293 cells over‐expressing human ADI1 and CD81 are permissive for serum‐derived hepatitis C virus infection

Cheng, Ju‐Chien; Yeh, Yung-Ju; Pai, Li‐Mei; Chang, Ming‐Ling; Yeh, Chau‐Ting

doi:10.1002/jmv.21495

Cited by 12 publications

(21 citation statements)

References 37 publications

(50 reference statements)

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“…(iv) Protein folding. Several cochaperone proteins of the DNAJ protein family, which regulate the heat shock proteins HSP70 and HSP90 involved in HCV replication via NS3 viral protein (39), were upregulated, of which DNAJB1 is necessary for HCV replication (40). Several members of the immunophilin protein family, cis-trans prolyl isomerases that accelerate protein folding, were downregulated (FKBP5, FKBP7, FKBP3, FKBP9, FKBP1B, and FKBP1A), while cyclophilin B, which stimulates the function of the HCV RNA polymerase NS5B (41), was upregulated.…”

Section: Main Biological Processes Regulated By Hcv At the Translatiomentioning

confidence: 99%

Genome-Wide Analysis of Host mRNA Translation during Hepatitis C Virus Infection

Colman

Berre‐Scoul

Hernandez

et al. 2013

J Virol

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fIn the model of Huh-7.5.1 hepatocyte cells infected by the JFH1 hepatitis C virus (HCV) strain, transcriptomic and proteomic studies have revealed modulations of pathways governing mainly apoptosis and cell cycling. Differences between transcriptomic and proteomic studies pointed to regulations occurring at the posttranscriptional level, including the control of mRNA translation. In this study, we investigated at the genome-wide level the translational regulation occurring during HCV infection. Sucrose gradient ultracentrifugation followed by microarray analysis was used to identify translationally regulated mRNAs (mRNAs associated with ribosomes) from JFH1-infected and uninfected Huh-7.5.1 cells. Translationally regulated mRNAs were found to correspond to genes enriched in specific pathways, including vesicular transport and posttranscriptional regulation. Interestingly, the strongest translational regulation was found for mRNAs encoding proteins involved in pre-mRNA splicing, mRNA translation, and protein folding. Strikingly, these pathways were not previously identified, through transcriptomic studies, as being modulated following HCV infection. Importantly, the observed changes in host mRNA translation were directly due to HCV replication rather than to HCV entry, since they were not observed in JFH1-infected Huh-7.5.1 cells treated with a potent HCV NS3 protease inhibitor. Overall, this study highlights the need to consider, beyond transcriptomic or proteomic studies, the modulation of host mRNA translation as an important aspect of HCV infection.

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Section: Main Biological Processes Regulated By Hcv At the Translatiomentioning

confidence: 99%

Genome-Wide Analysis of Host mRNA Translation during Hepatitis C Virus Infection

Colman

Berre‐Scoul

Hernandez

et al. 2013

J Virol

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“…ADI1 is a downstream protein of ENOPH1 and has been shown to play an important role in cell apoptosis, oxidoreductase reaction and virus infection (Hirano et al, 2005; Oram et al, 2007; Cheng et al, 2009). Therefore, we speculated that ADI1 might mediate the effect of ENOPH1 on OGD-induced endothelial cell death.…”

Section: Resultsmentioning

confidence: 99%

“…ADI1 is a downstream molecule of ENOPH1 in methionine salvage pathway and has been shown to be implicated in cell apoptosis, cell growth inhibition, oxidoreductase reaction and virus infection (Hirano et al, 2005; Oram et al, 2007; Cheng et al, 2009). In addition, ADI1 is an oxidoreductase and can combine molecular oxygen donor to generate ROS (Oram et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Cerebral Microvascular Endothelial Cell Apoptosis after Ischemia: Role of Enolase-Phosphatase 1 Activation and Aci-Reductone Dioxygenase 1 Translocation

Zhang

Wang

Yang

et al. 2016

Front. Mol. Neurosci.

