Molecular cloning, expression, and characterization of cyclophilin A from Clonorchis sinensis

Wu, Weihua; Chen, Jiajia; Zeng, Suxiang; Zhang, Zhaoping; Gan, Wen-jia; Yu, Xinbing; Hu, Xuchu

doi:10.1007/s00436-011-2262-2

Cited by 8 publications

(4 citation statements)

References 37 publications

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“…In some species of yeast and Cryptococcus, the CsA-CyPA interaction can prevent growth and recovery from stress. Secreted CyPA can act as a growth factor involved with oncogenesis and metastasis in several types of tumor cells, as a chemoattractant to recruit inflammatory cells, and facilitates viral infections and cardiovascular disease Wu et al 2011). Several researches reported that several cyclophilin genes in schistosome had been identified (Gourlay et al 2007;Argaet et al 1992;Kiang et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and characterization of a cyclophilin A homologue from Schistosoma japonicum

Peng

Hong

et al. 2012

Parasitol Res

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Cyclophilins belong to a group of proteins that have peptidyl-prolyl cis-trans isomerase activity and have been identified in all cell types and all organisms studied. In both prokaryotes and eukaryotes, they have been characterized as functional chaperones and involved in cell signaling. In the present study, Sj cyclophilin A (CyPA) was cloned, characterized, and subcloned into a prokaryotic expression vector to produce soluble recombinant rSjCyPA protein. qPCR analysis revealed that SjCyPA was expressed at each schistosome developmental stage tested, but reached its highest levels at days 7 and 13. In addition, the gene was also found to be significantly downregulated in adult worms from Microtus fortis. The SjCyPA protein was located on the subtegumental musculature of Schistosoma japonicum as determined by immunohistochemical staining analysis. Direct administration of recombinant SjCyPA to mice induced partial protective efficacy against subsequent schistosome infection. Length and width of adult worms and expression of SjCyPA were significantly decreased in the immunized groups, at 42 days post-infection, indicating that immunization with recombinant SjCyPA may suppress the schistosomes development. rSjCyPA can also react with sera from S. japonicum-infected rabbits at different time points. The data presented here suggest that SjCyPA may be an important molecule in the schistosome life-cycle and may be useful as a therapeutic target to treat schistosomiasis infection or as a potential diagnostic antigen.

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Section: Introductionmentioning

confidence: 99%

Molecular cloning and characterization of a cyclophilin A homologue from Schistosoma japonicum

Peng

Hong

et al. 2012

Parasitol Res

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“…Recombinant CsCyPA (rCsCyPA) was produced in a previous study [ 16 ]. Furthermore, recombinant CyPA of Schistosoma japonicum (rSjCyPA), mouse (rMuCyPA) and human (rHsCyPA) were produced using the same process.…”

Section: Methodsmentioning

confidence: 99%

“…A C.sinensis adult full-length complementary DNA (cDNA) plasmid library was established in our laboratory in 2004 [ 15 ]. CsCyPA was found to be an excretory protein and able to induce high anti-CsCyPA antibodies (anti-CsCyPAs) titers in patients infected with C.sinensis in our previous study [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

Prognosis of sepsis induced by cecal ligation and puncture in mice improved by anti-Clonorchis Sinensis cyclopholin a antibodies

et al. 2015

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BackgroundCyclophilin A (CyPA), a ubiquitously distributed intracellular protein, is thought to be one of the important inflammatory factors and plays a significant role in the development process of sepsis. In the form of cytokine, CyPA deteriorates sepsis by promoting intercellular communication, apoptosis of endothelial cells and chemotactic effect on inflammatory cells. In our previous study, cyclophilin A of Clonorchis sinensis (CsCyPA), a type of excretory-secretory antigen, could induce the patients infected with Clonorchis sinensis to produce specific anti-CsCyPA antibodies. In this study, we investigated whether anti-CsCyPA antibodies could cross-react with CyPA and then play a protective role against sepsis, just like other anti-cytokine antagonists.MethodsThe mice model with sepsis was established with cecal ligation and puncture (CLP). Fifty mg/kg purified anti-CsCyPA antibodies were injected via the caudal vein 6 h after the CLP operation, and persistent observation was performed for 72 h. Blood samples and tissues were collected at 6 h, 12 h, 24 h, 48 h and 72 h after CLP. Cytokines in serum were measured by ELISA. Lung and mesentery tissues were stained with hematoxylin-eosin. Endothelial cells (ECs) isolated from murine aorta were co-cultured with CyPA of mice (MuCyPA) and anti-CsCyPAs for 24 h, then, viability was measured by Cell Counting Kit-8.ResultsAnti-CsCyPA antibodies could combine with MuCyPA and inhibite its peptidyl prolyl isomerase (PPIase) activity. In the antibodies treatment group, blood coagulation indicators including PT, aPTT, D-dimer and platelet count were obviously more ameliorative, the proinflammary factors like IL-6, TNF-α, IL-1β were significantly lower at 12 h and 24 h after surgery and the viability of ECs was significantly improved compared to those in the control group. Furthermore, the survival rate was elevated, ranging from 10.0 % to 45.0 % compared to the control group.ConclusionsThese antibodies may have a favorable effect on sepsis via inhibition of enzymic activity or protection of endothelial cells.

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“…The other well-known cancer inducing parasite Opisthorchis and Clonorchis have also been shown to exhibit PPIase activity. Clonorchis sinensis adult in biliary ducts has been shown to release C. sinensis cyclophilin A, a protein with PPIase activity, into the liver and play a role in inflammation and biliary epithelium proliferation and adenomatoid hyperplasia ( 9 ).…”

mentioning

confidence: 99%

Commentary: Theileria Parasites Secrete a Prolyl Isomerase to Maintain Host Leukocyte Transformation

2018

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Molecular cloning, expression, and characterization of cyclophilin A from Clonorchis sinensis

Cited by 8 publications

References 37 publications

Molecular cloning and characterization of a cyclophilin A homologue from Schistosoma japonicum

Molecular cloning and characterization of a cyclophilin A homologue from Schistosoma japonicum

Prognosis of sepsis induced by cecal ligation and puncture in mice improved by anti-Clonorchis Sinensis cyclopholin a antibodies

Commentary: Theileria Parasites Secrete a Prolyl Isomerase to Maintain Host Leukocyte Transformation

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