Neoglycolipids as probes of oligosaccharide recognition by recombinant and natural mannose-binding proteins of the rat and man
- 15 August 1989
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 262 (1), 131-138
- https://doi.org/10.1042/bj2620131
Abstract
Oligosaccharide recognition by three mammalian mannose-binding proteins was investigated by using as probes a series of structurally characterized neoglycolipids in t.l.c. binding assays. The neoglycolipids were derived from N-linked oligosaccharides of complex, high-mannose and hybrid types and from human milk oligosaccharides and simple di- and tri-saccharides. The three proteins, namely the recombinant carbohydrate-recognition domain of rat mannose-binding Protein A and the multi-subunit forms of rat and human serum mannose-binding proteins, were shown to have in common reactivity with oligosaccharide probes containing one or more non-reducing terminal N-acetylglucosamine residue(s). Substitution with galactose masks reactivity. The three proteins also bound to non-reducing terminal mannose residues in high-mannose-type oligosaccharides, non-reducing terminal fucose residues in the sequence Fuc alpha 1-4(Gal beta 1-3)GlcNAc and non-reducing terminal glucose residues in dextran oligomers; the recombinant binding domain gave consistently weaker binding. The relative reactivities with the various probes differ for each protein. Overall, the reaction patterns of the three mammalian proteins differ from that of the plant lectin concanavalin A, which showed preferential binding to the high-mannose type, weak binding to biantennary complex type and no binding to the fuco-oligosaccharide and simple oligosaccharide probes. As a group, the three mammalian proteins resemble bovine serum conglutinin and behave as lectins with rather broad sugar specificities directed at certain non-reducing terminal N-acetylglucosamine, mannose, glucose and fucose residues, but with subtle differences in fine specificities. These results illustrate the potential of neoglycolipids in studies of oligosaccharide recognition by natural and recombinant proteins of diverse biological systems.This publication has 32 references indexed in Scilit:
- Bovine serum conglutinin is a lectin which binds non-reducing terminal N-acetylglucosamine, mannose and fucose residuesBiochemical Journal, 1989
- Demonstration of carbohydrate-recognition activity in diverse proteins which share a common primary structure motifBiochemical Society Transactions, 1989
- Improved procedure for the construction of neoglycolipids having antigenic and lectin-binding activities, from reducing oligosaccharidesBiochemical Journal, 1988
- Isolation and characterization of endogenous ligands for liver mannan-binding proteinArchives of Biochemistry and Biophysics, 1988
- A human mannose-binding protein is an acute-phase reactant that shares sequence homology with other vertebrate lectins.The Journal of Experimental Medicine, 1988
- Developmental patterning of carbohydrate antigens during early embryogenesis of the chick: expression of antigens of the poly-N-acetyllactosamine seriesDevelopment, 1988
- Isolation and characterization of two distinct mannan-binding proteins from rat serumArchives of Biochemistry and Biophysics, 1988
- Fractionation of Glycopeptides by Affinity Column Chromatography on Concanavalin A-Sepharose1The Journal of Biochemistry, 1975
- Characterization studies on a new lectin found in seeds of Vicia erviliaFEBS Letters, 1975
- Conglutinin and ImmunoconglutininsAdvances in Immunology, 1967