Fine carbohydrate recognition of Euphorbia milii lectin.

Abstract

Glycans are key structures involved in biological processes such as cell attachment, migration, and invasion. Information coded on cell-surface glycans is frequently deciphered by proteins, as lectins, that recognize specific carbohydrate topology. Here, we describe the fine carbohydrate specificity of Euphorbia milii lectin (EML). Competitive assays using various sugars showed that GalNAc was the strongest inhibitor, and that the hydroxyl axial position of C4 and acetamido on C2 of GalNAc are critical points of EML recognition. A hydrophobic locus adjacent to GalNAc is also an important region for EML binding. Direct binding assays of EML revealed a stereochemical requirement for a structure adjacent to terminal GalNAc, showing that GalNAc residue is a necessary but not sufficient condition for EML interaction. The capacity of EML to bind epithelial tumor cells makes it a potentially useful tool for study of some over-expressed GalNAc glycoconjugates.

• Authors: Fernando J Irazoqui, Magdolna M Vozari-Hampe, Ricardo D Lardone, Marcos A Villarreal, Victor G Sendra, Guillermo G Montich, Vera M Trindade, Henrik Clausen, Gustavo A Nores
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 336 Issue 1 Pg. 14-21 (Oct 14 2005) ISSN: 0006-291X [Print] United States
• PMID: 16122701 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Lectins

Topics

• Carbohydrate Conformation
• Carbohydrate Metabolism
• Carbohydrate Sequence
• Chromatography, Thin Layer
• Electrophoresis, Polyacrylamide Gel
• Euphorbia (chemistry)
• Lectins (metabolism)
• Models, Molecular
• Molecular Sequence Data
• Stereoisomerism