Glycosylation of a synthetic peptide representing a T-cell determinant of influenza virus hemagglutinin results in loss of recognition by CD4+ T-cell clones.

Glycosylation of a synthetic peptide representing a T-cell determinant of influenza virus hemagglutinin results in loss of recognition by CD4+ T-cell clones.
复制标题

代表流感病毒血凝素 T 细胞决定簇的合成肽的糖基化会导致 CD4 T 细胞克隆失去识别能力。

DOI:
10.1006/viro.1994.1140
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发表时间:
1994
期刊:
影响因子:
3.7
通讯作者:
Brown,LE
Brown,LE
中科院分区:
医学3区
文献类型:
--
作者:
Jackson,DC;Drummer,HE;Urge,L;OtvosJr,L;Brown,LE

文献摘要

被引文献

相似文献

使用合成糖肽来研究流感病毒特异性 CD4+T 细胞对血凝素中的氨基酸取代导致碳水化合物侧链附着的病毒株反应减弱的可能机制。肽 NCTLIDALLGDPH 刺激血凝素特异性 T 细胞克隆 F1-36 和 F1-40 的剧烈增殖,但添加接近天然碳水化合物触角大小的七糖,消除了肽的刺激能力。即使 N 端天冬酰胺的碳水化合物附着位点位于该序列所包含的 T 细胞决定簇之外,也会发生这种情况。仅具有两个糖单位的糖肽对 F1-36 具有刺激作用,但对 F1-40 没有刺激作用,这表明具有碳水化合物侧链的肽能够与 MHC 分子结合,但某些克隆的 T 细胞受体与糖肽 MHC 复合物的接近受到阻碍。将长碳水化合物侧链附着到 T 细胞决定簇后 T 细胞识别的丧失并不是普遍发现,因为将六个碳水化合物单位附着到 NKYVKQNTLKLA 肽上,对该序列特异的 T 细胞克隆的刺激影响很小或没有影响。
Synthetic glycopeptides were used to study possible mechanisms for the reduction observed in the response of influenza virus-specific CD4+T-cells to strains of virus in which amino acid substitution in the hemagglutinin has led to attachment of a carbohydrate side chain. The peptide NCTLIDALLGDPH stimulates vigorous proliferation of hemagglutinin-specific T-cell clones F1-36 and F1-40 but addition of a heptasaccharide, which approaches the size of natural carbohydrate antennae, eliminated the stimulatory capacity of the peptide. This occurs even though the site of carbohydrate attachment at the N-terminal asparagine lies outside the T-cell determinants encompassed by this sequence. A glycopeptide with only two sugar units was stimulatory for F1-36 but not F1-40, suggesting that peptides with a carbohydrate side chain are able to bind to MHC molecules but that approach of the T-cell receptor of certain clones to the glycopeptide MHC complex is hindered. Loss of T-cell recognition following attachment of a long carbohydrate side-chain to T-cell determinants is not a general finding because attachment of six carbohydrate units to the peptide, NKYVKQNTLKLA, had little or no effect on the stimulation of a T-cell clone specific for this sequence.