ArticleParasitology research2013
Identification and immunological characterization of thioredoxin transmembrane-related protein from Clonorchis sinensis.
Article in Parasitology research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Perturbations of Metabolomic Profiling of Spleen From Rats Infected WithFrontiers in molecular biosciences · 2020Article
- Identification and Analysis of the Tegument Protein and Excretory-Secretory Products of the Carcinogenic Liver FlukeFrontiers in microbiology · 2020Article
- Multifunctional Thioredoxin-Like Protein from the Gastrointestinal Parasitic NematodesJournal of parasitology research · 2016Article
- Investigation on oxidative stress of nitric oxide synthase interacting protein from Clonorchis sinensis.Parasitology research · 2016Article
- Identification, immunolocalization, and characterization analyses of an exopeptidase of papain superfamily, (cathepsin C) from Clonorchis sinensis.Parasitology research · 2014Article
- Biochemical and immunological characterization of annexin B30 from Clonorchis sinensis excretory/secretory products.Parasitology research · 2014Article
- Identification, immunolocalization, and immunological characterization of nitric oxide synthase-interacting protein from Clonorchis sinensis.Parasitology research · 2014Article
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Authors and funding
12 authors at 1 institution in 1 country.
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Abstract
Thioredoxin transmembrane related protein (TMX), a member of thioredoxin superfamily, is localized to the endoplasmic reticulum and possesses a thioredoxin-like domain that plays an important role as an oxidoreductase. The functions of TMX in Clonorchis sinensis remain to be elucidated. In this study, we cloned and characterized a novel TMX of C. sinensis (CsTMX). The CsTMX cDNA sequence contained a 414-nucleotide open-reading frame encoding a protein of 137 amino acids. A thioredoxin domain was found in the position of aa21-117 and contained the putative active-site motif Cys-Pro-Ala-Cys. BLASTx analysis showed that CsTMX shared 39-57% amino acid identities with TMX of other organisms. Quantitative RT-PCR analysis demonstrated that CsTMX was differentially transcribed, with the highest level of expression in the adult worm stage and the lowest expression in egg stage. In addition, immunofluorescence assay showed CsTMX was localized in the tegument, vitelline gland, intestine, and intrauterine eggs of adult worm. Besides, immunoblot assay revealed that the recombinant CsTMX (rCsTMX) could be recognized by the sera from rats infected with C. sinensis and the sera from rats immunized by excretory-secretory products. Furthermore, analysis of the antibody isotype profile revealed that rats subcutaneously immunized with rCsTMX developed rCsTMX-specific antibody, which is dominance of IgG2a in sera. Meanwhile, production of IFN-γ was elevated strongly in the supernatants of spleen cell. The results collectively indicated that CsTMX might play an important role in the host-parasite interaction, as well as CsTMX probably involved in immunoregulation of host by inducing Th1-type dominated immune response in rats.
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