Characterization of O-glycan binding lectin from the red alga Hydropuntia eucheumatoides

Le Dinh Hung; Tran Thi Hai Yen; Dinh Thanh Trung

doi:10.15625/1811-4989/16/4/13056

Author affiliations

Authors

Le Dinh Hung Nhatrang Institute of Technology Research and Application-Vietnam Academy of Science and Technology
Tran Thi Hai Yen
Dinh Thanh Trung

DOI:

https://doi.org/10.15625/1811-4989/16/4/13056

Keywords:

Carbohydrate binding specificity, Hydropuntia eucheumatoides, lectin, molecular mass, red alga, stable

Abstract

The red alga, Hydropuntia eucheumatoides is one of the algal genera from which agar is commercially extracted, and is the main source of agar in the world. The lectin HEL from the red alga H. eucheumatoides was isolated by a combination of aqueous ethanol extraction, ethanol precipitation, ion exchange and filtration chromatography. Lectin gave a single band with molecular mass of 17,000 Da in both non-reducing and reducing SDS-PAGE conditions, therefore lectin exists in monomeric form. The hemagglutination activities of HEL were stable over a wide range of pH from 3 to 10, temperature up 60 ^oC and not affected by either the presence of EDTA or addition of divalent cations, indicating that lectin requires no metal for biological activity. The hemagglutination activities of HEL were not inhibited by monosaccharides and glycoproteins, D-glucose, D-mannose, D-galactose, D-xylose, N-acety-D-mannosamine, transferin, fetuin and yeast mannan, but strongly inhibited by monosaccharides containing acetamido groups at equatorial C2 position, such as N-acetyl-galactosamine, N-acetyl-glucosamine, N-acetyl-neuraminic acid and glycoprotein porcine stomach mucin bearing O-glycans. Thus, lectin is specific for O-glycans and may recognize the sequences GalNAcαSer/Thr, GalNAc(α1-3)[Fuc(α1-2)]Gal(β1-4)GlcNAc(β1-3)GalNAc- and GluNAc(α1-4)Gal- under interacting with the acetamido groups at equatorial C2 position of the terminal sugar residues in oligosaccharide structures of O-glycans. The red alga H. eucheumatoides could promise to be a source of valuable lectins for application in biochemistry and biomedicine.

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