ArticleParasitology research2017
Biochemical properties and vaccine effect of recombinant TPx-3 from Schistosoma japonicum.
Article in Parasitology research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Helminth-derived molecules: Pathogenic and pharmacopeial roles.Journal of biomedical research · 2024Article
- Evaluation of the immunoprotective effects of eight recombinant proteins from Baylisascaris schroederi in mice model.Parasites & vectors · 2023Article
- Wound healing approach based on excretory-secretory product and lysate of liver flukes.Scientific reports · 2022Article
- Regulation of piglet T-cell immune responses by thioredoxin peroxidase fromFrontiers in microbiology · 2022Article
- Cadmium Stress Reprograms ROS/RNS Homeostasis inInternational journal of molecular sciences · 2020Article
- Analyses of the expression, immunohistochemical properties and serodiagnostic potential of Schistosoma japonicum peroxiredoxin-4.Parasites & vectors · 2020Article
- Role of the Pumilio gene in the reproductive system of Schistosoma japonicum.Parasitology research · 2020Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thioredoxin peroxidases (TPxs) play an important role in maintaining redox homeostasis and in protecting organisms from the accumulation of toxic reactive oxygen species (ROS). In this study, we isolated the thioredoxin peroxidase-3 gene of Schistosoma japonicum, SjTPx-3. The open reading frame (ORF) of SjTPx-3 was 663 bp encoding 220 amino acids with a molecular weight of 24.99 kDa and an isoelectric point of 6.20. Quantitative real-time reverse transcription-polymerase chain reaction indicated that SjTPx-3 was expressed in all different stages of the parasites, with highest expression in 35-day-old worms. The ORF of SjTPx-3 was subcloned into pET-32a (+) vectors and expressed in Escherichia coli. Recombinant SjTPx-3 (rSjTPx-3) was expressed as a soluble protein with good antigenicity, as demonstrated by western blotting. Immunohistochemical analysis revealed that SjTPx-3 was mainly localized on the tegument of the parasites. Mice vaccinated with rSjTPx-3 had a 37.02% (P < 0.05) reduction in worm burden and 56.52% (P < 0.05) reduction in liver egg production compared with control, unvaccinated mice. Enzyme-linked immunosorbent assay analysis demonstrated that rSjTPx-3 could induce high levels of anti-rSjTPx-3-specific IgG, IgG1, and IgG2a antibodies. Characteristic Th1 and Th2 immune response cytokines were detected by flow cytometry and were increased by rSjTPx-3. Taken together, these results suggest that SjTPx-3 is an antioxidant enzyme responsible for protecting S. japonicum from oxidative stress. rSjTPx-3 may represent a potential vaccine candidate and/or new drug target for patients with schistosomiasis.
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