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The ubiquitin-proteasome pathway is important for dengue virus infection in primary human endothelial cells

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dc.contributor.authorRattiyaporn Kanlayaen_US
dc.contributor.authorSa Nga Pattanakitsakulen_US
dc.contributor.authorSupachok Sinchaikulen_US
dc.contributor.authorShui Tein Chenen_US
dc.contributor.authorVisith Thongboonkerden_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherGenomics Research Center, Academia Sinicaen_US
dc.contributor.otherNational Taiwan Universityen_US
dc.date.accessioned2018-09-24T08:42:43Z
dc.date.available2018-09-24T08:42:43Z
dc.date.issued2010-10-01en_US
dc.description.abstractDengue hemorrhagic fever (DHF) and dengue shock syndrome (DSS) are the most severe forms of dengue virus infection with hemorrhage and plasma leakage. However, pathogenic mechanisms of DHF and DSS remain poorly understood. We therefore investigated host responses as determined by changes in the cellular proteome of primary human endothelial cells upon infection with dengue virus serotype 2 (DEN-2) at a multiplicity of infection (MOI) of 10 for 24 h. Two-dimensional PAGE and quantitative intensity analysis revealed 38 significantly altered protein spots (16 upregulated and 22 downregulated) in DEN-2-infected cells compared to mock controls. These altered proteins were successfully identified by mass spectrometry, including those involved in oxidative stress response, transcription and translation, cytoskeleton assembly, protein degradation, cell growth regulation, apoptosis, cellular metabolism, and antiviral response. The proteomic data were validated by Western blot analyses [upregulated ubiquitin-activating enzyme E1 (UBE1) and downregulated annexin A2] and an immunofluorescence study (upregulated MxA). Interestingly, we found that MxA was colocalized with DEN-2 viral capsid protein, strengthening its role as an antiviral protein. Moreover, we also identified upregulation of a proteasome subunit. Our functional study revealed the significant role of ubiquitination in dengue infection and UBE1 inhibition by its specific inhibitor (UBEI-41) caused a significant reduction in the level of viral protein synthesis and its infectivity. Our findings suggest that various biological processes were triggered in response to dengue infection, particularly antiviral IFN and ubiquitin-proteasome pathways. © 2010 American Chemical Society.en_US
dc.identifier.citationJournal of Proteome Research. Vol.9, No.10 (2010), 4960-4971en_US
dc.identifier.doi10.1021/pr100219yen_US
dc.identifier.issn15353907en_US
dc.identifier.issn15353893en_US
dc.identifier.other2-s2.0-77957366917en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/28634
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=77957366917&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemistryen_US
dc.titleThe ubiquitin-proteasome pathway is important for dengue virus infection in primary human endothelial cellsen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=77957366917&origin=inwarden_US
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