Polyvalency of Tn (GalNAcα1→Ser/Thr) glycotope as a critical factor for Vicia villosa B4 and glycoprotein interactions

Albert M. Wu*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

38 Scopus citations


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 languageEnglish
Pages (from-to)51-58
Number of pages8
JournalFEBS Letters
Issue number1-3
StatePublished - 26 03 2004


  • 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


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