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首页> 外文期刊>Infection and immunity >Mapping of multiple HLA class II-restricted T-cell epitopes of the mycobacterial 70-kilodalton heat shock protein.
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Mapping of multiple HLA class II-restricted T-cell epitopes of the mycobacterial 70-kilodalton heat shock protein.

机译：分支杆菌70-千洛酮热休克蛋白的多个HLA II类限制性T细胞表位的定位。

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By combining a DNA subclone and synthetic-peptide approach, we mapped epitopes of the immunogenic mycobacterial 70-kDa heat shock protein (HSP70) recognized by human CD4+ T-cell clones and lines. In addition, we identified the respective HLA-DR molecules used in antigen presentation. The donor groups used were healthy persons immunized with killed Mycobacterium leprae and tuberculoid leprosy patients. The results show that the N-terminal part of the HSP70 molecule contains three different T-cell epitopes, of which two were presented by DR7 (amino acids [aa] 66 to 82 and 210 to 226) and one was presented by DR3 (aa 262 to 274). The C-terminal part contains one epitope (aa 413 to 424) presented by HLA-DR2. The C-terminal epitope shows extensive homology to the corresponding region of the human HSP70 sequence. All of the T-cell epitopes identified were presented by only one particular HLA-DR molecule. We also found that HLA-DR5 and DRw53 can present HSP70 to T cells, demonstrating the presence of additional epitopes not yet defined at the peptide level. On the basis of the donors used in this study, recognition of HSP70 at the epitope level seems to be ruled by the restriction elements expressed by the donor rather than by any difference in reactivity between healthy individuals and patients. In conclusion, mycobacterial HSP70 is relevant to subunit vaccine design since it contains a variety of T-cell epitopes presented in the context of multiple HLA-DR molecules.
机译：通过结合DNA亚克隆和合成肽方法，我们绘制了人类CD4 + T细胞克隆和细胞系识别的免疫原性分枝杆菌70 kDa热激蛋白（HSP70）的表位。此外，我们鉴定了抗原呈递中使用的各个HLA-DR分子。所使用的捐助者是健康的人，他们被杀死的麻风分枝杆菌和结核性麻风病人免疫。结果显示，HSP70分子的N端部分包含三个不同的T细胞表位，其中两个由DR7呈现（氨基酸[aa] 66至82和210至226），一个由DR3呈现（aa 262至274）。 C末端部分包含由HLA-DR2呈递的一个表位（aa 413至424）。 C末端表位显示出与人HSP70序列的相应区域的广泛同源性。鉴定的所有T细胞表位仅由一个特定的HLA-DR分子呈递。我们还发现，HLA-DR5和DRw53可以将HSP70呈递给T细胞，证明存在尚未在肽水平上定义的其他表位。根据本研究中使用的供体，在表位水平上对HSP70的识别似乎是由供体表达的限制因素决定的，而不是由健康个体与患者之间反应性的任何差异决定的。总之，分枝杆菌HSP70与亚单位疫苗设计有关，因为它包含在多个HLA-DR分子的背景下呈现的多种T细胞表位。

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