- 作者: Albert M. Wu; June H. Wu; Tanuja Singh; Kang-Chang Chu; Willy J. Peumans; Pierre Rouge; Els J.M. Van Damme
- 作者服務機構: Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular Biology and Department of Microbiology and Immunology, College of Medicine, Chang-Gung University Kweishan, Taoyuan, Taiwan; Department of Molecular Biotechnology, Faculty of Agricultural and Applied Biological Sciences, Ghent Univeristy Coupure Links, Gent, Belgium; Sufaces Cellulaires et Signalisation chez les Vegetaux, UMR-CNRS5546, Pole de Biotechnologi vegetale, Castanet Tolosan, France
- 中文摘要: --
- 英文摘要: Morniga M is a jacalin-related and mannose-specific lec-tin isolated from the bark of the mulberry (Morus nigra).In order to understand the function and application ofthis novel lectin,the binding property of Morniga M wasstudied in detail using an enzyme-linked lectinosorbentassay and lectin-glycan inhibition assay with extendedglycan/ligand collection.From the results, it was foundthat the di-,tri-, and oligomannosyl structural units of N-glycans such as those of the bovine α1-acid glycoprotein(gp)and lactoferrin were the most active gps, but not theO-glycans or polysaccharides including mannan fromyeast. The binding affinity of Morniga M for ligands canbe ranked in decreasing order as follows:gps carryingmultiple N-glycans with oligomannosyl residues>>N-glycopeptide with a single trimannosyl core>Tri-Manoligomer【Mana1→6(Man α1→3)Man】, Penta-Man oli-gomer【Manα1→6(Manα1→3)Manα1→6(Mana1→3)Man】≧ Man α1→2,3or6Man>Man>GIcNAc, Glc>>L-Fuc, Gal,GaINAc (inactive),demonstrating the uniquespecificity of this lectin that may not only assist in ourunderstanding of cell surface carbohydrate ligand-lectinrecognition,but also provide informative guidelines forthe application of this structural probe in biotechnologi-cal and clinical regimens, especially in the detection andpurification of N-linked glycans.
- 中文關鍵字: --
- 英文關鍵字: --