Abstract
A cDNA clone encoding a homologue of transforming growth factor beta (TGF-β) receptor interacting protein 1 (TRIP-1) was recognized and isolated from full-length cDNA plasmid library of Clonorchis sinensis adult. TRIP-1 is a bifunctional molecule in all eukaryote, which modulates the signaling pathway of TGF-β as a phosphorylation substrate of TGF-β type II receptor kinase and controls ribosome assembly and mRNA translation as p36 subunit of the eukaryotic translation initiation factor 3. The structural and immunological characteristics of TRIP-1 from C. sinensis (CsTRIP-1) were analyzed by bioinformatics. The complete coding sequence was expressed in Escherichia coli, and the purified recombinant product was obtained. Western blotting with mixed sera from clonorchiasis patients was positive, whereas the normal was negative, suggesting it is a candidate of diagnostic antigen for clonorchiasis. CsTRIP-1 will aid to explore interaction between host and the parasite as well as the mechanism by which TGF-β controls the development of C. sinensis and participates in the pathogenesis.
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This work was supported by the National Natural Science Foundation grant funded by National Natural Science Foundation of China (no. 30771887).
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Hu, X., Zhou, H., Hu, F. et al. Recognition and characterization of TGF-β receptor interacting protein 1 (TRIP-1) containing WD40 repeats from Clonorchis sinensis by bioinformatics, cloning, and expression in Escherichia coli . Parasitol Res 103, 1151–1158 (2008). https://doi.org/10.1007/s00436-008-1109-y
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DOI: https://doi.org/10.1007/s00436-008-1109-y