstract
Vicia villosa B4 (VVL-B4) is an important lectin for detecting exposed Tn (GalNAcα1-Ser/Thr) determinants on cancer cells. In order to elucidate the binding factors involved in VVL-B4 and glycotope interaction, the binding properties of this lectin were analyzed by enzyme-linked lectinosorbent and inhibition assays. From the results, it is concluded that the most critical factor affecting VVL-B4 binding is polyvalency at the α anomer of Gal with –NH CH3CO at carbon-2 (Tn epitope), which enhances the reactivity by 3.3×105 times over monovalent Gal. The reactivities of glycotopes can be ranked as follows: high density Tn cluster≫Tn glycopeptides (MWGal and Galα- or β-linked ligands, demonstrating the essential role of the polyvalency of Tn glycotopes in the enhancement of the bindingKeywords
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