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作 者:刘安定[1] 杨燕[1] 李方和[1] 陆蒙吉[2] 龚非力[3] 杨东亮[1]
机构地区:[1]华中科技大学同济医学院附属同济医院实验医学研究中心,湖北武汉430030 [2]华中科技大学同济医学院附属同济医院病原生物学系,湖北武汉430030 [3]华中科技大学同济医学院附属同济医院免疫学系,湖北武汉430030
出 处:《第四军医大学学报》2007年第14期1260-1263,共4页Journal of the Fourth Military Medical University
基 金:国家自然科学基金(30571646);国家重大基础研究项目(973)(2005CB522901)
摘 要:目的:预测人宫颈癌基因(human cervical cancer oncogene,HCCR)蛋白的二级结构,B细胞表位及其HLA-A,B限制性细胞毒性T细胞表位.方法:综合分析二级结构、亲水性、柔韧性、表面可及性与抗原性指数,预测HCCR蛋白的B细胞抗原表位;利用BIMAS,SYFPEITHI和NetCTL方法预测分析其HLA-A*0201限制性CTL表位,运用NetCTL方法对HLA-A的其他等位基因和HLA-B限制性CTL表位进行预测分析.结果:HCCR蛋白的二级结构主要由α-螺旋结构组成,B细胞优势表位位于N端第41~53,216~228,310~325和355~360区段;预测得到5个HLA-A*0201限制性CTL优势表位分别为YLVFLLMYL(152~160),YLFPRQLLI(159~167),LLLHNVVLL(343~351),CLFLGIISI(138~146)和SIPPFA-NYL(145~153),HCCR蛋白HLA-A,B限制CTL表位主要位于胞外区.结论:应用多参数预测HCCR蛋白B细胞表位及其HLA-A,B限制性细胞毒性T细胞表位,为进一步实验鉴定其表位进而制备单克隆抗体和基于HCCR抗原的肿瘤免疫学治疗奠定了基础.AIM: To predict the secondary structure, the B cell epitopes and the HLA-A, B restricted T cell epitopes of human cervical cancer oncogene ( HCCR ) protein. METHODS : The secondary structure was predicted by the methods of Proteus and SOPMA. The hydrophilicity, surface probability, flexibility and antigenic index were predicted by the methods of Kyte-Doolittle, Emini, Karplus-Schultz and Jameson-wolf, respectively. According to the above methods, the B cell epitopes for HCCR protein were predicted. HLA-A * 0201-restricted T cell epitopes were predicted by BIMAS, SYFPEITHI and NetCTL. And the restricted T cell epitopes of HLA-B and the other alleles of HLA-A were predicted by NetCTL. RESULTS: The secondary structure of HCCR1 protein was mainly composed of α- helix. The B cell epitopes were probably located at or adjacent to the N-terminal No. 41 - 53,216 - 228,310 - 325 and 355 - 360 regions. And the five predominant HLA-A * 0201-restricted T cell epitopes were YLVFLL.MYL(152-160), YLFPRQLLI(159-153), LLLHNVVLL(343-351), CLFLGIISI(138-146) and SIPPFANYL(145-153). The HLA-A, B restricted T cell epitopes of HCCR protein were probably located at extracelluar domain of protein. CONCLUSION: Prediction of the epitopes of HCCR protein can provide a basis for production of the monoclonal antibody and development of some promising antigen peptides for tumor vaccines.
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