Unfolded protein response in hepatitis C virus infection

Chan, Shiu-Wan

doi:10.3389/fmicb.2014.00233

Cited by 57 publications

(57 citation statements)

References 225 publications

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“…Further, HCMV protein UL50 and its murine CMV homolog M50, can both downregulate IRE1 to suppress the UPR 111 . Hepatitis C virus also downregulates the IRE1-XBP1 pathway to promote viral replication 113,114 . Rotavirus can modulate the UPR via sequestration of UPR components 115,116 .…”

Section: Figurementioning

confidence: 99%

Bacteria, the endoplasmic reticulum and the unfolded protein response: friends or foes?

2014

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The Unfolded Protein Response (UPR) is a cytoprotective response aimed at restoring cellular homeostasis following physiological stress exerted on the endoplasmic reticulum (ER) that also invokes innate immune signaling in response to invading microorganisms. While the UPR is modulated by various viruses, recent evidence indicates that it also plays multiple roles during bacterial infections. In this Review, we describe how bacteria adapt to live in the ER and discuss the intricacies of bacterial interactions with the UPR, including how UPR subversion promotes the proliferation of intracellular bacterial pathogens and how the UPR contributes to innate immune responses against invading bacteria.

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Section: Figurementioning

confidence: 99%

Bacteria, the endoplasmic reticulum and the unfolded protein response: friends or foes?

2014

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“…However, the contributions of lipogenesis and fatty acid oxidation (FAox) in vivo are not known, since the actual activity of these pathways has not been assessed. Importantly, ER stress has been implicated in a number of chronic diseases that result in lipid dysregulation, including obesity (Özcan et al, 2004), alcoholism (Ji, 2014), viral hepatitis (Chan, 2014), and others. Thus, the mechanisms leading from ER stress to lipid dysregulation are of considerable physiological importance.…”

Section: Introductionmentioning

confidence: 99%

ER Stress Inhibits Liver Fatty Acid Oxidation while Unmitigated Stress Leads to Anorexia-Induced Lipolysis and Both Liver and Kidney Steatosis

et al. 2017

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Summary The unfolded protein response (UPR), induced by endoplasmic reticulum (ER) stress, regulates the expression of factors that restore protein folding homeostasis. However, in the liver and kidney, ER stress also leads to lipid accumulation, accompanied at least in the liver by transcriptional suppression of metabolic genes. The mechanisms of this accumulation are unclear, including which pathways contribute to the phenotype in each organ. We combined gene expression profiling, biochemical assays, and untargeted lipidomics to understand the basis of stress-dependent lipid accumulation, taking advantage of enhanced hepatic and renal steatosis in mice lacking the ER stress sensor ATF6α. We found that impaired fatty acid oxidation contributed to the early development of steatosis in the liver, but not the kidney; while anorexia-induced lipolysis promoted late triglyceride and free fatty acid accumulation in both organs. These findings provide evidence for both direct and indirect regulation of peripheral metabolism by ER stress.

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“…Such perturbation (ER stress) occurs during viral propagation (Jheng et al . ) including hepatitis C virus (HCV) infection (Chan ).…”

Section: Introductionmentioning

confidence: 99%

Immature Core protein of hepatitis C virus induces an unfolded protein response through inhibition of ERAD‐L in a yeast model system

et al. 2017

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The structural protein Core of hepatitis C virus (HCV), a cytosolic protein, induces endoplasmic reticulum (ER) stress and unfolded protein response (UPR) in hepatocytes, and is responsible for the pathogenesis of persistent HCV infection. Using yeast as a model system, we evaluated mechanisms underlying Core-induced interference of ER homeostasis and UPR, and found that UPR is induced by the immature Core (aa 1-191, Core191) but not by the mature Core (aa 1-177, Core177). Interestingly, Core191 inhibits both ERAD-L, a degradation system responsible for misfolded/unfolded proteins in the ER lumen, and ERAD-M, a degradation system responsible for proteins carrying a misfolded/unfolded region in the ER membrane. In contrast, Core177 inhibits ERAD-M but not ERAD-L. In addition, requirement of an unfolded protein sensor in the ER lumen suggested that inhibition of ERAD-L is probably responsible for Core191-dependent UPR activation. These results implicate inadequate maturation of Core as a trigger for induction of ER stress and UPR.

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Unfolded protein response in hepatitis C virus infection

Cited by 57 publications

References 225 publications

Bacteria, the endoplasmic reticulum and the unfolded protein response: friends or foes?

Bacteria, the endoplasmic reticulum and the unfolded protein response: friends or foes?

ER Stress Inhibits Liver Fatty Acid Oxidation while Unmitigated Stress Leads to Anorexia-Induced Lipolysis and Both Liver and Kidney Steatosis

Immature Core protein of hepatitis C virus induces an unfolded protein response through inhibition of ERAD‐L in a yeast model system

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