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
中科院分区:
文献类型:
--
作者:
Jackson,DC;Drummer,HE;Urge,L;OtvosJr,L;Brown,LE
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.