Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production
Dengue virus infection is an important mosquito-borne disease and a public health problem worldwide. A better understanding of interactions between human cellular host and dengue virus proteins will provide insight into dengue virus replication and cellular pathogenesis. The glycosylated envelope pr...
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th-cmuir.6653943832-593902018-09-10T03:14:37Z Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production Thawornchai Limjindaporn Wiyada Wongwiwat Sansanee Noisakran Chatchawan Srisawat Janjuree Netsawang Chunya Puttikhunt Watchara Kasinrerk Panisadee Avirutnan Somchai Thiemmeca Rungtawan Sriburi Nopporn Sittisombut Prida Malasit Pa thai Yenchitsomanus Biochemistry, Genetics and Molecular Biology Dengue virus infection is an important mosquito-borne disease and a public health problem worldwide. A better understanding of interactions between human cellular host and dengue virus proteins will provide insight into dengue virus replication and cellular pathogenesis. The glycosylated envelope protein of dengue virus, DENV E, is processed in the endoplasmic reticulum of host cells and therefore reliant on host processing functions. The complement of host ER functions involved and nature of the interactions with DENV E has not been thoroughly investigated. By employing a yeast two-hybrid assay, we found that domain III of DENV E interacts with human immunoglobulin heavy chain binding protein (BiP). The relevance of this interaction was demonstrated by co-immunoprecipitation and co-localization of BiP and DENV E in dengue virus-infected cells. Using the same approach, association of DENV E with two other chaperones, calnexin and calreticulin was also observed. Knocking-down expression of BiP, calnexin, or calreticulin by siRNA significantly decreased the production of infectious dengue virions. These results indicate that the interaction of these three chaperones with DENV E plays an important role in virion production, likely facilitating proper folding and assembly of dengue proteins. © 2008 Elsevier Inc. All rights reserved. 2018-09-10T03:14:37Z 2018-09-10T03:14:37Z 2009-02-06 Journal 10902104 0006291X 2-s2.0-58149529737 10.1016/j.bbrc.2008.12.070 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=58149529737&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/59390 |
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Biochemistry, Genetics and Molecular Biology Thawornchai Limjindaporn Wiyada Wongwiwat Sansanee Noisakran Chatchawan Srisawat Janjuree Netsawang Chunya Puttikhunt Watchara Kasinrerk Panisadee Avirutnan Somchai Thiemmeca Rungtawan Sriburi Nopporn Sittisombut Prida Malasit Pa thai Yenchitsomanus Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production |
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Dengue virus infection is an important mosquito-borne disease and a public health problem worldwide. A better understanding of interactions between human cellular host and dengue virus proteins will provide insight into dengue virus replication and cellular pathogenesis. The glycosylated envelope protein of dengue virus, DENV E, is processed in the endoplasmic reticulum of host cells and therefore reliant on host processing functions. The complement of host ER functions involved and nature of the interactions with DENV E has not been thoroughly investigated. By employing a yeast two-hybrid assay, we found that domain III of DENV E interacts with human immunoglobulin heavy chain binding protein (BiP). The relevance of this interaction was demonstrated by co-immunoprecipitation and co-localization of BiP and DENV E in dengue virus-infected cells. Using the same approach, association of DENV E with two other chaperones, calnexin and calreticulin was also observed. Knocking-down expression of BiP, calnexin, or calreticulin by siRNA significantly decreased the production of infectious dengue virions. These results indicate that the interaction of these three chaperones with DENV E plays an important role in virion production, likely facilitating proper folding and assembly of dengue proteins. © 2008 Elsevier Inc. All rights reserved. |
format |
Journal |
author |
Thawornchai Limjindaporn Wiyada Wongwiwat Sansanee Noisakran Chatchawan Srisawat Janjuree Netsawang Chunya Puttikhunt Watchara Kasinrerk Panisadee Avirutnan Somchai Thiemmeca Rungtawan Sriburi Nopporn Sittisombut Prida Malasit Pa thai Yenchitsomanus |
author_facet |
Thawornchai Limjindaporn Wiyada Wongwiwat Sansanee Noisakran Chatchawan Srisawat Janjuree Netsawang Chunya Puttikhunt Watchara Kasinrerk Panisadee Avirutnan Somchai Thiemmeca Rungtawan Sriburi Nopporn Sittisombut Prida Malasit Pa thai Yenchitsomanus |
author_sort |
Thawornchai Limjindaporn |
title |
Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production |
title_short |
Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production |
title_full |
Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production |
title_fullStr |
Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production |
title_full_unstemmed |
Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production |
title_sort |
interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production |
publishDate |
2018 |
url |
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=58149529737&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/59390 |
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1681425242417790976 |