ArticleParasites & vectors2011
Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis.
Article in Parasites & vectors, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- Novel recombinant proteins and peptides fromBiochemistry and biophysics reports · 2023Article
- Proteomics of Gnathostomiasis: A Way Forward for Diagnosis and Treatment Development.Pathogens (Basel, Switzerland) · 2021Review
- Clonorchis sinensis excretory-secretory products increase malignant characteristics of cholangiocarcinoma cells in three-dimensional co-culture with biliary ductal plates.PLoS pathogens · 2019Article
- Clonorchiasis sinensis detected by laparoscopic exploration of biliary tracts in two patients with obstructive jaundice.BMC infectious diseases · 2019Article
- Transcriptome and excretory-secretory proteome of infective-stage larvae of the nematode Gnathostoma spinigerum reveal potential immunodiagnostic targets for development.Parasite (Paris, France) · 2019Article
- Cysteine proteases as digestive enzymes in parasitic helminths.PLoS neglected tropical diseases · 2018Review
- Identification and characterization of Clonorchis sinensis cathepsin B proteases in the pathogenesis of clonorchiasis.Parasites & vectors · 2015Article
- Immunodiagnosis of opisthorchiasis using parasite cathepsin F.Parasitology research · 2015Article
- CsRNASET2 is an important component of Clonorchis sinensis responsible for eliciting Th2 immune response.Parasitology research · 2015Article
- Microscopic identification of possible Clonorchis/Opisthorchis infection in two Ghanaian women with undiagnosed abdominal discomfort: two case reports.Journal of medical case reports · 2014Article
- Identification, immunolocalization, and characterization analyses of an exopeptidase of papain superfamily, (cathepsin C) from Clonorchis sinensis.Parasitology research · 2014Article
- Characterization of the secreted cathepsin B cysteine proteases family of the carcinogenic liver fluke Clonorchis sinensis.Parasitology research · 2014Article
- Clonorchis sinensis infestation promotes three-dimensional aggregation and invasion of cholangiocarcinoma cells.PloS one · 2014Article
- Identification and characterization of the second cysteine protease inhibitor of Clonorchis sinensis (CsStefin-2).Parasitology research · 2014Article
- Molecular characterization and immune modulation properties of Clonorchis sinensis-derived RNASET2.Parasites & vectors · 2013Article
- Current drug targets for helminthic diseases.Parasitology research · 2013Review
- Molecular characterization of severin from Clonorchis sinensis excretory/secretory products and its potential anti-apoptotic role in hepatocarcinoma PLC cells.PLoS neglected tropical diseases · 2013Article
- Frontiers of parasitology research in the People's Republic of China: infection, diagnosis, protection and surveillance.Parasites & vectors · 2012Review
- Current status of food-borne trematode infections.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2012Review
- Molecular cloning and characterization of a cyclophilin A homologue from Schistosoma japonicum.Parasitology research · 2012Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCathepsin cysteine proteases play multiple roles in the life cycle of parasites such as food uptake, immune invasion and pathogenesis, making them valuable targets for diagnostic assays, vaccines and drugs. The purpose of this study was to identify a cathepsin B of Clonorchis sinensis (CsCB) and to investigate its diagnostic value for human helminthiases.
resultsThe predicted amino acid sequence of the cathepsin B of C. sinensis shared 63%, 52%, 50% identity with that of Schistosoma japonicum, Homo sapiens and Fasciola hepatica, respectively. Sequence encoding proenzyme of CsCB was overexpressed in Escherichia coli. Reverse transcription PCR experiments revealed that CsCB transcribed in both adult worm and metacercaria of C. sinensis. CsCB was identified as a C. sinensis excretory/secretory product by immunoblot assay, which was consistent with immunohistochemical localization showing that CsCB was especially expressed in the intestine of C. sinensis adults. Both ELISA and western blotting analysis showed recombinant CsCB could react with human sera from clonorchiasis and other helminthiases.
conclusionsOur findings revealed that secreted CsCB may play an important role in the biology of C. sinensis and could be a diagnostic candidate for helminthiases.
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