MiR-101 regulates HSV-1 replication by targeting ATP5B

Zheng, Shufang; Li, Yixuan; Zhang, Yan; Li, Xin; Tang, Hua

doi:10.1016/j.antiviral.2011.01.008

Cited by 104 publications

(71 citation statements)

References 35 publications

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“…ATP synthase subunit beta (ATP5B) is also downregulated in herpes simplex virus infection for productive replication [64]. The lipid metabolism protein, mitochondrial enoyl-CoA hydratase (ECHS1), suppresses STAT3 signaling in active tumor cells [65].…”

Section: Discussionmentioning

confidence: 99%

Cellular proteome alterations in response to enterovirus 71 and coxsackievirus A16 infections in neuronal and intestinal cell lines

Chan

Sam

Lai

et al. 2015

Journal of Proteomics

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Section: Discussionmentioning

confidence: 99%

Cellular proteome alterations in response to enterovirus 71 and coxsackievirus A16 infections in neuronal and intestinal cell lines

Chan

Sam

Lai

et al. 2015

Journal of Proteomics

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“…It is worth to mention that ATP synthase subunits have been reported as targets of several viral proteins acting as pro-viral factors regulating virus replication, transmission and propagation in the host4243. The SQRD also represents an interesting candidate as PtpA substrate since this enzyme participates in cell metabolic and microbicidal pathways in cells44454647.…”

Section: Discussionmentioning

confidence: 99%

New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state

Margenat

Labandera

Gil

et al. 2015

Sci Rep

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The bacterial protein tyrosine phosphatase PtpA is a key virulence factor released by Mycobacterium tuberculosis in the cytosol of infected macrophages. So far only two unrelated macrophage components (VPS33B, GSK3α) have been identified as PtpA substrates. As tyrosine phosphatases are capable of using multiple substrates, we developed an improved methodology to pull down novel PtpA substrates from an enriched P-Y macrophage extract using the mutant PtpA D126A. This methodology reduced non-specific protein interactions allowing the identification of four novel putative PtpA substrates by MALDI-TOF-MS and nano LC-MS: three mitochondrial proteins - the trifunctional enzyme (TFP), the ATP synthase, and the sulfide quinone oxidoreductase - and the cytosolic 6-phosphofructokinase. All these proteins play a relevant role in cell energy metabolism. Using surface plasmon resonance, PtpA was found to bind immunopurified human TFP through its catalytic site since TFP-PtpA association was inhibited by a specific phosphatase inhibitor. Moreover, PtpA wt was capable of dephosphorylating immunopurified human TFP in vitro supporting that TFP may be a bona fide PtpA susbtrate. Overall, these results suggest a novel scenario where PtpA-mediated dephosphorylation may affect pathways involved in cell energy metabolism, particularly the beta oxidation of fatty acids through modulation of TFP activity and/or cell distribution.

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“…Notably, the LAT locus encodes several miRNAs (Flores et al, 2013; Jurak et al, 2010; Tang et al, 2008; Tang et al, 2009; Umbach et al, 2008), which are differentially expressed during acute infection and latent infection (Kramer et al, 2011; Tang et al, 2008; Umbach et al, 2008) and have been hypothesized to play a role in repressing lytic gene expression. Some host miRNAs have also been suggested to play a role in HSV infection (Hill et al, 2009; Mulik et al, 2012; Zheng et al, 2011). However, repression of HSV gene expression by host miRNAs has not been demonstrated.…”

Section: Introductionmentioning

confidence: 99%

A Neuron-Specific Host MicroRNA Targets Herpes Simplex Virus-1 ICP0 Expression and Promotes Latency

Pan

Flores

Umbach

et al. 2014

Cell Host & Microbe

135

141

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Summary After infecting peripheral sites, herpes simplex virus (HSV) invades the nervous system and initiates latent infection in sensory neurons. Establishment and maintenance of HSV latency requires host survival, and entails repression of productive cycle (“lytic”) viral gene expression. We find that a neuron-specific microRNA, miR-138, represses expression of ICP0, a viral transactivator of lytic gene expression. A mutant HSV-1 (M138) with disrupted miR-138 target sites in ICP0 mRNA exhibits enhanced expression of ICP0 and other lytic proteins in infected neuronal cells in culture. Following corneal inoculation, M138-infected mice have higher levels of ICP0 and lytic transcripts in trigeminal ganglia during establishment of latency, and exhibit increased mortality and encephalitis symptoms. After full establishment of latency, the fraction of trigeminal ganglia harboring detectable lytic transcripts is greater in M138-infected mice. Thus, miR-138 is a neuronal factor that represses HSV-1 lytic gene expression, promoting host survival and viral latency.

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MiR-101 regulates HSV-1 replication by targeting ATP5B

Cited by 104 publications

References 35 publications

Cellular proteome alterations in response to enterovirus 71 and coxsackievirus A16 infections in neuronal and intestinal cell lines

Cellular proteome alterations in response to enterovirus 71 and coxsackievirus A16 infections in neuronal and intestinal cell lines

New potential eukaryotic substrates of the mycobacterial protein tyrosine phosphatase PtpA: hints of a bacterial modulation of macrophage bioenergetics state

A Neuron-Specific Host MicroRNA Targets Herpes Simplex Virus-1 ICP0 Expression and Promotes Latency

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