Molecular cloning and identification of a novel Clonorchis sinensis gene encoding a tegumental protein

The tegumental membrane of platyhelminth parasites is of crucial importance for modulation of the host response and parasite survival. A cDNA encoding a novel tegumental protein 20.8 kDa (TP20.8) was found by large-scale sequencing of a Clonorchis sinensis cDNA library. This new cDNA was 755 bp long...

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Veröffentlicht in:Parasitology research (1987) 2007-08, Vol.101 (3), p.737-742
Hauptverfasser: Zhou, Zhenwen, Hu, Xuchu, Huang, Yan, Hu, Huixia, Ma, Changling, Chen, Xiaoxiang, Hu, Fengyu, Xu, Jin, Lu, Fangli, Wu, Zhongdao, Yu, Xinbing
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container_title Parasitology research (1987)
container_volume 101
creator Zhou, Zhenwen
Hu, Xuchu
Huang, Yan
Hu, Huixia
Ma, Changling
Chen, Xiaoxiang
Hu, Fengyu
Xu, Jin
Lu, Fangli
Wu, Zhongdao
Yu, Xinbing
description The tegumental membrane of platyhelminth parasites is of crucial importance for modulation of the host response and parasite survival. A cDNA encoding a novel tegumental protein 20.8 kDa (TP20.8) was found by large-scale sequencing of a Clonorchis sinensis cDNA library. This new cDNA was 755 bp long containing an open reading frame of 555 bp, which encoded a 20.8-kDa protein with an isoelectric point of 4.33. The deduced amino acid sequence exhibits 40 and 37% identity to Schistosoma japonicum sj20.8 and Schistosoma mansoni Sm 20.8, respectively. TP20.8 transcripts were detected in the adult worm and metacercariae cDNA libraries of C. sinensis but not in the egg. Recombinant C. sinensis TP20.8 protein was produced and purified from Escherichia coli BL21. Using specific anti-recombinant TP20.8 protein sera, the TP20.8 protein was immunohistochemically localized to the outer-surface membrane of C. sinensis. The specificity and sensitivity of the recombinant antigen for serologic diagnosis was assessed by enzyme-linked immunosorbent assay using serum from 100 patients with clonorchiasis, 20 patients with schistosomiasis, and 30 negative controls. The sensitivity was 68%, and the specificity was 84%. The antigen was less useful for the serodiagnosis of clonorchiasis with IgG.
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A cDNA encoding a novel tegumental protein 20.8 kDa (TP20.8) was found by large-scale sequencing of a Clonorchis sinensis cDNA library. This new cDNA was 755 bp long containing an open reading frame of 555 bp, which encoded a 20.8-kDa protein with an isoelectric point of 4.33. The deduced amino acid sequence exhibits 40 and 37% identity to Schistosoma japonicum sj20.8 and Schistosoma mansoni Sm 20.8, respectively. TP20.8 transcripts were detected in the adult worm and metacercariae cDNA libraries of C. sinensis but not in the egg. Recombinant C. sinensis TP20.8 protein was produced and purified from Escherichia coli BL21. Using specific anti-recombinant TP20.8 protein sera, the TP20.8 protein was immunohistochemically localized to the outer-surface membrane of C. sinensis. 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Psychology</topic><topic>Gene Library</topic><topic>General aspects</topic><topic>General aspects and techniques. Study of several systematic groups. 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A cDNA encoding a novel tegumental protein 20.8 kDa (TP20.8) was found by large-scale sequencing of a Clonorchis sinensis cDNA library. This new cDNA was 755 bp long containing an open reading frame of 555 bp, which encoded a 20.8-kDa protein with an isoelectric point of 4.33. The deduced amino acid sequence exhibits 40 and 37% identity to Schistosoma japonicum sj20.8 and Schistosoma mansoni Sm 20.8, respectively. TP20.8 transcripts were detected in the adult worm and metacercariae cDNA libraries of C. sinensis but not in the egg. Recombinant C. sinensis TP20.8 protein was produced and purified from Escherichia coli BL21. Using specific anti-recombinant TP20.8 protein sera, the TP20.8 protein was immunohistochemically localized to the outer-surface membrane of C. sinensis. The specificity and sensitivity of the recombinant antigen for serologic diagnosis was assessed by enzyme-linked immunosorbent assay using serum from 100 patients with clonorchiasis, 20 patients with schistosomiasis, and 30 negative controls. The sensitivity was 68%, and the specificity was 84%. The antigen was less useful for the serodiagnosis of clonorchiasis with IgG.</abstract><cop>Berlin</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>17476530</pmid><doi>10.1007/s00436-007-0541-8</doi><tpages>6</tpages></addata></record>
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ispartof Parasitology research (1987), 2007-08, Vol.101 (3), p.737-742
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subjects Animals
Antibodies, Helminth - blood
Antigens, Helminth - chemistry
Antigens, Helminth - genetics
Antigens, Helminth - immunology
Antigens, Helminth - metabolism
Biological and medical sciences
Cats
Cloning, Molecular
Clonorchiasis - diagnosis
Clonorchiasis - parasitology
Clonorchis
Clonorchis sinensis
Clonorchis sinensis - genetics
Clonorchis sinensis - immunology
Clonorchis sinensis - metabolism
Enzyme-Linked Immunosorbent Assay
Escherichia coli
Fundamental and applied biological sciences. Psychology
Gene Library
General aspects
General aspects and techniques. Study of several systematic groups. Models
Helminth Proteins - chemistry
Helminth Proteins - genetics
Helminth Proteins - immunology
Helminth Proteins - metabolism
Humans
Immunoglobulin G - blood
Invertebrates
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - immunology
Membrane Proteins - metabolism
Molecular Sequence Data
Rats
Rats, Sprague-Dawley
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - immunology
Recombinant Proteins - metabolism
Schistosoma japonicum
Schistosoma mansoni
Sensitivity and Specificity
Sequence Analysis, DNA
title Molecular cloning and identification of a novel Clonorchis sinensis gene encoding a tegumental protein
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