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...
Main Authors: | , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2011-07-01
|
Series: | Parasites & Vectors |
Online Access: | http://www.parasitesandvectors.com/content/4/1/149 |
id |
doaj-287fdeb6f73749bcab7304b361d8d1ad |
---|---|
record_format |
Article |
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 |
work_keys_str_mv |
AT zhouchenhui molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT lvxiaoli molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT lixuerong molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT wangxiaoyun molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT chenwenjun molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT dengchuanhuan molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT leihuali molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT menjingtao molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT fanyongxiu molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT liangchi molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis AT yuxinbing molecularcharacterizationofcathepsinbfromitclonorchissinensisitexcretorysecretoryproductsandassessmentofitspotentialforserodiagnosisofclonorchiasis |
_version_ |
1725460209431740416 |