Interactions of concanavalin A with asparagine-linked glycopeptides. Structure/activity relationships of the binding and precipitation of oligomannose and bisected hybrid-type glycopeptides with concanavalin A

L. Bhattacharyya, Curtis F. Brewer

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45 Citations (Scopus)

Abstract

We have recently demonstrated that certain oligomannose and bisected hybrid-type glycopeptides are bivalent for concanavalin A (ConA) binding and that they can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzone, P. & Brewer, C.F. (1987) J. Biol. Chem. 262, 1288-1293]. Two protein-binding sites on each glycopeptide were identified: one on the α(1-6) arm of the core β-mannose residue which binds with high affinity (primary site); the other on the α(1-3) arm of the core β-mannose residue which binds with lower affinity (secondary site). In the present study, we have investigated the relationship between the structures of the primary sites of oligomannose-type glycopeptides and their affinities for ConA. Two mechanisms of binding at the primary sites of oligomannose-type glycopeptides have been identified which account for the 3000-fold increase in affinity of a Man9 glycopeptide relative to that of methyl α-D-mannopyranoside. Changes in the structures and affinities of both the primary and secondary sites are observed to influence the precipitation activities of the glycopeptides. These findings have important consequences for the specificity of ConA binding in solution containing mixtures of the carbohydrates.

Original languageEnglish (US)
Pages (from-to)721-726
Number of pages6
JournalEuropean Journal of Biochemistry
Volume178
Issue number3
StatePublished - 1989

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Glycopeptides
Asparagine
Structure-Activity Relationship
Concanavalin A
Mannose
Lectins
Protein Binding
Precipitates
Binding Sites
Carbohydrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "Interactions of concanavalin A with asparagine-linked glycopeptides. Structure/activity relationships of the binding and precipitation of oligomannose and bisected hybrid-type glycopeptides with concanavalin A",
abstract = "We have recently demonstrated that certain oligomannose and bisected hybrid-type glycopeptides are bivalent for concanavalin A (ConA) binding and that they can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzone, P. & Brewer, C.F. (1987) J. Biol. Chem. 262, 1288-1293]. Two protein-binding sites on each glycopeptide were identified: one on the α(1-6) arm of the core β-mannose residue which binds with high affinity (primary site); the other on the α(1-3) arm of the core β-mannose residue which binds with lower affinity (secondary site). In the present study, we have investigated the relationship between the structures of the primary sites of oligomannose-type glycopeptides and their affinities for ConA. Two mechanisms of binding at the primary sites of oligomannose-type glycopeptides have been identified which account for the 3000-fold increase in affinity of a Man9 glycopeptide relative to that of methyl α-D-mannopyranoside. Changes in the structures and affinities of both the primary and secondary sites are observed to influence the precipitation activities of the glycopeptides. These findings have important consequences for the specificity of ConA binding in solution containing mixtures of the carbohydrates.",
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AU - Brewer, Curtis F.

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AB - We have recently demonstrated that certain oligomannose and bisected hybrid-type glycopeptides are bivalent for concanavalin A (ConA) binding and that they can precipitate the lectin [Bhattacharyya, L., Ceccarini, C., Lorenzone, P. & Brewer, C.F. (1987) J. Biol. Chem. 262, 1288-1293]. Two protein-binding sites on each glycopeptide were identified: one on the α(1-6) arm of the core β-mannose residue which binds with high affinity (primary site); the other on the α(1-3) arm of the core β-mannose residue which binds with lower affinity (secondary site). In the present study, we have investigated the relationship between the structures of the primary sites of oligomannose-type glycopeptides and their affinities for ConA. Two mechanisms of binding at the primary sites of oligomannose-type glycopeptides have been identified which account for the 3000-fold increase in affinity of a Man9 glycopeptide relative to that of methyl α-D-mannopyranoside. Changes in the structures and affinities of both the primary and secondary sites are observed to influence the precipitation activities of the glycopeptides. These findings have important consequences for the specificity of ConA binding in solution containing mixtures of the carbohydrates.

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