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KMID : 0425120010390010057
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Parasites, Hosts and Diseases
2001 Volume.39 No. 1 p.57 ~ p.66
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Molecular cloning and characterization of an antigenic protein with a repeating region from Clonorchis sinensis
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Sung Jong Hong/Tae Yun Kim
Shin Yong Kang/Il Young Ahn/Seung Yull Cho/Sung Jong Hong
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Abstract
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In the course of immunoscreening of Clonorchis sinensis cDNA library, a cDNA CsRP12 containing a tandem repeat was isolated. The cDNA CsRP12 encodes two putative peptides of open reading frames (ORFs) 1 and 2 (CsRP12-1 and -2). The repetitive region is composed of 15 repeats of 10 amino acids. Of the two putative peptides, CsRP12-1 was proline-rich and found to have homologues in several organisms. Recombinant proteins of the putative peptides were bacterially produced and purified by an affinity chromatography. Recombinant CsRP12-1 protein was recognized by sera of clonorchiasis patients and experimental rabbits, but recombinant CsRP12-2 was not. One of the putative peptide, CsRP12-1, is designated CsPRA, proline-rich antigen of C. sinensis. Both the C-termini of CsRP12-1 and -2 were bacterially produced and analysed to show no antigenicity. Recombinant CsPRA protein showed high sensitivity and specificity. In experimental rabbits, IgG antibodies to CsPRA was produced between 4 and 8 weeks after the infection and decreased thereafter over one year. These results indicate that CsPRA is equivalent to a natural protein and a useful antigenic protein for serodiagnosis of human clonorchiasis.
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KEYWORD
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Clonorchis sinensis, repetitive peptide, antigenic, proline-rich, CsPRA,
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