Tyrosine phosphorylation events during coxsackievirus B3 replication

Huber, Michael; Selinka, Hans‐Christoph; Kandolf, Reinhard

doi:10.1128/jvi.71.1.595-600.1997

Cited by 31 publications

(13 citation statements)

References 38 publications

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“…During infection with echovirus 1 and 7, ERK-1/2 activation was shown to be induced by 5 hours after infection, while p38 MAPK was activated by 10 hours after infection (25). CVB3 infection has been shown to induce tyrosine phosphorylation of host proteins in HeLa cells from 3 to 5 hours after infection (23). Sam68, a cellular target of Src's, interacts with the poliovirus RNAdependent RNA polymerase 3D (26) and associates with RasGAP in response to CVB3 infection (24).…”

Section: Discussionmentioning

confidence: 98%

“…Several viruses have evolved diverse mechanisms to stimulate signal transduction pathways that may promote viral replication, regulate host inflammatory responses to infection, or induce viral oncogenic transformation of cells. Reports of the effects of Enteroviruses on intracellular signal transduction pathways are limited and focus on later stages of infection, at the time of virus-induced host protein synthesis shutoff (23)(24)(25). During infection with echovirus 1 and 7, ERK-1/2 activation was shown to be induced by 5 hours after infection, while p38 MAPK was activated by 10 hours after infection (25).…”

Section: Discussionmentioning

confidence: 99%

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Enhanced ERK-1/2 activation in mice susceptible to coxsackievirus-induced myocarditis

Opavsky¹,

Martino²,

Rabinovitch³

et al. 2002

J. Clin. Invest.

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Group B coxsackieviral (CVB) infection commonly causes viral myocarditis. Mice are protected from CVB3 myocarditis by gene-targeted knockout of p56(Lck)(Lck), the Src family kinase (Src) essential for T cell activation. Extracellular signal-regulated kinase 1 and 2 (ERK-1/2) can influence cell function downstream of Lck. Using T cell lines and neonatal cardiac myocytes we investigated the role of ERK-1/2 in CVB3 infection. In Jurkat T cells ERK-1/2 is rapidly activated by CVB3; but, this response is absent in Lck-negative JCaM T cells. Inhibition of ERK-1/2 with UO126 reduced CVB3 titers in Jurkat cells, but not in JCaM cells. In cardiac myocytes CVB3 activation of ERK-1/2 is blocked by the Src inhibitor PP2. In addition, viral production in myocytes is decreased by Src or ERK-1/2 inhibition. In vitro, in both immune and myocardial cells, ERK-1/2 is activated by CVB3 downstream of Lck and other Src's and is necessary for efficient CVB3 replication. In vivo, following CVB3 infection, ERK-1/2 activation is evident in the myocardium. ERK-1/2 activation is intense in the hearts of myocarditis-susceptible A/J mice. In contrast, significantly less ERK-1/2 activation is found in the hearts of myocarditis-resistant C57BL/6 mice. Therefore, the ERK-1/2 response to CVB3 infection may contribute to differential host susceptibility to viral myocarditis.

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Enhanced ERK-1/2 activation in mice susceptible to coxsackievirus-induced myocarditis

Opavsky¹,

Martino²,

Rabinovitch³

et al. 2002

J. Clin. Invest.

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“…HeLa cells were pre‐incubated with increasing concentrations of various inhibitors as specified in the figure legends for 30 min. Cells were then infected with CVB3 (Kandolf strain, from Dr. Reinhard Kandolf [18], University of Tubingen, Germany) at a multiplicity of infection of 10 or mock infected with phosphate buffered saline (PBS) for 1 h. The infected cells were then washed with PBS and replaced with new DMEM containing fresh inhibitors.…”

Section: Methodsmentioning

confidence: 99%

Tripeptidyl peptidase II serves as an alternative to impaired proteasome to maintain viral growth in the host cells

et al. 2010

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a b s t r a c tThe ubiquitin-proteasome system is known to be utilized by coxsackievirus to facilitate its propagation within the host cells. The present study explores the role of tripeptidyl peptidase II (TPPII), a serine peptidase contributing to protein turnover by acting downstream of the proteasome, in regulating coxsackievirus infection. Inhibition of TPPII does not affect virus replication in cells with functional proteasome. However, when the proteasome is impaired, TPPII appears to serve as an alternative to maintain low levels of virus infection. Our results suggest an important function of TPPII in the maintenance of viral growth and may have implications for anti-viral therapy.

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“…The accompanying tyrosine phosphorylation events are of paramount importance in the regulation of neuronal cell death and microglial expression of proinflammatory cytokines (25,30,39,40). Accumulating evidence also shows that virus infection is able to initiate protein tyrosine phosphorylation in cellular and/or viral proteins after which affects viral adsorption, replication, and cytotoxicity (25,30,31,(41)(42)(43).…”

Section: Figmentioning

confidence: 99%

Enterovirus 71 infection caused neuronal cell death and cytokine expression in cultured rat neural cells

Chang

et al. 2015

IUBMB Life

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Fatal enterovirus type-71 (EV71) cases are associated with central nervous system infection characterized by inflammatory cell infiltration and activation, cytokine overproduction, and neuronal cell death. Although EV71 antigen has been detected in neurons and glia, the molecular mechanisms underlying EV71-associated neuroinflammation and neuronal cell death are not fully understood. Using cultured rodent neural cell models, we found that EV71 infection preferentially caused cell death in neurons but not brain-resident immune cells astrocytes and microglia. Neurons, astrocytes, and microglia responded to EV71 infection by releasing distinct profiles of cytokines, including nitric oxide (NO), tumor necrosis factor-a (TNF-a), interleukin (IL)21b, regulated on activation normal T cell expressed and secreted (RANTES), and glutamate. EV71 infection-induced neuronal cell death correlated well with the elevated production of NO, TNF-a, IL-1b, and glutamate as well as activation of microglia. Exogenous addition studies further demonstrated the neurotoxic potential of NO, TNF-a, IL-1b, and glutamate. EV71 infection-induced cytokine expression was accompanied by activation of protein tyrosine phosphorylation, mitogen-activated protein kinases (MAPKs), and NFjB. Intriguingly, EV71 susceptibility was accompanied by infection-elevated neuronal human scavenger receptor class B member 2 expression in cultured neural cells with agedependent manner. Biochemical and pharmacological studies revealed that after EV71 infection, microglia and accompanied cytokines play an active role in triggering bystander damage to neurons involving the tyrosine kinase/MAPKs/NF-jB signaling cascade. These data suggest that bystander damage caused by activated glia particularly the microglia could be an alternative mechanism of EV71-associated neuronal cell death. However, its clinical importance and implication require further investigation. V C 2015 IUBMB Life, 67(10):789-800, 2015

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Tyrosine phosphorylation events during coxsackievirus B3 replication

Cited by 31 publications

References 38 publications

Enhanced ERK-1/2 activation in mice susceptible to coxsackievirus-induced myocarditis

Enhanced ERK-1/2 activation in mice susceptible to coxsackievirus-induced myocarditis

Tripeptidyl peptidase II serves as an alternative to impaired proteasome to maintain viral growth in the host cells

Enterovirus 71 infection caused neuronal cell death and cytokine expression in cultured rat neural cells

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