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1 February 2013 Characterization and Expression of the Schistosoma japonicum Thioredoxin Peroxidase-2 Gene
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Abstract
We analyzed proteins that were differentially expressed by 10-day-old schistosomula from 3 different hosts and determined that a functional thioredoxin peroxidase-2 gene has an important antioxidant role in Schistosoma japonicum, which we investigated further. A full-length cDNA encoding the S. japonicum thioredoxin peroxidase-2 (SjTPx-2) had an open reading frame of 681 bp that encoded 226 amino acids with a signal peptide of 24 amino acids. A cDNA encoding SjTPx-2 without the signal peptide sequence was isolated from 42-day-old schistosome cDNAs. Real-time quantitative RT-PCR analysis revealed that SjTPx-2 was upregulated in 7- and 13-day-old schistosomes, while the expression level in females was around 2-fold higher than that in male worms at 42 days. SjTPx was subcloned into pET28a( ) and expressed as both inclusion bodies and supernatant in Escherichia coli BL21 (DE3) cells. Western blotting showed that the recombinant SjTPx-2 (rSjTPx-2) was immunogenic. The purified recombinant protein could form disulfide-bonded dimers and it had peroxidase activity in vitro. An immunoprotection experiment in BALB/c mice showed that vaccination with recombinant SjTPx-2 could induce 31.2% and 34.0% reductions in the numbers of worms and eggs in the liver, respectively. This study suggests that SjTPx-2 may be an important antioxidative enzyme in scavenging ROS, and it may be a potential vaccine candidate or new drug target for schistosomiasis.
Yang Hong, Yanhui Han, Zhiqiang Fu, Hongxiao Han, Chunhui Qiu, Min Zhang, Jianmei Yang, Yaojun Shi, Xiangrui Li and Jiaojiao Lin "Characterization and Expression of the Schistosoma japonicum Thioredoxin Peroxidase-2 Gene," Journal of Parasitology 99(1), (1 February 2013). https://doi.org/10.1645/GE-3096.1
Received: 16 January 2012; Accepted: 1 June 2012; Published: 1 February 2013
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