A comparison of the fine saccharide-binding specificity of Dioclea grandiflora lectin and concanavalin A

Dipti Gupta, Stefan Oscarson, T. Shantha Raju, Pamela Stanley, Eric J. Toone, Curtis F. Brewer

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

The lectin from the seeds of Dioclea grandiflora (DGL) is a Man/Glc-specific tetrameric protein with physical and saccharide-binding properties reported to be similar to that of the-jack bean lectin concanavalin A (ConA). Unlike other plant lectins, both DGL and ConA bind with high affinity to the core trimannoside moiety, 3,6-di-O-(α-D-mannopyranosyl)-α-D-mannopyranoside, which is present in all asparagine-linked carbohydrates. in the present study, hemagglutination inhibition techniques have been used to investigate binding of DGL and ConA to a series of mono- and dideoxy analogs of methyl 3,6-di-O-(α-D-mannopyranosyl)-α-D-mannopyranoside and to a series of asparagine-linked oligomannose and complex oligosaccharides and glycopeptides. The results indicate that both DGL and ConA recognize epitopes on all three residues of the trimannoside: the 3-, 4-, and 6-hydroxyl groups of the α(1-6)Man residue, the 3-hydroxyl group of the α(1-3)Man residue, and the 2- and 4-hydroxyl groups of the central Man residue of the core trimannoside. However, unlike ConA, DGL does not bind to biantennary complex carbohydrates. This was confirmed by showing that biantennary complex glycopeptides do not bind to a DGL-Sepharose affinity column. Unlike ConA, DGL does not show enhanced affinity for a large N-linked oligomannose carbohydrate (Man9 glycopeptide) relative to the trimannoside. Thus, DGL and ConA share similar epitope recognition of the core trimannoside moiety. However, they exhibit differences in their fine specificities for larger N-linked oligomannose and complex carbohydrates.

Original languageEnglish (US)
Pages (from-to)320-326
Number of pages7
JournalEuropean Journal of Biochemistry
Volume242
Issue number2
StatePublished - 1996

Fingerprint

Dioclea
Concanavalin A
Glycopeptides
Carbohydrates
Hydroxyl Radical
Asparagine
Mannose
Lectins
Epitopes
Plant Lectins
Jacks
Hemagglutination
Dioclea grandiflora lectin
Oligosaccharides
Sepharose
Seed
Seeds

Keywords

  • Carbohydrate
  • Cross-linking
  • Glycopeptide
  • Lectin
  • Specificity

ASJC Scopus subject areas

  • Biochemistry

Cite this

A comparison of the fine saccharide-binding specificity of Dioclea grandiflora lectin and concanavalin A. / Gupta, Dipti; Oscarson, Stefan; Raju, T. Shantha; Stanley, Pamela; Toone, Eric J.; Brewer, Curtis F.

In: European Journal of Biochemistry, Vol. 242, No. 2, 1996, p. 320-326.

Research output: Contribution to journalArticle

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