Expression profiles of glyceraldehyde-3-phosphate dehydrogenase from Clonorchis sinensis: a glycolytic enzyme with plasminogen binding capacity
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- 作者：Yue Hu (1) (2)
Erhong Zhang (3)
Lisi Huang (2) (4)
Wenfang Li (2) (5)
Pei Liang (2) (5)
Xiaoyun Wang (2) (5)
Jin Xu (2) (5)
Yan Huang (2) (5)
Xinbing Yu (2) (5) - 关键词：Clonorchis sinensis ; Glyceraldehyde ; 3 ; phosphate dehydrogenase ; Molecular function ; Enzyme activity ; Expression pattern
- 刊名：Parasitology Research
- 出版年：2014
- 出版时间：December 2014
- 年：2014
- 卷：113
- 期：12
- 页码：4543-4553
- 全文大小：2,390 KB
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15. Huang Y, Chen WJ, Wang XY, Liu HL, Chen YY, Guo L, Luo F, Sun JF, Mao Q, Liang P, Xie ZZ, Zhou CH, Tian YL, Lv XL, Huang LS, Zhou JJ, Hu Y, Li R, Zhang F, Lei HL, Li WF, Hu XC, Liang C, Xu J, Li XR, Yu XB (2013a) The carcinogenic liver fluke, / Clonorchis sinensis: new assembly, reanno - 作者单位：Yue Hu (1) (2)
Erhong Zhang (3)
Lisi Huang (2) (4)
Wenfang Li (2) (5)
Pei Liang (2) (5)
Xiaoyun Wang (2) (5)
Jin Xu (2) (5)
Yan Huang (2) (5)
Xinbing Yu (2) (5)
1. Department of Clinical Laboratory, The Second People’s Hospital of Hefei, Hefei City, China
2. Department of Parasitology, Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou, China
3. Department of Infertility and Sexual Medicine, The Third Affiliated Hospital of Sun Yat-Sen University, Guangzhou, China
4. Department of Clinical Laboratory, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, China
5. Key Laboratory for Tropical Diseases Control, Sun Yat-Sen University, Ministry of Education, Guangzhou, China - ISSN：1432-1955
文摘
Globally, 15-0 million people are infected with Clonorchis sinensis (C. sinensis) which results in clonorchiasis. In China, clonorchiasis is considered to be one of the fastest-growing food-borne parasitic diseases. That more key molecules of C. sinensis are characterized will be helpful to understand biology and pathogenesis of the carcinogenic liver fluke. Glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) from many species have functions other than their catalytic role in glycolysis. In the present study, we analyzed the sequence and structure of GAPDH from C. sinensis (CsGAPDH) by using bioinformatics tools and obtained its recombinant protein by prokaryotic expression system, to learn its expression profiles and molecular property. CsGAPDH could bind to human intrahepatic biliary epithelial cell in vivo and in vitro by the method of immunofluorescence assays. CsGAPDH also disturbed in lumen of biliary tract near to the parasite in the liver of infected rat. Western blotting analysis together with immunofluorescence assay indicated that CsGAPDH was a component of excretory/secretory proteins (CsESPs) and a surface-localized protein of C. sinensis. Quantitative real-time PCR (Q-PCR) and Western blotting demonstrated that CsGAPDHs are expressed at the life stages of adult worm, metacercaria, and egg, but the expression levels were different from each other. Recombinant CsGAPDH (rCsGAPDH) was confirmed to have the capacity to catalyze the conversion of glyceraldehyde 3-phosphate to D-glycerate 1,3-bisphosphate which was inhibited by AMP in a dose-dependent manner. In addition, rCsGAPDH was able to interact with human plasminogen in a dose-dependent manner by ELISA. The interaction could be inhibited by lysine. The plasminogen binding capacity of rCsGAPDH along with the distribution of CsGAPDH in vivo and in the liver of C. sinensis-infected rat hinted that surface-localized CsGAPDH might play an important role in host invasion of the worm besides its glycolytic activity. Our work will be a cornerstone for getting more messages about CsGAPDH and its role in biology and parasitism of C. sinensis.