Recognition of influenza A matrix protein by HLA-A2-restricted cytotoxic T lymphocytes. Use of analogues to orientate the matrix peptide in the HLA-A2 binding site
Recognition of influenza A matrix protein by HLA-A2-restricted cytotoxic T lymphocytes. Use of analogues to orientate the matrix peptide in the HLA-A2 binding site
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HLA-A2 限制性细胞毒性 T 淋巴细胞对甲型流感基质蛋白的识别。
DOI：
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发表时间：
1988
影响因子：
15.3
通讯作者：
Jonathan B. Rothbard
中科院分区：
文献类型：
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作者：
Frances M. Gotch;Andrew J. McMichael;Jonathan B. Rothbard
研究了甲型流感病毒基质肽57-68特异性、受HLA-A2限制的CTL。他们的能力，以识别一组类似肽，每一个不同于天然肽的一个氨基酸，进行了分析。这揭示了一个核心的五个氨基酸，61-65，其中一个或多个变化完全取消了识别。第61位的甘氨酸是唯一不能被取代的残基。不诱导CTL介导裂解的类似肽作为天然肽的竞争对手进行了测试；那些在60、64和65位取代的位点被抑制，识别出与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种CTL克隆。不同CTL克隆对几种取代肽的识别存在显著差异。数据表明，大多数类似物与HLA-A2结合，可能在肽的精细定位上存在差异。讨论了肽的α螺旋取向。
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 positions 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 analogues bind to HLA-A2 with possible differences in fine positioning of the peptide. An alpha helical orientation for the peptide is discussed.
DOI：
10.1073/pnas.82.6.1785
发表时间：
1985-01-01
影响因子：
11.1
作者：
YEWDELL, JW;BENNINK, JR;MOSS, B
通讯作者：
MOSS, B