Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein

Huang, Jing-Zhi; Schneider, Robert J.

doi:10.1016/0092-8674(91)90161-q

Cited by 167 publications

(135 citation statements)

References 53 publications

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“…Alternatively, infection of cells with another picornavirus, encephalomyocarditis virus, does not induce eIF4G cleavage but leads to dephosphorylation of 4E-BP1, which binds to eIF4E and prevents its interaction with eIF4G (33). Late in adenovirus infection, eIF4E itself is dephosphorylated as a result of the displacement of the eIF4E-kinase Mnk-1 from eIF4G (34). However, viruses have also evolved a number of ways in which to overcome these modifications to the host cell translational machinery.…”

Section: Discussionmentioning

confidence: 99%

Caliciviruses Differ in Their Functional Requirements for eIF4F Components

Chaudhry

Nayak

Bordeleau

et al. 2006

Journal of Biological Chemistry

127

199

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Two classes of viruses, namely members of the Potyviridae and Caliciviridae, use a novel mechanism for the initiation of protein synthesis that involves the interaction of translation initiation factors with a viral protein covalently linked to the viral RNA, known as VPg. The calicivirus VPg proteins can interact directly with the initiation factors eIF4E and eIF3. Translation initiation on feline calicivirus (FCV) RNA requires eIF4E because it is inhibited by recombinant 4E-BP1. However, to date, there have been no functional studies carried out with respect to norovirus translation initiation, because of a lack of a suitable source of VPg-linked viral RNA. We have now used the recently identified murine norovirus (MNV) as a model system for norovirus translation and have extended our previous studies with FCV RNA to examine the role of the other eIF4F components in translation initiation. We now demonstrate that, as with FCV, MNV VPg interacts directly with eIF4E, although, unlike FCV RNA, translation of MNV RNA is not sensitive to 4E-BP1, eIF4E depletion, or foot-and-mouth disease virus Lb protease-mediated cleavage of eIF4G. We also demonstrate that both FCV and MNV RNA translation require the RNA helicase component of the eIF4F complex, namely eIF4A, because translation was sensitive (albeit to different degrees) to a dominant negative form and to a small molecule inhibitor of eIF4A (hippuristanol). These results suggest that calicivirus RNAs differ with respect to their requirements for the components of the eIF4F translation initiation complex.

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Section: Discussionmentioning

confidence: 99%

Caliciviruses Differ in Their Functional Requirements for eIF4F Components

Chaudhry

Nayak

Bordeleau

et al. 2006

Journal of Biological Chemistry

127

199

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“…7,8 PKR is also activated by dsRNA; this leads to the phosphorylation of its substrate, eIF2a, which inhibits the guanosine nucleotide exchange factor, eIF2b, and halts viral replication. 9,10 PKR may act by shutting down protein synthesis following infection of a cell and limit the transmission of virus to uninfected cells. 11 Interactions between the HCV and PKR are believed to be an important mechanism behind the resistance of HCV to interferon therapies.…”

Section: Introductionmentioning

confidence: 99%

Polymorphisms in interferon-induced genes and the outcome of hepatitis C virus infection: roles of MxA, OAS-1 and PKR

et al. 2003

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Interferon stimulates the expression of a number of genes encoding enzymes with antiviral activities, including myxovirus resistance-1 (MxA), 2-5-oligoadenylate synthetase 1 (OAS-1) and double-stranded RNA-dependent protein kinase (PKR). We examined whether polymorphisms in these genes influenced the outcome of hepatitis C virus (HCV) infection. We observed a lower frequency of the GG genotype at position À88 in the MxA gene promoter in self-limiting HCV infection (OR ¼ 0.56; 95% CI: 0.35-0.8; P ¼ 0.010) and in nonresponders to therapy (OR ¼ 0.49; 95% CI: 0.25-0.95; P ¼ 0.020). This genotype predominantly influenced the outcome of treatment in patients with viral genotype 1 (OR ¼ 0.22 95% CI: 0.07-0.67; P ¼ 0.002). A polymorphism in the 3 0 -untranslated region of the OAS-1 gene was associated with outcome of infection (GG genotype less frequent in self-limiting infection: OR ¼ 0.43; 95% CI: 0.21-0.86; P ¼ 0.010). A polymorphism at position À168 in the promoter region of the PKR gene was associated with self-limiting infection (CT genotype: OR ¼ 2.75; 95% CI: 1.45-5.24; P ¼ 0.002). Further associations were found with a CGG trinucleotide repeat in the 5 0 UTR region of the PKR gene. Polymorphisms in the interferon-induced genes, MxA, OAS-1 and PKR appear thus associated with HCV outcome.

