ArticleParasitology research2012
Molecular cloning and characterization of a cyclophilin A homologue from Schistosoma japonicum.
Article in Parasitology research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- Comparative proteomics analysis ofFrontiers in cellular and infection microbiology · 2022Article
- iTRAQ-Based Comparative Proteomic Analysis of AdultFrontiers in microbiology · 2018Article
- Composition of the Schistosoma mansoni worm secretome: Identification of immune modulatory Cyclophilin A.PLoS neglected tropical diseases · 2017Article
- Microbial cyclophilins: specialized functions in virulence and beyond.World journal of microbiology & biotechnology · 2017Review
- Advances in the Diagnosis of Human Schistosomiasis.Clinical microbiology reviews · 2015Review
- Comparative characterization of microRNAs in Schistosoma japonicum schistosomula from Wistar rats and BALB/c mice.Parasitology research · 2015Article
- Cyclophilin A from Schistosoma japonicum promotes a Th2 response in mice.Parasites & vectors · 2013Article
- Citrate synthase from the liver fluke Fasciola hepatica.Parasitology research · 2013Article
- Comparison of the differential expression miRNAs in Wistar rats before and 10 days after S.japonicum infection.Parasites & vectors · 2013Article
- Salivary gland proteome of the human malaria vector, Anopheles campestris-like (Diptera: Culicidae).Parasitology research · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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Registered trials
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