A lectin recognizes differential arrangements of O-glycans on mucin repeats
A lectin recognizes differential arrangements of O-glycans on mucin repeats
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DOI：
10.1016/j.bbrc.2008.04.120
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发表时间：
2008-07-11
影响因子：
3.1
通讯作者：
Irimura, Tatsuro
中科院分区：
文献类型：
--
作者：
Kato, Kentaro;Takeuchi, Hideyuki;Irimura, Tatsuro
利用表面等离子体共振技术研究了长柔毛野豌豆凝集素B4（VVA-B4）与含O-连接的GalNAc糖肽的相互作用。显示亲和力受肽PTTTPITTTTK上的O-糖基化位点的排列影响，所述肽代表MUC 2的串联重复。结合速率常数相对较高，其中超过三个氨基酸残基被放置在GalNAc-Thr残基之间的特定类别的GalNAc-肽。PTT*T*PITT*T*TK（T* 表示GalNAc-Thr）在测试的糖肽中具有最高的缔合速率常数。含有连续GalNAc残基的肽的解离速率常数较低，PT*TTPIT*T*T*TK是检测的糖肽中最低的。解离常数（K-D），计算为k（d）/k（a），其中PTT*T*PITT*T*TK最低。因此，GalNAc残基的排列而不是数量显然决定了VVA-B4和具有连接的GalNAc残基的肽之间的亲和力。皇冠版权所有（C）2008由爱思唯尔公司出版。All rights reserved.
Interaction of Vicia villosa agglutinin-B4 (VVA-B4) to glycopeptides with O-linked GalNAc residues was investigated by surface plasmon resonance. The affinity was shown to be influenced by the arrangement of O-glycosylation sites on a peptide, PTTTPITTTTK, representing the tandem repeat of MUC2. The association rate constant was relatively high with a particular category of GalNAc-peptides in which more than three amino acid residues were placed between GalNAc-Thr residues. PTT*T*PITT*T*TK (T* indicates GalNAc-Thr) had the highest association rate constant among the glycopeptides tested. The dissociation rate constant was low in the peptides containing consecutive GalNAc residues and PT*TTPIT*T*T*TK was the lowest of the glycopeptides tested. Dissociation constant (K-D), calculated as k(d)/k(a) was the lowest with PTT*T*PITT*T*TK. Therefore, the arrangement but not the quantity of GalNAc residues apparently determines the affinity between VVA-B4 and peptides with attached GalNAc residues. Crown Copyright (C) 2008 Published by Elsevier Inc. All rights reserved.