Enolase, a Cellular Glycolytic Enzyme, Is Required for Efficient Transcription of Sendai Virus Genome

Ogino, Tomoaki; Yamadera, Tadayuki; Nonaka, Takashi; Imajoh‐Ohmi, Shinobu; Mizumoto, Kiyohisa

doi:10.1006/bbrc.2001.5160

Cited by 37 publications

(27 citation statements)

References 43 publications

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“…Recent studies have demonstrated that some of these enzymes are multifaceted proteins rather than simple components of the glycolytic pathway. One of them, enolase, is involved in transcriptional regulation [37] and was shown to stimulate transcription of the Sendai virus genome [38], but it is unclear whether this is due to its glycolytic activity or an alternative function.…”

Section: Resultsmentioning

confidence: 99%

Differential Protein Modulation in Midguts of Aedes aegypti Infected with Chikungunya and Dengue 2 Viruses

et al. 2010

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BackgroundArthropod borne virus infections cause several emerging and resurgent infectious diseases. Among the diseases caused by arboviruses, dengue and chikungunya are responsible for a high rate of severe human diseases worldwide. The midgut of mosquitoes is the first barrier for pathogen transmission and is a target organ where arboviruses must replicate prior to infecting other organs. A proteomic approach was undertaken to characterize the key virus/vector interactions and host protein modifications that happen in the midgut for viral transmission to eventually take place.Methodology and Principal FindingsUsing a proteomics differential approach with two-Dimensional Differential in-Gel Electrophoresis (2D-DIGE), we defined the protein modulations in the midgut of Aedes aegypti that were triggered seven days after an oral infection (7 DPI) with dengue 2 (DENV-2) and chikungunya (CHIKV) viruses. Gel profile comparisons showed that the level of 18 proteins was modulated by DENV-2 only and 12 proteins were modulated by CHIKV only. Twenty proteins were regulated by both viruses in either similar or different ways. Both viruses caused an increase of proteins involved in the generation of reactive oxygen species, energy production, and carbohydrate and lipid metabolism. Midgut infection by DENV-2 and CHIKV triggered an antioxidant response. CHIKV infection produced an increase of proteins involved in detoxification.Conclusion/SignificanceOur study constitutes the first analysis of the protein response of Aedes aegypti's midgut infected with viruses belonging to different families. It shows that the differentially regulated proteins in response to viral infection include structural, redox, regulatory proteins, and enzymes for several metabolic pathways. Some of these proteins like antioxidant are probably involved in cell protection. On the other hand, we propose that the modulation of other proteins like transferrin, hsp60 and alpha glucosidase, may favour virus survival, replication and transmission, suggesting a subversion of the insect cell metabolism by the arboviruses.

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Section: Resultsmentioning

confidence: 99%

Differential Protein Modulation in Midguts of Aedes aegypti Infected with Chikungunya and Dengue 2 Viruses

et al. 2010

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“…Enolase is a glycolytic enzyme and has been found in small vesicles outside the cell [61, 62]; it binds to plasminogen and helps pathogens to invade [63]. Enolase is also found in viral particles [64–66] and is required for the transcription of Sendai virus [67]. Furthermore, enolase has been identified in the MG brush border of Ae.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Identification of Dengue Virus Binding Proteins inAedes aegyptiMosquitoes andAedes albopictusCells

Muñoz

Limón-Camacho

Tovar

et al. 2013

BioMed Research International

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The main vector of dengue in America is the mosquito Aedes aegypti, which is infected by dengue virus (DENV) through receptors of midgut epithelial cells. The envelope protein (E) of dengue virus binds to receptors present on the host cells through its domain III that has been primarily recognized to bind cell receptors. In order to identify potential receptors, proteins from mosquito midgut tissue and C6/36 cells were purified by affinity using columns with the recombinant E protein domain III (rE-DIII) or DENV particles bound covalently to Sepharose 4B to compare and evaluate their performance to bind proteins including putative receptors from female mosquitoes of Ae. aegypti. To determine their identity mass spectrometric analysis of purified proteins separated by polyacrylamide gel electrophoresis was performed. Our results indicate that both viral particles and rE-DIII bound proteins with the same apparent molecular weights of 57 and 67 kDa. In addition, viral particles bound high molecular weight proteins. Purified proteins identified were enolase, beta-adrenergic receptor kinase (beta-ARK), translation elongation factor EF-1 alpha/Tu, and cadherin.

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“…Phosphopyruvate hydratase is a key protein in the glycolytic pathway, catalyzing the conversion of 2-phosphoglycerate to phosphoenopyruvate, but it can also be a receptor for plasminogen [46,47] or a transcriptional repressor [45]. Together with phosphoglycerate kinase and tubulin, phosphopyruvate hydratase forms an active transcription initiation complex that enhances transcriptional elongation of the Sendai virus genome [48]. In addition, this enzyme has also been described as a stress protein induced by hypoxia [49].…”

Section: Discussionmentioning

confidence: 99%

Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon

Leu

Chang²,

et al. 2007

BMC Genomics

116

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Background: White spot syndrome (WSS) is a viral disease that affects most of the commercially important shrimps and causes serious economic losses to the shrimp farming industry worldwide. However, little information is available in terms of the molecular mechanisms of the host-virus interaction. In this study, we used an expressed sequence tag (EST) approach to observe global gene expression changes in white spot syndrome virus (WSSV)-infected postlarvae of Penaeus monodon.

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Enolase, a Cellular Glycolytic Enzyme, Is Required for Efficient Transcription of Sendai Virus Genome

Cited by 37 publications

References 43 publications

Differential Protein Modulation in Midguts of Aedes aegypti Infected with Chikungunya and Dengue 2 Viruses

Differential Protein Modulation in Midguts of Aedes aegypti Infected with Chikungunya and Dengue 2 Viruses

Proteomic Identification of Dengue Virus Binding Proteins inAedes aegyptiMosquitoes andAedes albopictusCells

Comparative analysis of differentially expressed genes in normal and white spot syndrome virus infected Penaeus monodon

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