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

被引:45
作者
Gupta, D
Oscarson, S
Raju, TS
Stanley, P
Toone, EJ
Brewer, CF
机构
[1] YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT MOL PHARMACOL,BRONX,NY 10461
[2] ALBERT EINSTEIN COLL MED,DEPT MICROBIOL & IMMUNOL,BRONX,NY 10467
[3] UNIV STOCKHOLM,DEPT ORGAN CHEM,STOCKHOLM,SWEDEN
[4] ALBERT EINSTEIN COLL MED,DEPT CELL BIOL,BRONX,NY 10467
[5] DUKE UNIV,DEPT CHEM,DURHAM,NC 27706
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1996年 / 242卷 / 02期
关键词
lectin; specificity; cross-linking; carbohydrate; glycopeptide;
D O I
10.1111/j.1432-1033.1996.0320r.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The lectin from the seeds of Dioclea grandiflora (DGL) is st 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-(alpha-D-mannopyranosyl)-alpha-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-(alpha-D-mannopyranosyl)-alpha-D-mannopyranos 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 alpha(1-6)Man residue, the 3-hydroxyl group of the alpha(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.
引用
收藏
页码:320 / 326
页数:7
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