A novel lectin (morniga M) from mulberry (Morus nigra) bark recognizes oligomannosyl residues in N-Glycans |
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Authors: | Albert M. Wu June H. Wu Tanuja Singh Kang-Chuang Chu Willy J. Peumans Pierre Rougé Els J. M. Van Damme |
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Affiliation: | (1) Department of Microbiology and Immunology, College of Medicine, Chang-Gung University, Kweishan, Taoyuan, Taiwan;(2) Department of Molecular Biotechnology, Faculty of Agricultural and Applied Biological Sciences, Ghent University, Coupure Links, Gent, Belgium;(3) Surfaces Cellulaires et Signalisation chez les Végétaux, UMR-CNRS 5546, Pôle de Biotechnologie végétale, Castanet Tolosan, France;(4) Glyco-Immunochemistry Research Laboratory Institute of Molecular and Cellular Biology, Chang-Gung University, 333 Kweishan, Taoyuan, Taiwan |
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Abstract: | Morniga M is a jacalin-related and mannose-specific lectin isolated from the bark of the mulberry (Morus nigra). In order to understand the function and application of this novel lectin, the binding property of Morniga M was studied in detail using an enzyme-linked lectinosorbent assay and lectin-glycan inhibition assay with extended glycan/ligand collection. From the results, it was found that the di-, tri-, and oligomannosyl structural units of N-glycans such as those of the bovine1-acid glycoprotein (gp) and lactoferrin were the most active gps, but not the O-glycans or polysaccharides including mannan from yeast. The binding affinity of Morniga M for ligands can be ranked in decreasing order as follows: gps carrying multiple N-glycans with oligomannosyl residues >> N-glycopeptide with a single trimannosyl core > Tri-Man oligomer [Man1 6(Man 1 3) Man], Penta-Man oligomer [Man1 6(Man1 3)Man1 6(Man1 3) Man] Man 1 2, 3 or 6 Man > Man > GlcNAc, Glc >>L-Fuc, Gal, GalNAc (inactive), demonstrating the unique specificity of this lectin that may not only assist in our understanding of cell surface carbohydrate ligand-lectin recognition, but also provide informative guidelines for the application of this structural probe in biotechnological and clinical regimens, especially in the detection and purification of N-linked glycans. |
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Keywords: | Morus nigra Morniga M Carbohydrate specificity Jacalin-related lectin Glycoproteins Oligomannosyl residues N-glycans |
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