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“…Therefore, it seemed likely that inhibition of translation initiation was caused by diminishing ribosome recruitment to capped mRNAs during mitosis. Viral mRNAs whose translation is initiated by an internal ribosome entry site (IRES) 1 mechanism (10), such as polioviral and hepatitis C viral mRNAs (4,(11)(12)(13)(14) or mRNAs which lack significant structures in their 5Ј-non-coding regions (5Ј-NCRs), such as the mRNAs containing the late leader of adenovirus (15), were found to be selectively translated during mitosis due to their lessened requirement for eIF4F. More recently, additional IREScontaining mRNAs, those encoding ornithine decarboxylase and kinase p58 PITSLRE , have been reported to be selectively translated during G 2 /M of the cell cycle in cultured cells (11,12).…”

mentioning

confidence: 99%

Preferential Translation of Internal Ribosome Entry Site-containing mRNAs during the Mitotic Cycle in Mammalian Cells

Qin¹,

Sarnow

2004

Journal of Biological Chemistry

148

161

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A cell synchronization protocol was established in which global and individual mRNA translational efficiencies could be examined. While global translational efficiency was reduced in mitotic cells, ϳ3% of mRNAs remained predominantly associated with large polysomes during mitosis, as determined by cDNA microarray analyses. The 5-non-coding regions of six mRNAs were shown to contain internal ribosome entry sites (IRES). However, not all known mRNAs that contain IRES elements were actively translated during mitosis, arguing that specific IRES sequences are differentially regulated during mitosis.Cells of higher organisms can regulate gene expression at the translational level in response to a wide variety of stimuli and conditions. While much is known about the control of translational initiation and elongation in response to nutritional deprivation (1, 2) and environmental stress (2), the role of translational control in mammalian cell cycle progression is not well understood. It has long been known that specific proteins are needed at specific times during the cell cycle to ensure cell cycle progression. For the most part, the expression of these cell cycle-specific proteins is thought to be regulated at the transcriptional or posttranslational level (3).In cultured mammalian cells arrested at G 2 and M phases, the rate of total protein synthesis was markedly decreased to about 25% of the rate in non-arrested, cycling cells (4). This reduction was shown to be, at least partly, due to inhibition of the initiation step of polypeptide synthesis (4 -6). Subsequently, several eukaryotic initiation factors that regulate the assembly of 40 S ribosomes at the 5Ј ends of capped mRNAs were observed to change their phosphorylation status (7-9). Therefore, it seemed likely that inhibition of translation initiation was caused by diminishing ribosome recruitment to capped mRNAs during mitosis. Viral mRNAs whose translation is initiated by an internal ribosome entry site (IRES) 1 mechanism (10), such as polioviral and hepatitis C viral mRNAs (4,(11)(12)(13)(14) or mRNAs which lack significant structures in their 5Ј-non-coding regions (5Ј-NCRs), such as the mRNAs containing the late leader of adenovirus (15), were found to be selectively translated during mitosis due to their lessened requirement for eIF4F. More recently, additional IREScontaining mRNAs, those encoding ornithine decarboxylase and kinase p58 PITSLRE , have been reported to be selectively translated during G 2 /M of the cell cycle in cultured cells (11,12). These findings raise the question whether all IREScontaining genes are preferentially translated during mitosis and whether any of these encoded products play roles in cell cycle progression. We have begun to address these questions by genomic analysis of cellular mRNAs that are associated with mitotic polysomes and are, thus, predicted to be translated during the overall translation repression in mitosis. We determined that many, but not all, IRES elements are present in mRNAs which are selectively translated...

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Adenovirus inhibition of cellular protein synthesis involves inactivation of cap-binding protein

Cited by 167 publications

References 53 publications

Caliciviruses Differ in Their Functional Requirements for eIF4F Components

Caliciviruses Differ in Their Functional Requirements for eIF4F Components

Polymorphisms in interferon-induced genes and the outcome of hepatitis C virus infection: roles of MxA, OAS-1 and PKR

Preferential Translation of Internal Ribosome Entry Site-containing mRNAs during the Mitotic Cycle in Mammalian Cells

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