Molecular cloning and characterization of an antigenic protein with a repeating region from Clonorchis sinensis
The Korean Journal of Parasitology
; : 57-66, 2001.
Article
in En
| WPRIM
| ID: wpr-67266
Responsible library:
WPRO
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.
Full text:
1
Index:
WPRIM
Main subject:
Recombinant Proteins
/
Molecular Sequence Data
/
Base Sequence
/
Repetitive Sequences, Nucleic Acid
/
Gene Library
/
Amino Acid Sequence
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Cloning, Molecular
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Clonorchis sinensis
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DNA, Helminth
/
Antigens, Helminth
Limits:
Animals
/
Humans
Language:
En
Journal:
The Korean Journal of Parasitology
Year:
2001
Type:
Article