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作 者:王海燕 何梦雅 余飞艳 张柯 Wajid Ameen Mirza 陈帅印[1] 张荣光[1] 段广才[1] WANG Hai-yan;HE Meng-ya;YU Fei-yan;ZHANG Ke;Wajid Ameen Mirza;CHEN Shuai-yin;ZHANG Rong-guang;DUAN Guang-cai(Department of Kpidemiology,College of Public Health,Zhengzhou University,Zhengzhou,China 450001)
机构地区:[1]郑州大学公共卫生学院流行病与统计学教研室,河南郑州450001
出 处:《中国病原生物学杂志》2020年第1期1-4,9,共5页Journal of Pathogen Biology
基 金:国家自然科学基金面上项目(No.81773495);国家科技重大专项(No.2018ZX10301407)。
摘 要:目的应用生物学软件预测幽门螺杆菌(Helicobacter pylori,Hp)ompP1基因编码蛋白(OmpP1)的结构与功能。方法从NCBI数据库中获取ompP1基因的相关信息,应用软件MEGAX 10.0.5构建Hp进化树,应用生物信息学软件分析OmpP1蛋白的氨基酸序列、理化性质、跨膜区、信号肽、糖基化和磷酸化位点、空间结构以及抗原表位。结果 ompP1基因核苷酸序列编码区长1 764 bp,编码587个氨基酸;生物信息学分析显示ompP1基因在不同菌株间的同源性为96.2%~97.17%,其编码的OmpP1蛋白是一种性质稳定、偏碱性的亲水蛋白;该蛋白无跨膜区和信号肽,含有糖基化和磷酸化位点;OmpP1二级结构中含α-螺旋178个,延长链162个,β转角37个,无规则卷曲210个,分别占30.32%、27.60%、6.30%和35.78%;三级结构分析显示OmpP1含有OM_channels蛋白家族特征性结构域;BepiPred1.0和SYFPEITHI9预测该蛋白含有22个B淋巴细胞和28个CTL淋巴细胞相关抗原表位。结论 Hp OmpP1为碱性亲水性蛋白,含有T、B细胞抗原表位,可为其抗原性研究和高效表位疫苗的研发提供理论参考。Objective To analyze the structure and function of the ompP1-encoded protein(OmpP1) of Helicobacter pylori using bioinformatics. Methods Genetic information related to the ompP1 gene was obtained from the NCBI database. The nuclear blast tool provided by the NCBI was used to obtain the homologous sequences of ompP1. The phylogenetic tree of H. pylori was constructed using MEGAX 10.0.5. The amino acid sequence, physicochemical properties, transmembrane regions, signal peptides, glycosylation and phosphorylation sites, secondary and tertiary structures, and epitopes of the OmpP1 protein were analyzed using bioinformatic software. Results The coding region of the ompP1 gene was 1,764 bp in length and encoded 587 amino acids. Bioinformatic analysis indicated that nucleic acid sequences of the ompP1 gene were 96.2-97.17%, similar among different H. pylori strains while amino acid sequences encoded by ompP1 were 98.98-99.32% similar. OmpP1 was a stable and alkaline hydrophilic protein with no transmembrane regions or signal peptides, but it did contain glycosylation and phosphorylation sites. The secondary structure of OmpP1 consisted of 178 alpha helixes(30.32%), 162 extended strands(27.60%), 37 beta turns(6.30%), and 210 random coils(35.78%). Analysis of the tertiary structure of OmpP1 with BepiPred1.0 and SYFPEITHI9 indicated that the conserved structure found in OmpP1 might be a characteristic domain of outer membrane(OM) channel proteins, and OmpP1 possessed 22 B cell-associated epitopes and 28 CTL cell epitopes. Conclusion H. pylori OmpP1 is an alkaline hydrophilic protein with T and B cell epitopes. These findings provide a theoretical reference for study of the antigenicity of H. pylori and for development of highly efficient epitope-based vaccines.
分 类 号:R378.91[医药卫生—病原生物学]
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