Clonorchis sinensis: Expression, characterization, immunolocalization and serological reactivity of one excretory/secretory antigen-LPAP homologue

From a Clonorchis sinensis adult cDNA plasmid library, a cDNA clone encoding a novel lysophosphatidic acid phosphatase (LPAP) homologue was isolated. The predicted molecular weight of putative protein was 48.8 kDa and the deduced amino acid sequence had 45%, 32%, and 29% identity with LPAP of Schist...

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Veröffentlicht in:	Experimental parasitology 2007-10, Vol.117 (2), p.157-164
Hauptverfasser:	Hu, Fengyu, Yu, Xinbing, Ma, Changling, Zhou, Hongjuan, Zhou, Zhenwen, Li, Yanwen, Lu, Fangli, Xu, Jin, Wu, Zhongdao, Hu, Xuchu
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence amino acid sequences Animals Antibodies, Helminth - blood Antigens, Helminth - biosynthesis Antigens, Helminth - chemistry Antigens, Helminth - genetics Antigens, Helminth - immunology Biological and medical sciences Blotting, Western C. sinensis Cloning, Molecular Clonorchiasis - diagnosis Clonorchiasis - immunology Clonorchis sinensis Clonorchis sinensis - enzymology Clonorchis sinensis - genetics Clonorchis sinensis - immunology complementary DNA Consensus Sequence CsLPAP Danio rerio DNA, Complementary - chemistry DNA, Helminth - chemistry Electrophoresis, Polyacrylamide Gel ELISA Enzyme-Linked Immunosorbent Assay ES antigen excretory-secretory products excretory–secretory antigen Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology gene expression Gene Expression Regulation, Enzymologic Humans Immune Sera - immunology immunologic techniques IPTG isopropyl-β- d-thiogalactopyranoside Life cycle. Host-agent relationship. Pathogenesis Localization LPAP LPAP of Clonorchis sinensis lysophosphatidic acid phosphatase lysophosphatidic acid phosphatase gene molecular cloning Molecular Sequence Data nucleotide sequences Phosphoric Monoester Hydrolases - biosynthesis Phosphoric Monoester Hydrolases - chemistry Phosphoric Monoester Hydrolases - genetics Phosphoric Monoester Hydrolases - immunology polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate Protozoa recombinant antigens Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - isolation & purification Schistosoma japonicum SDS–PAGE Sequence Alignment sequence homology Serodiagnosis tissue distribution Trematode
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Zusammenfassung:	From a Clonorchis sinensis adult cDNA plasmid library, a cDNA clone encoding a novel lysophosphatidic acid phosphatase (LPAP) homologue was isolated. The predicted molecular weight of putative protein was 48.8 kDa and the deduced amino acid sequence had 45%, 32%, and 29% identity with LPAP of Schistosoma japonicum, Danio rerio, and Homo sapiens, respectively. Prediction of signal peptide and Western blot analysis indicated that the CsLPAP homologue was an excretory–secretory antigen (ES antigen) of C. sinensis. Immunostaining revealed that the CsLPAP was markedly localized in the intestinal cecum, seminal receptacle and eggs of the adult worm. The recombinant CsLPAP showed slightly higher sensitivity (82.14%) and specificity (85.86%) than the crude worm antigen by enzyme-linked immunosorbent assay (ELISA), a result which suggested that the recombinant antigen might be valuable in the serodiagnosis of human clonorchiasis.
ISSN:	0014-4894 1090-2449
DOI:	10.1016/j.exppara.2007.04.003