RECOGNITION OF INFLUENZA-A MATRIX PROTEIN BY HLA-A2-RESTRICTED CYTO-TOXIC LYMPHOCYTES-T - USE OF ANALOGS TO ORIENT THE MATRIX PEPTIDE IN THE HLA-A2 BINDING-SITE
RECOGNITION OF INFLUENZA-A MATRIX PROTEIN BY HLA-A2-RESTRICTED CYTO-TOXIC LYMPHOCYTES-T - USE OF ANALOGS TO ORIENT THE MATRIX PEPTIDE IN THE HLA-A2 BINDING-SITE
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DOI：
10.1084/jem.168.6.2045
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发表时间：
1988-12-01
影响因子：
15.3
通讯作者：
ROTHBARD, J
中科院分区：
文献类型：
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作者：
GOTCH, F;MCMICHAEL, A;ROTHBARD, J
研究了针对甲型流感病毒基质肽57-68的特异性CTL和HLA-A2限制性CTL。分析了它们识别一组类似肽的能力，其中每一个类似肽与天然肽相差一个氨基酸。这揭示了一个由五个氨基酸组成的核心，61-65，其中一个或多个变化完全废除了识别。第61位的甘氨酸是唯一不容许取代的残基。测试不诱导CTL介导的裂解的拮抗肽作为天然肽的竞争者;在位置60、64和65处具有取代的拮抗肽被抑制，鉴定与TCR相互作用的残基。另一种方法是在所有类似物上测试一组四个CTL克隆。观察到几种取代肽在单个CTL克隆识别中的显著差异。数据表明，大多数类似物与HLA-A2结合，在肽的精细定位方面可能存在差异。α。螺旋取向的肽进行了讨论。
CTL specific for the influenza A virus matrix peptide 57-68 and restricted by HLA-A2 were studied. Their ability to recognize a set of analogue peptides, each of which differed from the natural peptide by a single amino acid, was analyzed. This revealed a core of five amino acids, 61-65, where one or more changes completely abrogated recognition. The glycine at position 61 was the only residue where no substitution was tolerated. Analogue peptides that did not induce CTL-mediated lysis were tested as competitors with the natural peptide; those with substitutions at postions 60, 64 and 65 inhibited, identifying residues that interact with the TCR. Another approach was to test a set of four CTL clones on all of the analogues. Marked differences in recognition by individual CTL clones were observed for several substituted peptides. The data indicate that most of the anlogues bind to HLA-A2 with possible differences in fine positioning of the peptide. An .alpha. helical orientation for the peptide is discussed.