[1]何欣蓉,杨阳,张永霞,等.拟穴青蟹细丝蛋白C的生物信息学分析及重组表达[J].集美大学学报(自然版),2021,26(1):14-21.
 HE Xinrong,YANG Yang,ZHANG Yongxia,et al.Bioinformatics Analysis and Recombinant Expression of Filamin C in Scylla paramamosain[J].Journal of Jimei University,2021,26(1):14-21.
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拟穴青蟹细丝蛋白C的生物信息学分析及重组表达()
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《集美大学学报(自然版)》[ISSN:1007-7405/CN:35-1186/N]

卷:
第26卷
期数:
2021年第1期
页码:
14-21
栏目:
水产、食品与生物工程
出版日期:
2021-01-28

文章信息/Info

Title:
Bioinformatics Analysis and Recombinant Expression of Filamin C in Scylla paramamosain
作者:
何欣蓉123杨阳123张永霞123刘红123曹敏杰123刘光明123
(1.集美大学食品与生物工程学院,福建 厦门 361021;2.水产品深加工技术国家地方联合工程研究中心,福建 厦门 361021;3.厦门市海洋功能食品重点实验室,福建 厦门 361021)
Author(s):
HE Xinrong123YANG Yang123ZHANG Yongxia123LIU Hong123CAO Minjie123LIU Guangming123
(1.College of Food and Biological Engineering,Jimei University,Xiamen 361021,China;2.National & Local Joint Engineering Research Center of Processing Technology for Aquatic Products,Xiamen 361021,China;3.Xiamen Key Laboratory of Marine Functional Food,Xiamen 361021,China)
关键词:
拟穴青蟹细丝蛋白C生物信息学重组表达
Keywords:
Scylla paramamosainfilamin Cbioinformatics analysisrecombinant expression
摘要:
为了探讨抗原表位与细丝蛋白C(filamin C,FLN c)结构之间的构效关系,对FLN c进行生物信息学分析及分段重组表达。生物信息学分析结果表明,FLN c二级结构以β折叠及无规则卷曲为主,确定其具有9个结构域,三级结构呈免疫球蛋白样折叠,具有典型的细丝蛋白家族特征。基于生物信息学分析,将拟穴青蟹(Scylla paramamosain)FLN c通过分段原核表达,纯化出带有麦芽糖结合蛋白(maltose binding protein,MBP)标签的重组表达蛋白rFLN c1(AA:1-335)、rFLN c2(AA:336-531)、rFLN c3(AA:532-847)。血清学分析结果显示,rFLN c2与蟹类过敏患者血清IgE结合能力最强,推测此区域含有大部分抗原表位。因此,定位拟穴青蟹FLN c氨基酸336-531结构域为抗原表位优势区,rFLN c2可用于FLN c的晶体学研究。
Abstract:
In order to explore the structureactivity relationship between the epitope and the structure of filamin C (FLN c),bioinformatics analysis and segmented recombinant expression of FLN c were performed.The results of bioinformatics analysis showed that the secondary structure of FLN c had 9 domains mainly with β-sheet and random coil.The tertiary structure was an immunoglobulinlike fold and had a typical filamin family characteristics.Based on bioinformatics analysis,the fragmented FLN c were expressed in Escherichia coli,and the recombinant protein rFLN c1 (AA:1-335),rFLN c2 (AA:336-531) and rFLN c3 (AA:532-847) with maltose binding protein tag were purified.The results of serological analysis showed that rFLN c2 had the strongest binding ability to IgE in sera of crab allergy patients.It was speculated that this region contained most of the epitopes.So the amino acid 336-531 domain of Scylla paramamosain FLN c as the epitope predominant region was mapped,indicating that rFLN c2 could be used for crystallographic research of FLN c.

相似文献/References:

[1]邹清,李君华,朱小明.人工感染呼肠孤病毒对拟穴青蟹部分免疫因子的影响[J].集美大学学报(自然版),2012,17(5):327.
 ZOU Qing,LI Jun-hua,ZHU Xiao-ming.Effects of Artifical Infection Reovirus Trails on Some Immune Factors of Mud Crab,Scylla paramamosain[J].Journal of Jimei University,2012,17(1):327.
[2]陈仲玮,费丹霞,杨阳,等.拟穴青蟹新型过敏原磷酸丙糖异构酶的鉴定分析[J].集美大学学报(自然版),2016,21(6):428.
 CHEN Zhong-wei,FEI Dan-xia,YANG Yang,et al.Identification and Characterization of Triosephosphate Isomerase as a Novel Allergen in Scylla paramamosain[J].Journal of Jimei University,2016,21(1):428.

更新日期/Last Update: 2021-03-25