A FAMILY OF CONCANAVALIN A-BINDING PEPTIDES FROM A HEXAPEPTIDE EPITOPE LIBRARY
A FAMILY OF CONCANAVALIN A-BINDING PEPTIDES FROM A HEXAPEPTIDE EPITOPE LIBRARY
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DOI：
10.1073/pnas.89.12.5398
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发表时间：
1992-06-15
影响因子：
11.1
通讯作者：
GOLDSTEIN, IJ
中科院分区：
文献类型：
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作者：
SCOTT, JK;LOGANATHAN, D;GOLDSTEIN, IJ
凝集素刀豆蛋白A(ConA)在寡糖的非还原末端与甲基α-D-甘露糖苷(Me-α-Man)以及α-D-甘露糖基结合。通过筛选丝状噬菌体展示随机六肽的表位文库，筛选出模拟Me-α-Man与ConA结合的配基多肽。在亲和纯化的噬菌体中鉴定出一个共同的序列；ConA与带有该序列的噬菌体结合，并被Me-Alpha-Man抑制。当测试与一组凝集素的结合时，携带该序列的噬菌体仅与密切相关的D-甘露糖结合凝集素结合很弱，表明与ConA的结合具有高度的选择性。含有共有序列的合成肽可阻断葡聚糖对ConA的沉淀，其抑制强度相当于甲基α-D-吡喃葡萄糖苷。这些结果表明，ConA的特异性不仅限于碳水化合物，而且可以从表位文库中鉴定出针对植物、动物或细菌来源的凝集素的高选择性糖模拟物。
The lectin concanavalin A (Con A) binds methyl alpha-D-mannopyranoside (Me-alpha-Man) as well as alpha-D-mannosyl groups at the nonreducing terminus of oligosaccharides. Ligand peptides that mimic the binding of Me-alpha-Man to Con A were identified from screening an epitope library composed of filamentous phage displaying random hexapeptides. A consensus sequence was identified among affinity-purified phage; Con A binds phage bearing this sequence and is inhibited from doing so by Me-alpha-Man. When tested for binding against a panel of lectins, phage bearing this sequence bind only weakly to a closely related D-mannose-binding lectin, indicating that binding to Con A is highly selective. A synthetic peptide bearing the consensus sequence blocks the precipitation of Con A by dextran with an inhibition strength equivalent to that of methyl alpha-D-glucopyranoside. These results demonstrate that the specificity of Con A is not limited to carbohydrates and that highly selective sugar-mimics for lectins of plant, animal, or bacterial origin may be identified from epitope libraries.