Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production

Limjindaporn, Thawornchai; Wongwiwat, Wiyada; Noisakran, Sansanee; Srisawat, Chatchawan; Netsawang, Janjuree; Puttikhunt, Chunya; Kasinrerk, Watchara; Avirutnan, Panisadee; Thiemmeca, Somchai; Sriburi, Rungtawan; Sittisombut, Nopporn; Malasit, Prida; Yenchitsomanus, Pa‐thai

doi:10.1016/j.bbrc.2008.12.070

Cited by 89 publications

(78 citation statements)

References 30 publications

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“…Based on these results, it was hypothesized that CALR functioned at a step late during infection related to virus assembly (91). Our results using a DENV replicon confirm a role for CALR in DENV replication, but indicate that CALR acts at an earlier step in the DENV life cycle.…”

Section: Fig 3 Enriched Annotation Terms and Pathways Among The Humsupporting

confidence: 69%

“…Of the 20 DENV-human protein interactions identified in the literature, only the interaction between NS5 and STAT2 was also detected in this study (85,86). Other proteins in our data set (UBE2I, CALR, and PTBP1) were reported to interact with DENV proteins, though the interacting viral proteins differ from those identified here (87)(88)(89)(90)(91); these host factors may bind to multiple DENV proteins, as has previously been observed for other viruses (21), or may represent false-positives. PTBP1, which has been reported to bind to NS4A, also colocalized with NS1 and NS3 in DENVinfected cells (92), consistent with our finding that PTBP1 interacted with NS1 and NS3 in the yeast two-hybrid assay.…”

Section: Mapping the Denv-human Protein Interactionsupporting

confidence: 64%

“…Based on this data, it was proposed that CALR's critical role in viral production was related to virus protein folding or virion assembly (91). Our results are consistent with a requirement for CALR in DENV replication and do not rule out a role for CALR at a late step during infection.…”

Section: Fig 3 Enriched Annotation Terms and Pathways Among The Humsupporting

confidence: 51%

“…While this study was in progress, CALR was reported to bind to DENV envelope (E) protein and was shown to be required for DENV virus production (91). Based on this data, it was proposed that CALR's critical role in viral production was related to virus protein folding or virion assembly (91).…”

Section: Fig 3 Enriched Annotation Terms and Pathways Among The Hummentioning

confidence: 99%

“…Colocalization of CALR with DENV Proteins During Viral Infection-CALR was recently reported to bind to and colocalize with the DENV envelope protein (E) in infected cells, and to be required for DENV replication (91). Based on these results, it was hypothesized that CALR functioned at a step late during infection related to virus assembly (91).…”

Section: Fig 3 Enriched Annotation Terms and Pathways Among The Hummentioning

confidence: 99%

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A Physical Interaction Network of Dengue Virus and Human Proteins

Khadka

Vangeloff

Zhang

et al. 2011

Molecular & Cellular Proteomics

154

148

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Dengue virus (DENV), an emerging mosquito-transmitted pathogen capable of causing severe disease in humans, interacts with host cell factors to create a more favorable environment for replication. However, few interactions between DENV and human proteins have been reported to date. To identify DENV-human protein interactions, we used high-throughput yeast two-hybrid assays to screen the 10 DENV proteins against a human liver activation domain library. From 45 DNA-binding domain clones containing either full-length viral genes or partially overlapping gene fragments, we identified 139 interactions between DENV and human proteins, the vast majority of which are novel. These interactions involved 105 human proteins, including six previously implicated in DENV infection and 45 linked to the replication of other viruses. Human proteins with functions related to the complement and coagulation cascade, the centrosome, and the cytoskeleton were enriched among the DENV interaction partners. To determine if the cellular proteins were required for DENV infection, we used small interfering RNAs to inhibit their expression. Six of 12 proteins targeted (CALR, DDX3X, ERC1, GOLGA2, TRIP11, and UBE2I) caused a significant decrease in the replication of a DENV replicon. We further showed that calreticulin colocalized with viral dsRNA and with the viral NS3 and NS5 proteins in DENV-infected cells, consistent with a direct role for calreticulin in DENV replication. Human proteins that interacted with DENV had significantly higher average degree and betweenness than expected by chance, which provides additional support for the hypothesis that viruses preferentially target cellular proteins that occupy central position in the human protein interaction network. This study provides a valuable starting point for additional investigations into the roles of human proteins in

