Molecular cloning and characterization of an antigenic protein with a repeating region from Clonorchis sinensis.
- Authors
- Kim, T.Y.; Kang, S.Y.; Ahn, I.Y.; Cho, S.Y.; Hong, S.J.
- Issue Date
- Mar-2001
- Citation
- The Korean journal of parasitology, v.39, no.1, pp 57 - 66
- Pages
- 10
- Journal Title
- The Korean journal of parasitology
- Volume
- 39
- Number
- 1
- Start Page
- 57
- End Page
- 66
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/26303
- DOI
- 10.3347/kjp.2001.39.1.57
- ISSN
- 0023-4001
1738-0006
- Abstract
- 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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