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Enolase-phosphatase 1 (ENOPH1), a newly discovered enzyme of the methionine salvage pathway, is emerging as an important molecule regulating stress responses. In this study, we investigated the role of ENOPH1 in blood brain barrier (BBB) injury under ischemic conditions. Focal cerebral ischemia induced ENOPH1 mRNA and protein expression in ischemic hemispheric microvessels in rats. Exposure of cultured brain microvascular endothelial cells (bEND3 cells) to oxygen-glucose deprivation (OGD) also induced ENOPH1 upregulation, which was accompanied by increased cell death and apoptosis reflected by increased 3-(4, 5-Dimethylthiazol-2-yl)-2, 5- diphenyltetrazolium bromide formation, lactate dehydrogenase release and TUNEL staining. Knockdown of ENOPH1 expression with siRNA or overexpressing ENOPH1 with CRISPR-activated plasmids attenuated or potentiated OGD-induced endothelial cell death, respectively. Moreover, ENOPH1 knockdown or overexpression resulted in a significant reduction or augmentation of reactive oxygen species (ROS) generation, apoptosis-associated proteins (caspase-3, PARP, Bcl-2 and Bax) and Endoplasmic reticulum (ER) stress proteins (Ire-1, Calnexin, GRP78 and PERK) in OGD-treated endothelial cells. OGD upregulated the expression of ENOPH1’s downstream protein aci-reductone dioxygenase 1 (ADI1) and enhanced its interaction with ENOPH1. Interestingly, knockdown of ENOPH1 had no effect on OGD-induced ADI1 upregulation, while it potentiated OGD-induced ADI1 translocation from the nucleus to the cytoplasm. Lastly, knockdown of ENOPH1 significantly reduced OGD-induced endothelial monolayer permeability increase. In conclusion, our data demonstrate that ENOPH1 activation may contribute to OGD-induced endothelial cell death and BBB disruption through promoting ROS generation and the activation of apoptosis associated proteins, thus representing a new therapeutic target for ischemic stroke.

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“…In a subsequent study, we demonstrated that human aci-reductone dioxygenase 1 (hADI1) over-expression in 293 cells enhances viral entry into cells but not replication of HCV [[20]]. ADI1, an MTA cycle enzyme, belongs to the cupin domain superfamily and has aci-reductone dioxygenase (ARD) enzymatic activity.…”

Section: Introductionmentioning

confidence: 99%

ADI1, a methionine salvage pathway enzyme, is required for Drosophila fecundity

et al. 2014

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BackgroundMethionine, an essential amino acid, is required for protein synthesis and normal cell metabolism. The transmethylation pathway and methionine salvage pathway (MTA cycle) are two major pathways regulating methionine metabolism. Recently, methionine has been reported to play a key role in Drosophila fecundity.ResultsHere, we revealed that the MTA cycle plays a crucial role in Drosophila fecundity using the mutant of aci-reductone dioxygenase 1 (DADI1), an enzyme in the MTA cycle. In dietary restriction condition, the egg production of adi1 mutant flies was reduced compared to that of control flies. This fecundity defect in mutant flies was rescued by reintroduction of Dadi1 gene. Moreover, a functional homolog of human ADI1 also recovered the reproduction defect, in which the enzymatic activity of human ADI1 is required for normal fecundity. Importantly, methionine supply rescued the fecundity defect in Dadi1 mutant flies. The detailed analysis of Dadi1 mutant ovaries revealed a dramatic change in the levels of methionine metabolism. In addition, we found that three compounds namely, methionine, SAM and Methionine sulfoxide, respectively, may be required for normal fecundity.ConclusionsIn summary, these results suggest that ADI1, an MTA cycle enzyme, affects fly fecundity through the regulation of methionine metabolism.

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293 cells over‐expressing human ADI1 and CD81 are permissive for serum‐derived hepatitis C virus infection

Cited by 12 publications

References 37 publications

Genome-Wide Analysis of Host mRNA Translation during Hepatitis C Virus Infection

Genome-Wide Analysis of Host mRNA Translation during Hepatitis C Virus Infection

Cerebral Microvascular Endothelial Cell Apoptosis after Ischemia: Role of Enolase-Phosphatase 1 Activation and Aci-Reductone Dioxygenase 1 Translocation

ADI1, a methionine salvage pathway enzyme, is required for Drosophila fecundity

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