A recombinant pore-forming peptide of Clonorchis sinensis, clonorin, was evaluated for serodiagnostic reagent of clonorchiasis by enzyme-linked immunosorbent assay detecting IgG antibody. Recombinant clonorin showed 100% specificity and low sensitivity for sera of human clonorchiasis. In contrast, C. sinensis crude antigen revealed lower specificity and higher sensitivity than recombinant clonorin did. In sera of experimental rabbits, clonorin-specific IgG antibody was increased remarkably 8 weeks after the infection and retained around level of OD(490)=0.2 for 1 year. With excellent antigenic specificity, it is suggested that the recombinant clonorin can be used as an ingredient of the cocktail antigen for serodiagnosis of clonorchiasis from early stages of the infection.
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http://dx.doi.org/10.1016/s1383-5769(03)00002-3 | DOI Listing |
Parasitol Int
June 2003
Department of Parasitology, Chung-Ang University College of Medicine, Tongjak-gu, Seoul 156-756, South Korea.
A recombinant pore-forming peptide of Clonorchis sinensis, clonorin, was evaluated for serodiagnostic reagent of clonorchiasis by enzyme-linked immunosorbent assay detecting IgG antibody. Recombinant clonorin showed 100% specificity and low sensitivity for sera of human clonorchiasis. In contrast, C.
View Article and Find Full Text PDFBiochem Biophys Res Commun
September 2002
Department of Parasitology, Chung-Ang University College of Medicine, Tongjak-gu, 156-756, Seoul, Republic of Korea.
Peptides pore-forming in cell membrane have been identified from a wide range of animals. A putative pore-forming peptide deduced from a cDNA clone of Clonorchis sinensis (clonorin) was predicted to consist of four amphipathic alpha-helices. Clonorin contained six invariably conserved cysteine residues, identified to form three disulfide bonds.
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