TY - JOUR
T1 - A comparison of the fine saccharide-binding specificity of Dioclea grandiflora lectin and concanavalin A
AU - Gupta, Dipti
AU - Oscarson, Stefan
AU - Raju, T. Shantha
AU - Stanley, Pamela
AU - Toone, Eric J.
AU - Brewer, C. Fred
PY - 1996
Y1 - 1996
N2 - 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.
AB - 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.
KW - Carbohydrate
KW - Cross-linking
KW - Glycopeptide
KW - Lectin
KW - Specificity
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U2 - 10.1111/j.1432-1033.1996.0320r.x
DO - 10.1111/j.1432-1033.1996.0320r.x
M3 - Article
C2 - 8973650
AN - SCOPUS:0029850081
SN - 0014-2956
VL - 242
SP - 320
EP - 326
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 2
ER -