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Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
BACKGROUND: Cathepsin 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 (C...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3163202/ https://www.ncbi.nlm.nih.gov/pubmed/21794140 http://dx.doi.org/10.1186/1756-3305-4-149 |
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author | Chen, Wenjun Wang, Xiaoyun Li, Xuerong Lv, Xiaoli Zhou, Chenhui Deng, Chuanhuan Lei, Huali Men, Jingtao Fan, Yongxiu Liang, Chi Yu, Xinbing |
author_facet | Chen, Wenjun Wang, Xiaoyun Li, Xuerong Lv, Xiaoli Zhou, Chenhui Deng, Chuanhuan Lei, Huali Men, Jingtao Fan, Yongxiu Liang, Chi Yu, Xinbing |
author_sort | Chen, Wenjun |
collection | PubMed |
description | BACKGROUND: Cathepsin 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. RESULTS: The 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. CONCLUSIONS: Our findings revealed that secreted CsCB may play an important role in the biology of C. sinensis and could be a diagnostic candidate for helminthiases. |
format | Online Article Text |
id | pubmed-3163202 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-31632022011-08-29 Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis Chen, Wenjun Wang, Xiaoyun Li, Xuerong Lv, Xiaoli Zhou, Chenhui Deng, Chuanhuan Lei, Huali Men, Jingtao Fan, Yongxiu Liang, Chi Yu, Xinbing Parasit Vectors Research BACKGROUND: Cathepsin 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. RESULTS: The 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. CONCLUSIONS: Our findings revealed that secreted CsCB may play an important role in the biology of C. sinensis and could be a diagnostic candidate for helminthiases. BioMed Central 2011-07-27 /pmc/articles/PMC3163202/ /pubmed/21794140 http://dx.doi.org/10.1186/1756-3305-4-149 Text en Copyright ©2011 Chen et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Chen, Wenjun Wang, Xiaoyun Li, Xuerong Lv, Xiaoli Zhou, Chenhui Deng, Chuanhuan Lei, Huali Men, Jingtao Fan, Yongxiu Liang, Chi Yu, Xinbing Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis |
title | Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis |
title_full | Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis |
title_fullStr | Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis |
title_full_unstemmed | Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis |
title_short | Molecular characterization of cathepsin B from Clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis |
title_sort | molecular characterization of cathepsin b from clonorchis sinensis excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3163202/ https://www.ncbi.nlm.nih.gov/pubmed/21794140 http://dx.doi.org/10.1186/1756-3305-4-149 |
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