Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis

<p>Abstract</p> <p>Background</p> <p>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...

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Main Authors: Zhou Chenhui, Lv Xiaoli, Li Xuerong, Wang Xiaoyun, Chen Wenjun, Deng Chuanhuan, Lei Huali, Men Jingtao, Fan Yongxiu, Liang Chi, Yu Xinbing
Format: Article
Language:English
Published: BMC 2011-07-01
Series:Parasites & Vectors
Online Access:http://www.parasitesandvectors.com/content/4/1/149
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spelling doaj-287fdeb6f73749bcab7304b361d8d1ad2020-11-24T23:56:00ZengBMCParasites & Vectors1756-33052011-07-014114910.1186/1756-3305-4-149Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasisZhou ChenhuiLv XiaoliLi XuerongWang XiaoyunChen WenjunDeng ChuanhuanLei HualiMen JingtaoFan YongxiuLiang ChiYu Xinbing<p>Abstract</p> <p>Background</p> <p>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 <it>Clonorchis sinensis </it>(<it>Cs</it>CB) and to investigate its diagnostic value for human helminthiases.</p> <p>Results</p> <p>The predicted amino acid sequence of the cathepsin B of <it>C. sinensis </it>shared 63%, 52%, 50% identity with that of <it>Schistosoma japonicum</it>, <it>Homo sapiens </it>and <it>Fasciola hepatica</it>, respectively. Sequence encoding proenzyme of <it>Cs</it>CB was overexpressed in <it>Escherichia coli</it>. Reverse transcription PCR experiments revealed that <it>Cs</it>CB transcribed in both adult worm and metacercaria of <it>C. sinensis</it>. <it>Cs</it>CB was identified as a <it>C. sinensis </it>excretory/secretory product by immunoblot assay, which was consistent with immunohistochemical localization showing that <it>Cs</it>CB was especially expressed in the intestine of <it>C. sinensis </it>adults. Both ELISA and western blotting analysis showed recombinant <it>Cs</it>CB could react with human sera from clonorchiasis and other helminthiases.</p> <p>Conclusions</p> <p>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.</p> http://www.parasitesandvectors.com/content/4/1/149
collection DOAJ
language English
format Article
sources DOAJ
author Zhou Chenhui
Lv Xiaoli
Li Xuerong
Wang Xiaoyun
Chen Wenjun
Deng Chuanhuan
Lei Huali
Men Jingtao
Fan Yongxiu
Liang Chi
Yu Xinbing
spellingShingle Zhou Chenhui
Lv Xiaoli
Li Xuerong
Wang Xiaoyun
Chen Wenjun
Deng Chuanhuan
Lei Huali
Men Jingtao
Fan Yongxiu
Liang Chi
Yu Xinbing
Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
Parasites & Vectors
author_facet Zhou Chenhui
Lv Xiaoli
Li Xuerong
Wang Xiaoyun
Chen Wenjun
Deng Chuanhuan
Lei Huali
Men Jingtao
Fan Yongxiu
Liang Chi
Yu Xinbing
author_sort Zhou Chenhui
title Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
title_short Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
title_full Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
title_fullStr Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
title_full_unstemmed Molecular characterization of cathepsin B from <it>Clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
title_sort molecular characterization of cathepsin b from <it>clonorchis sinensis </it>excretory/secretory products and assessment of its potential for serodiagnosis of clonorchiasis
publisher BMC
series Parasites & Vectors
issn 1756-3305
publishDate 2011-07-01
description <p>Abstract</p> <p>Background</p> <p>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 <it>Clonorchis sinensis </it>(<it>Cs</it>CB) and to investigate its diagnostic value for human helminthiases.</p> <p>Results</p> <p>The predicted amino acid sequence of the cathepsin B of <it>C. sinensis </it>shared 63%, 52%, 50% identity with that of <it>Schistosoma japonicum</it>, <it>Homo sapiens </it>and <it>Fasciola hepatica</it>, respectively. Sequence encoding proenzyme of <it>Cs</it>CB was overexpressed in <it>Escherichia coli</it>. Reverse transcription PCR experiments revealed that <it>Cs</it>CB transcribed in both adult worm and metacercaria of <it>C. sinensis</it>. <it>Cs</it>CB was identified as a <it>C. sinensis </it>excretory/secretory product by immunoblot assay, which was consistent with immunohistochemical localization showing that <it>Cs</it>CB was especially expressed in the intestine of <it>C. sinensis </it>adults. Both ELISA and western blotting analysis showed recombinant <it>Cs</it>CB could react with human sera from clonorchiasis and other helminthiases.</p> <p>Conclusions</p> <p>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.</p>
url http://www.parasitesandvectors.com/content/4/1/149
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