标题：广州管圆线虫钙网蛋白超家族结构和功能的生物信息学分析

      作者：劳甜甜 1，朱晨陆 2，崔伟乐 2，武其嘉 2，罗琳平 2，芦亚君 1，李丽花 3    (1.海南医学院热带医学与检验医学院，海南 海口 571199；2.海南医学院临床学院，海南 海口 571199；3.海南医学院基础医学与生命科学学院，海南 海口 571199)

      卷次： 2018年29卷7期

      【摘要】 目的 应用生物信息学技术预测广州管圆线虫钙网蛋白(CRT)的结构和功能，为进一步研究广州管圆线虫提供理论依据。方法 于NCBI PROTEIN数据库中确定广州管圆线虫钙网蛋白的氨基酸残基序列。应用分析工具Blast、Protparam、InterProScan、protscale、SignalP-3.0、PSORTⅡ、BepiPred、TMHMM、VectorNTI Suite 11软件包、Phyre2分别进行该蛋白质的基本性质、结构域、疏水性、信号肽、亚细胞定位、抗原表位、跨膜区及空间结构的预测及分析。结果 Blast预测该蛋白为钙网蛋白，有401个氨基酸残基，理论分子量为46 552.67 Da，具有钙网蛋白超家族结构域，为亲水蛋白，具有明显的信号肽和1个跨膜螺旋，具有9个B细胞抗原表位，二级结构含6个α-螺旋和18个β-折叠股。结论 钙网蛋白与广州管圆线虫的感染免疫密切相关，可参与感染过程或宿主免疫应答，具有作为诊断抗原分子的价值和潜在的疫苗候选分子。
      【关键词】 广州管圆线虫；钙网蛋白；生物信息学分析
      【中图分类号】 R383.1 【文献标识码】 A 【文章编号】 1003—6350（2018）07—0892—04

Bioinformatics analysis for structure and function of calreticulin superfamily from Angiostrongylus cantonensis.LAO Tian-tian 1, ZHU Chen-lu 2, CUI Wei-le 2, WU Qi-jia 2, LUO Lin-ping 2, LU Ya-jun 1, LI Li-hua 3.
1. School ofTropical and Laboratory Medicine, Hainan Medical University, Haikou 571199, Hainan, CHINA; 2. Clinical College ofHainan Medical University, Haikou 571199, Hainan, CHINA; 3. Institute of Basic Medicine and Life Science of HainanMedical University, Haikou 571199, Hainan, CHINA
【Abstract】 Objective The structure and function of calreticulin superfamily protein from Angiostrongylus canto-nensis were predicted by bioinformatics technology to provide a theoretical basis for further study. Methods Amino acidresidues of calreticulin were determined by NCBI PROTEIN database. By the method of online analysis tools: Blast, Prot-param, InterProScan, protscale, SignalP-3.0, PSORTⅡ, BepiPred, TMHMM, VectorNTI Suite 11 packages and Phyre 2,the structure and function of the protein were predicted and analyzed. Results The results showed that the protein wascalreticulin with 401 amino acid residues, the theoretical molecular weight was 46 552.67 Da. It has the domain of calretic-ulin superfamily, which is hydrophilic protein, with an obvious signal peptide, a transmembrane helice, and nine B cell epi-topes. And the two stage structure contains 6 alpha helices and 18 beta folded strands. Conclusion Calreticulin is closelyrelated to the infection immunity of Angiostrongylus cantonensis, and may be involved in the infection process and hostimmune response. The protein is valuable as a diagnostic antigen molecule and potential vaccine candidate.
      【Key words】 Angiostrongylus cantonensis; Calreticulin; Bioinformatics analysisdoi:10.3969/j.issn.1003-6350.2018.07.002基金项目：海南省大学生创新创业训练计划项目(编号：20150077)；海南医学院大学生创新创业训练计划项目(编号：HYCX2014044)