Formation of highly ordered cross-linked lattices between asparagine-linked oligosaccharides and lectins observed by electron microscopy

L Bhattacharyya,M I Khan,J Fant,C F Brewer

doi:10.1016/s0021-9258(18)80095-3

L Bhattacharyya, M I Khan + Show 2 more

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https://doi.org/10.1016/s0021-9258(18)80095-3

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Abstract

The interaction of asparagine-linked carbohydrates (N-linked) with carbohydrate binding proteins called lectins has been demonstrated to be involved in a variety of cellular recognition processes. Certain N-linked carbohydrates have been shown to be multivalent and capable of binding, cross-linking, and precipitating lectins (Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., and Brewer, C. F. (1987) J. Biol. Chem. 262, 1288-1293; Bhattacharyya, L., Haraldsson, M., and Brewer, C. F. (1987) J. Biol. Chem. 262, 1294-1299; Bhattacharyya, L., Haraldsson, M., and Brewer, C. F. (1988) Biochemistry 27, 1034-1041). Recent data have further suggested that certain oligomannose and bisected hybrid-type N-linked glycopeptides form homogeneous cross-linked lattices with concanavalin A (Bhattacharyya, L., Khan, M. I., and Brewer, C. F. (1988) Biochemistry 27, 8762-8767). In the present study, evidence has been obtained from electron microscopy for the formation of highly ordered and distinct lattices for two bivalent complex type oligosaccharides cross-linked with soybean lectin (Glycine max) and isolectin A from Lotus tetragonolobus, respectively. The results indicate a new source of specificity for interactions of N-linked carbohydrates with lectins, namely their ability to form highly ordered homogeneous aggregates.

Highlights

Formation of Highly Ordered Cross-linked Lattices between Asparagine-linked which are multivalent carbohydrate binding proteins present in a wide variety of organisms
New York10461 peptide and a series of oligomannose-type glycopeptideswith closely related structures which bind as divalent ligands and Precipitate with concanavalin A, a D-glucose/D-mannose specific lectin (8), the quantitative precipitation analyses data indicate that each glycopeptide forms a homogeneous crosslinked lattice with the protein, even from solutions containing binary mixtures of the carbohydrates (12, 13)
Heterogeneous complexes containing two different glycopeptides bound to the lectin fail to precipitate and exist only as soluble com

Summary

Introduction

Formation of Highly Ordered Cross-linked Lattices between Asparagine-linked which are multivalent carbohydrate binding proteins present in a wide variety of organisms. Oligosaccharides andLectins observed that these cross-linking interactions lead to an im- New York10461 peptide and a series of oligomannose-type glycopeptideswith closely related structures which bind as divalent ligands and Precipitate with concanavalin A, a D-glucose/D-mannose specific lectin (8), the quantitative precipitation analyses data indicate that each glycopeptide forms a homogeneous crosslinked lattice with the protein, even from solutions containing binary mixtures of the carbohydrates (12, 13).

Results

Conclusion