嗜麦芽窄食单胞菌外膜蛋白OmpA的生物信息学分析  

Bioinformatics analysis of Stenotrophomonas maltophilia outer membrane protein OmpA

作　　者：李燕[1,2] 赵尊全 刘鹏 尚学义 汤雪萍 李艳 LI Yan;ZHAO Zun-quan;LIU Peng;SHANG Xue-yi;TANG Xue-ping(Hospital 307 of PLA of Anhui Medical University, Hefei 230032, China;Department of Critical Care Medicine, Affiliated Hospital, Academy of Military Medical Sciences, Academy of Military Sciences, Beijing 100071, China;State Key Laboratory of Pathogen and Biosecurtity, Institute of Microbiology and Epidemiology, Academy of Military Medical Sciences, Academy of Military Sciences,Beijing 100071, China)

机构地区：[1]安徽医科大学解放军307医院临床学院,合肥230032 [2]军事科学院军事医学研究院附属医院重症医学科,北京100071 [3]军事科学院军事医学研究院微生物流行病研究所病原微生物生物安全国家重点实验室,北京100071

出　　处：《军事医学》2017年第12期987-990,共4页Military Medical Sciences

基　　金：国家自然科学基金资助项目(81571959;81071399)

摘　　要：目的对嗜麦芽窄食单胞菌外膜蛋白A(OmpA)的结构和功能进行预测与分析。方法利用生物信息学软件和生物数据库对OmpA蛋白的理化性质、信号肽、跨膜区、亚细胞定位、二级与三级结构、同源性、保守结构域及抗原决定簇进行预测分析。结果 OmpA蛋白为亲水性蛋白,其1~22位氨基酸为信号肽序列,无跨膜结构并定位于细胞膜外;二级结构中含无规则卷曲、α-螺旋、β-转角和β-片层比例分别为50.27%、24.59%、9.29%和15.85%;三级结构预测OmpA蛋白为桶状蛋白;OmpA蛋白在不同嗜麦芽窄食单胞菌株间高度保守,而与人、小鼠的蛋白序列进行比对分析未找到同源序列;OmpA蛋白保守结构域在N端为OM膜通道蛋白超家族,在C端为OmpA_C超家族;OmpA蛋白含有11个优势抗原决定簇区域。结论通过对OmpA进行生物信息学分析获得该蛋白的特性,不仅为进一步研究该蛋白的结构与功能提供参考资料,也为研制相关亚单位疫苗提供理论依据。Objective To predict and analyze the structure and function of Stenotrophomonas maltophilia OmpA. Methods Bioinformatics software and biological databases were used to analyze the physicochemical properties, signal peptides, and transmembrane structures of the OmpA protein and to predict the subcellular localization, secondary and tertiary structures, sequence homology and conserved domains, and epitopes of OmpA. Results OmpA protein had strong hydrophilicity but without transmembrane helices in mature protein, and positions 1 -22 of the sequence were predicted as signal peptide. In the second structure random coil helix, cdpha-helix, beta-turn and extended strand made up 50.27% , 24.59% , 9.29% and 15.85% , respectively. The three-dimensional structure was 13-barrel. OmpA was highly conserved among S. maltophilia strains but shared minimal homology with human and mouse proteins. The N-terminal domain of OmpA was OM-channels superfamily and the C-terminal domain of OmpA was OmpA_C-like superfamily. OmpA protein contained 11 dominant antigen epitopes. Conclusion The characteristics of OmpA identified by bioinformatics analysis can not only provide reference for the study of the structure and novel function of OmpA, but also theoretically contribute to the research on related new subunit vaccines.

关 键 词：嗜麦芽窄食单胞菌 外膜蛋白A 生物信息学 结构 功能 抗原决定簇 

分 类 号：R378[医药卫生—病原生物学]