Fine carohydrate recognition of Agaricus bisporus lectin

FERNANDO JOSE IRAZOQUI; VOZARI-HAMPE M,; LARDONE RD,; SENDRA VG,; VILLARREAL M,; MONTICH G,; CLAUSEN H,; NORES GA,

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Elsevier

Año: 2005 vol. 336 p. 14 - 14

0006-291X

font face="AdvEPSTIM" size="1"> 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 speci.c carbohydrate topology. Here, we describe the .ne carbohydrate speci.city 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