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Polyvalency of Tn (GalNAcalpha1-->Ser/Thr) glycotope as a critical factor for Vicia villosa B4 and glycoprotein interactions.

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chemistry, Vicia, metabolism, Plant Lectins, Oligosaccharides, Neoplasms, N-Acetylneuraminic Acid, Humans, Glycoproteins, Carbohydrate Sequence, Binding Sites, Antigens, Tumor-Associated, Carbohydrate, Animals

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      Vicia villosa B(4) (VVL-B(4)) is an important lectin for detecting exposed Tn (GalNAcalpha1-Ser/Thr) determinants on cancer cells. In order to elucidate the binding factors involved in VVL-B(4) 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-B(4) binding is polyvalency at the alpha anomer of Gal with -NH CH(3)CO at carbon-2 (Tn epitope), which enhances the reactivity by 3.3x10(5) times over monovalent Gal. The reactivities of glycotopes can be ranked as follows: high density Tn cluster >Tn glycopeptides (MW<3.0x10(3) > monomeric Tn to tri- Tn glycopeptides > other GalNAcalpha/beta-related structural units>Gal and Galalpha- or beta-linked ligands, demonstrating the essential role of the polyvalency of Tn glycotopes in the enhancement of the binding.

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