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Section: Fig 3 Enriched Annotation Terms and Pathways Among The Humsupporting

confidence: 69%

Section: Mapping the Denv-human Protein Interactionsupporting

confidence: 64%

Section: Fig 3 Enriched Annotation Terms and Pathways Among The Humsupporting

confidence: 51%

Section: Fig 3 Enriched Annotation Terms and Pathways Among The Hummentioning

confidence: 99%

Section: Fig 3 Enriched Annotation Terms and Pathways Among The Hummentioning

confidence: 99%

See 3 more Smart Citations

A Physical Interaction Network of Dengue Virus and Human Proteins

Khadka

Vangeloff

Zhang

et al. 2011

Molecular & Cellular Proteomics

154

148

View full text Add to dashboard Cite

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Characterization of putative Japanese encephalitis virus receptor molecules on microglial cells

Thongtan

Wikan

Wintachai

et al. 2012

Journal of Medical Virology

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Japanese encephalitis virus (JEV) a mosquito-borne flavivirus is a major cause of viral encephalitis in Asia. While the principle target cells for JEV in the central nervous system are believed to be neurons, microglia are activated in response to JEV and have been proposed to act as a long lasting virus reservoir. Viral attachment to a host cell is the first step of the viral entry process and is a critical mediator of tissue tropism. This study sought to identify molecules associated with JEV entry to microglial cells. Virus overlay protein-binding assay (VOPBA) and liquid chromatography-mass spectrometry (LC/MS/MS) identified the 37/67 kDa high-affinity laminin receptor protein and nucleolin as a potential JEV-binding proteins. These proteins were subsequently investigated for a contribution to JEV entry to mouse microglial BV-2 cells together with other possible candidate receptor molecules including Hsp70, Hsp90, GRP78, CD14, and CD4. In antibody mediated inhibition of infection experiments, both anti-laminin receptor and anti-CD4 antibodies significantly reduced virus entry while anti-Hsp70 and 90 antibodies produced a slight reduction. Significant inhibition of virus entry (up to 80%) was observed in the presence of lipopolysaccharide (LPS) which resulted in a complete down-regulation of CD4 and moderate down-regulation of CD14. These results suggest that multiple receptor proteins may mediate the entry of JEV to microglial cells, with CD4 playing a major role.

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Infection of epithelial cells with dengue virus promotes the expression of proteins favoring the replication of certain viral strains

Martínez-Betancur

Marín-Villa

Martínez-Gutiérrez

2013

Journal of Medical Virology

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Dengue virus (DENV) is the causative agent of dengue and severe dengue. To understand better the dengue virus-host interaction, it is important to determine how the expression of cellular proteins is modified due to infection. Therefore, a comparison of protein expression was conducted in Vero cells infected with two different DENV strains, both serotype 2: DENV-2/NG (associated with dengue) and DENV-2/16681 (associated with severe dengue). The viability of the infected cells was determined, and neither strain induced cell death at 48 hr. In addition, the viral genomes and infectious viral particles were quantified, and the genome of the DENV-2/16681 strain was determined to have a higher replication rate compared with the DENV-2/NG strain. Finally, the proteins from infected and uninfected cultures were separated using two-dimensional gel electrophoresis, and the differentially expressed proteins were identified by mass spectrometry. Compared with the uninfected controls, the DENV-2/NG- and DENV-2/16681-infected cultures had five and six differentially expressed proteins, respectively. The most important results were observed when the infected cultures were compared to each other (DENV-2/NG vs. DENV-2/16681), and 18 differentially expressed proteins were identified. Based on their cellular functions, many of these proteins were linked to the increase in the replication efficiency of DENV. Among the proteins were calreticulin, acetyl coenzyme A, acetyl transferase, and fatty acid-binding protein. It was concluded that the infection of Vero cells with DENV-2/NG or DENV-2/16681 differentially modifies the expression of certain proteins, which can, in turn, facilitate infection.

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Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production

Cited by 89 publications

References 30 publications

A Physical Interaction Network of Dengue Virus and Human Proteins

A Physical Interaction Network of Dengue Virus and Human Proteins

Characterization of putative Japanese encephalitis virus receptor molecules on microglial cells

Infection of epithelial cells with dengue virus promotes the expression of proteins favoring the replication of certain viral strains

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