Identification of a novel cytotoxic T lymphocyte epitope from CFP21, a secreted protein of Mycobacterium tuberculosis
Identification of a novel cytotoxic T lymphocyte epitope from CFP21, a secreted protein of Mycobacterium tuberculosis
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结核分枝杆菌分泌蛋白 CFP21 中新型细胞毒性 T 淋巴细胞表位的鉴定
DOI：
10.1016/j.imlet.2010.07.007
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发表时间：
2010-10-30
影响因子：
4.4
通讯作者：
Qi, Yuanming
中科院分区：
文献类型：
--
作者：
Lv, Hong;Gao, Yanfeng;Qi, Yuanming
CFP21是结核分枝杆菌（Mtb）的主要分泌蛋白，被认为是一种有前景的免疫治疗抗原。为了鉴定cfp21衍生的HLA-A*0201限制性表位，利用预测程序预测并合成了一系列天然肽及其类似物。天然肽p134 （AVADHVAAV）及其类似物p134- 1y2l和p134- 1y2l9l对HLA-A*0201分子具有很强的结合亲和力和稳定性。在ELISPOT实验中，这些肽诱导的细胞毒性T淋巴细胞（ctl）可以释放1fn - γ。在细胞毒性实验中，p134和p134- 1y2l9l诱导的ctl能够特异性地裂解装载肽的T2细胞。在这两项试验中，天然肽p134显示出最有效的活性。我们的结果表明p134可能是一个新的表位，可以作为开发抗结核分枝杆菌肽疫苗的良好候选者。(C) 2010 Elsevier B.V.版权所有
CFP21 is a major secreted protein of Mycobacterium tuberculosis (Mtb) which is considered as a promising antigen for immunotherapy. To identify CFP21-derived HLA-A*0201 restricted epitopes, a series of native peptides and their analogues were predicted with prediction programs and synthesized. The native peptide, p134 (AVADHVAAV), and its analogues, p134-1Y2L and p134-1Y2L9L, showed potent binding affinity and stability to HLA-A*0201 molecule. In ELISPOT assay, the cytotoxic T lymphocytes (CTLs) induced by these peptides could release 1FN-gamma. In cytotoxicity assay, the CTLs induced by p134 and p134-1Y2L9L could specifically lyse peptide-loaded T2 cells. In these two assays, the native peptide, p134, showed the most potent activity. Our results indicated that p134 could be a novel epitope which could serve as a good candidate to develop peptide vaccines against M. tuberculosis. (C) 2010 Elsevier B.V. All rights reserved.