The lectin from the algae Udotea petiolata: isolation, characterization and sugar binding properties.

In the present work, we describe a novel lectin which is specific for poly-N-acetyllactosamine sequences on complex N- and O-linked carbohydrate chains. This lectin was extracted and purified from the algae Udotea petiolata. The purified lectin is a monomer with a molecular mass of 65,000 and an isoelectric point of 5.6. It agglutinates normal, neuraminidase and protease-treated erythrocytes from humans irrespectively of the blood group (A, B and O) and animal erythrocytes. The Udotea lectin displays a strong mitogenic effect on human lymphocytes, especially T-cells. This lectin binds to the human serum plasma protein 8S alpha 3-glycoprotein with high affinity (ID50 0.02 microM); other species of human serum glycoproteins exhibiting a similar preponderance of complex type N-glycosylation showed also high binding capacities in the order 9.5 S alpha 1-glycoprotein greater than alpha 2-macroglobulin = beta 2 glycoprotein = immunoglobulin A greater than asialofetuin greater than alpha 1-acid glycoprotein and mucin glycopeptide (from amnion fluid). Monosaccharides and disaccharides tested do not bind to the lectin. This novel lectin will be useful for identification of N- and O-linked glycans rich in poly-N-acetyllactosamine.