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 (MW<3.0×10 3)≫monomeric Tn to tri- Tn glycopeptides⋙other GalNAcα/β-related structural units>Gal and Galα- or β-linked ligands, demonstrating the essential role of the polyvalency of Tn glycotopes in the enhancement of the binding.
Original language | English |
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Pages (from-to) | 51-58 |
Number of pages | 8 |
Journal | FEBS Letters |
Volume | 562 |
Issue number | 1-3 |
DOIs | |
State | Published - 26 03 2004 |
Keywords
- Carbohydrate specificity
- D-Fuc, D-fucopyranose
- GalNAc, 2-acetamido-2-deoxy-D-galactopyranose
- Glc, D-glucopyranose
- Glycoprotein binding
- L-Ara, L-arabinose
- Lectin
- Multivalent effect
- Polyvalency
- Sugars: Gal, D-galactopyranose
- Vicia villosa B