CAS Key Laboratory of Pathogenic Microbiology and Immunology (CASPMI), Chinese Academy of Sciences, Beijing, China.
Immunol Invest. 2010 Jan;39(2):103-13. doi: 10.3109/08820130903496777.
Tuberculosis is caused by an intracellular pathogen Mycobacterium tuberculosis (Mtb) and poses a persistent threat to global health. MHC class I-restricted CD8 cytotoxic T lymphocytes (CTL) are essential for protective immunity to Tuberculosis. Information for CTL epitopes derived from Mtb is desirable for vaccine design and assessment of T cell responses. However, the knowledge about CTL epitopes of Mtb, particularly those non-A2 HLA alleles restricted is rare. In this study, beta-2-microglobulin (beta 2m, beta(2)m) linked HLA-A24 single chain was expressed on RMA-S cell line defective in the endogenous antigen processing and applied for screening of peptides which could stabilize the HLA-A24 complex on the cell surface. From a group of peptides predicted as binders by a computer algorithm, five peptides were shown to bind to HLA-A24 protein on the cell surface. As comparison we have also identified a dozen Mtb proteins derived peptides that bind to HLA-A2 specifically. The cell line and HLA binders present here would be useful for further identification of CD8 restricted Mtb epitopes.
结核病是由细胞内病原体结核分枝杆菌（Mtb）引起的，对全球健康构成持续威胁。主要组织相容性复合体 I 类限制的 CD8 细胞毒性 T 淋巴细胞（CTL）对于结核病的保护性免疫至关重要。用于疫苗设计和评估 T 细胞反应的 Mtb CTL 表位信息是可取的。然而，关于 Mtb 的 CTL 表位，特别是那些非 A2 HLA 等位基因限制的表位的知识很少。在这项研究中，β-2-微球蛋白（β2m，β(2)m）连接的 HLA-A24 单链在缺乏内源性抗原加工的 RMA-S 细胞系上表达，并应用于筛选可稳定细胞表面 HLA-A24 复合物的肽。从一组通过计算机算法预测为结合物的肽中，有五个肽显示与细胞表面的 HLA-A24 蛋白结合。作为比较，我们还鉴定了十几个与 HLA-A2 特异性结合的 Mtb 蛋白衍生肽。此处呈现的细胞系和 HLA 结合物将有助于进一步鉴定 CD8 限制的 Mtb 表位。
