IOCAS-IR  > 实验海洋生物学重点实验室
Triosephosphate isomerase (TPI) facilitates the replication of WSSV in Exopalaemon carinicauda
Liu, Fei1,2; Li, Shihao2; Liu, Guangxing1; Li, Fuhua2,3
2017-06-01
发表期刊DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
卷号71页码:28-36
文章类型Article
摘要Triosephosphate isomerase (TPI) is a vital enzyme in the glycolytic pathway, which can catalyze the interconversion of glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). DHAP is involved in lipid metabolism and phospholipid synthesis. In order to know the role of TPI in WSSV infection to prawn, we cloned the full length cDNA of triosephosphate isomerase gene (EcTPI) from Exopalaemon carinicauda, and its function during WSSV infection was analyzed. EcTPI transcripts were widely distributed in all tissues, but showed relatively higher expression levels in the gill and epidermis. Its expression was apparently up-regulated after 24 h post WSSV injection (hpi), when the virus load began to rise. Furthermore, we detected the expressions of the key genes encoding the enzymes which catalyze the key steps in the glycolysis during WSSV infection. The data showed that genes encoding the enzymes which catalyzed upper steps of glycolysis to produce GAP including hexokinase (HK), glucose 6-phosphate isomerase (GPI) and phosphofructokinase-1 (PFK-1), were significantly up-regulated at 24 and 27 hpi. Genes encoding the enzymes catalyzing down steps of glycolysis after GAP, including glyceraldehyde-3-phosphate dehydrogenase (GAPDH), enolase (ENO) and pyruvate kinase (PM), were apparent down-regulated at 24 and 27 hpi. Meanwhile, the gene encoding the enzyme glycerol-3 phosphate dehydrogenase (GPDH) catalyzing DHAP to glycerol-3-phosphate (G-3-P) showed down regulation at 12-27 hpi, while the gene encoding dihydroxyacetone-phosphate acyltransferase (DHA-PAT) catalyzing DHAP to further synthesis of phospholipids showed up-regulation at 12-24 hpi. These data suggested that WSSV infection could change the glycolysis pathway to make them produce more phospholipids which could be very helpful for virus replication. In order to further confirm the above speculation, dsRNA interference (RNAi) approach was used to knock down EcTPI gene and analyze its effect on WSSV load in prawn. The data showed that interference of EcTPI gene led to a significant decrease of WSSV loads in WSSV infected prawn. These data provided useful information to understand the infection mechanism of WSSV. (C) 2017 Elsevier Ltd. All rights reserved.
关键词Ectpi Wssv Metabolic Pathway Exopalaemon Carinicauda
DOI10.1016/j.dci.2017.01.018
收录类别SCI
语种英语
WOS记录号WOS:000397834800004
引用统计
被引频次:17[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.qdio.ac.cn/handle/337002/136735
专题实验海洋生物学重点实验室
作者单位1.Ocean Univ China, Key Lab Marine Environm & Ecol, Minist Educ, Qingdao 266100, Peoples R China
2.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
3.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China
第一作者单位实验海洋生物学重点实验室
推荐引用方式
GB/T 7714
Liu, Fei,Li, Shihao,Liu, Guangxing,et al. Triosephosphate isomerase (TPI) facilitates the replication of WSSV in Exopalaemon carinicauda[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2017,71:28-36.
APA Liu, Fei,Li, Shihao,Liu, Guangxing,&Li, Fuhua.(2017).Triosephosphate isomerase (TPI) facilitates the replication of WSSV in Exopalaemon carinicauda.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,71,28-36.
MLA Liu, Fei,et al."Triosephosphate isomerase (TPI) facilitates the replication of WSSV in Exopalaemon carinicauda".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 71(2017):28-36.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
Triosephosphate isom(3115KB)期刊论文出版稿限制开放CC BY-NC-SA浏览
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Liu, Fei]的文章
[Li, Shihao]的文章
[Liu, Guangxing]的文章
百度学术
百度学术中相似的文章
[Liu, Fei]的文章
[Li, Shihao]的文章
[Liu, Guangxing]的文章
必应学术
必应学术中相似的文章
[Liu, Fei]的文章
[Li, Shihao]的文章
[Liu, Guangxing]的文章
相关权益政策
暂无数据
收藏/分享
文件名: Triosephosphate isomerase (TPI) facilitates the replication of WSSV in Exopalaemon carinicauda.pdf
格式: Adobe PDF
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。