摘要
目的对刚地弓形虫棒状体蛋白10(TgROP10)进行生物信息学预测,分析其免疫原性。方法运用生物信息学在线分析程序ProtParam、SOSUI、ProtScale、TMHMM、SignalP-4.1、TargetP1.1Server、SOPMA、MotifScan、SWISS-MODEL、SYFPEITHI和Bcepred等并结合生物信息学软件DNASTAR和DNAMAN分析预测TgROP10的理化性质、可溶性、亲疏水性、跨膜结构域、信号肽、胞内定位、二级结构、蛋白翻译后修饰位点、三级结构、柔韧性、表面可及性和B细胞、T细胞抗原表位等。结果 TgROP10蛋白由586个氨基酸组成,分子式为C2562H4045N739O964S9,分子质量单位(Mr)为60.912 21×103,理论等电点为4.19,吸光度值为0.476,半衰期为30h,不稳定系数为55.56,脂溶性指数为56.25,总平均亲水性系数为-0.699,属于亲水性蛋白;该蛋白无跨膜结构区域,信号肽切割位点在22-23位氨基酸之间,亚细胞定位预测可能是分泌蛋白;二级结构中α螺旋和β折叠分别占26.79%和13.31%,β转角和无规则卷曲分别占6.48%和53.41%,有6种翻译后修饰位点,15个B细胞抗原表位,3个CTL细胞抗原表位,12个Th细胞抗原表位,28个亲水性参数得分1.9的区域,15个柔韧性参数得分2.0的区域,27个表面可及性参数得分1.9的区域,3个暴露表面参数得分2.3的区域。结论生物信息学预测TgROP10含多个抗原表位,具有免疫原性,可作为弓形虫疫苗备选蛋白。
Objective To bioinformatically analyze the rhoptry protein 10 of Toxoplasma gondii（TgROP10）in order to analyze its immunogenicity. Methods The physico-chemical properties,solubility,hydrophilicity and hydrophobicity,transmembrane domains,signal peptides,intracellular localization,secondary structure,post translational modification sites,tertiary structure,flexibility and surface accessibility,and specific epitopes of TgROP10 were analyzed and predicted with bioinformatic software such as ProtParam,SOSUI,ProtScale,TMHMM,SignalP-4.1,TargetP1.1Server,SOPMA,MotifScan,SWISS-MODEL,SYFPEITHI,Bcepred,DNASTAR,and DNAMAN. Results TgROP10 consists of 586 amino acids with a molecular formula of2562H4045N739O964S9,a molecular weight of 60.912 21×103,a theoretical isoelectric point of 4.19,an absorbance coefficient of 0.476,an estimated half-life of 30 h,an instability index of 55.56,an aliphatic index of 56.25,and a grand average of hydropathicity of-0.699.TgROP10 is a hydrophilic protein without transmembrane regions and its signal peptide cleavage site is located at amino acids 22-23.Prediction of its subcellular localization indicated that TgROP10 may be a secreted protein.α-helices account for 26.79% of its secondary structure whileβ-sheets account for 13.31%,β-turns account for 6.48%,and random coils account for53.41%.The protein has 6post translational modification sites,15 Bcell epitopes,3CTL cell epitopes,12 Th cell epitopes,28 highly hydrophilic regions（critical value：1.9）,15 flexible regions（critical value：2.0）,27surface-accessible regions（critical value：1.9）,and 3exposed surfaces（critical value：2.3）. Conclusion TgROP10 has multiple epitopes,so it may be a highly immunogenic protein and an option for vaccine development.
作者
刘荣荣
张进顺
张晓磊
刘楠
贾晓晖
王璐瑶
LIU Rong-rong ZHANG Jin-shun ZHANG Xiaoqei LIU Nan JIA Xiao-hui WANG Lu-yao(Pathogen Biology and Immunology Research Institute, Hebei North University, Zhangjialeou 075000, Hebei, Chin)
出处
《中国病原生物学杂志》
CSCD
北大核心
2017年第9期855-859,共5页
Journal of Pathogen Biology
基金
河北省自然科学基金项目(No.H2013405091)
河北北方学院校级重大课题(No.ZD201312)
