scholarly journals Dicodon monitoring of protein synthesis (DiCoMPS) reveals levels of synthesis of a viral protein in single cells

2013 ◽  
Vol 41 (18) ◽  
pp. e177-e177 ◽  
Author(s):  
Sima Barhoom ◽  
Ian Farrell ◽  
Ben Shai ◽  
Dvir Dahary ◽  
Barry S. Cooperman ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Viral Protein ◽  
Single Cells

Initiation of Mammalian Viral Protein Synthesis

1971 ◽  
Vol 229 (8) ◽  
pp. 239-241 ◽  
Author(s):  
HANS CAFFIER ◽  
HESCHEL J. RASKAS ◽  
J. THOMAS PARSONS ◽  
MAURICE GREEN
Keyword(s):  
Protein Synthesis ◽  
Viral Protein ◽  
Viral Protein Synthesis

scholarly journals Effect of the Viral Hemorrhagic Septicemia Virus Nonvirion Protein on Translation via PERK-eIF2α Pathway

Viruses ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 499 ◽  
Author(s):  
Shelby Powell Kesterson ◽  
Jeffery Ringiesn ◽  
Vikram N. Vakharia ◽  
Brian S. Shepherd ◽  
Douglas W. Leaman ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Viral Protein ◽  
Molecular Mechanisms ◽  
Freshwater Ecosystems ◽  
Innate Immune ◽  
Host Cells ◽  
Initiation Factor ◽  
Viral Hemorrhagic Septicemia Virus ◽  
Viral Protein Synthesis ◽  
Viral Hemorrhagic Septicemia

Viral hemorrhagic septicemia virus (VHSV) is one of the most deadly infectious fish pathogens, posing a serious threat to the aquaculture industry and freshwater ecosystems worldwide. Previous work showed that VHSV sub-genotype IVb suppresses host innate immune responses, but the exact mechanism by which VHSV IVb inhibits antiviral response remains incompletely characterized. As with other novirhabdoviruses, VHSV IVb contains a unique and highly variable nonvirion (NV) gene, which is implicated in viral replication, virus-induced apoptosis and regulating interferon (IFN) production. However, the molecular mechanisms underlying the role of IVb NV gene in regulating viral or cellular processes is poorly understood. Compared to the wild-type recombinant (rWT) VHSV, mutant VHSV lacking a functional IVb NV reduced IFN expression and compromised innate immune response of the host cells by inhibiting translation. VHSV IVb infection increased phosphorylated eukaryotic initiation factor 2α (p-eIF2α), resulting in host translation shutoff. However, VHSV IVb protein synthesis proceeds despite increasing phosphorylation of eIF2α. During VHSV IVb infection, eIF2α phosphorylation was mediated via PKR-like endoplasmic reticulum kinase (PERK) and was required for efficient viral protein synthesis, but shutoff of host translation and IFN signaling was independent of p-eIF2α. Similarly, IVb NV null VHSV infection induced less p-eIF2α, but exhibited decreased viral protein synthesis despite increased levels of viral mRNA. These findings show a role for IVb NV in VHSV pathogenesis by utilizing the PERK-eIF2α pathway for viral-mediated host shutoff and interferon signaling to regulate host cell response.

Inhibition of viral protein synthesis in monkey cells treated with interferon late in simian virus 40 lytic cycle

Cell ◽  
1977 ◽  
Vol 12 (1) ◽  
pp. 73-81 ◽  
Author(s):  
Emanuel Yakobson ◽  
Carol Prives ◽  
Jacob R. Hartman ◽  
Ernest Winocour ◽  
Michel Revel
Keyword(s):  
Protein Synthesis ◽  
Viral Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Lytic Cycle ◽  
Viral Protein Synthesis

scholarly journals Replication and Cytopathic Effect of Oncolytic Vesicular Stomatitis Virus in Hypoxic Tumor Cells In Vitro and In Vivo

2004 ◽  
Vol 78 (17) ◽  
pp. 8960-8970 ◽  
Author(s):  
John H. Connor ◽  
Christine Naczki ◽  
Costas Koumenis ◽  
Douglas S. Lyles
Keyword(s):  
Protein Synthesis ◽  
Vesicular Stomatitis Virus ◽  
Viral Protein ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Progeny Virus ◽  
Hypoxic Stress ◽  
Α Subunit ◽  
Hypoxic Conditions ◽  
Vesicular Stomatitis

ABSTRACT Tumor hypoxia presents an obstacle to the effectiveness of most antitumor therapies, including treatment with oncolytic viruses. In particular, an oncolytic virus must be resistant to the inhibition of DNA, RNA, and protein synthesis that occurs during hypoxic stress. Here we show that vesicular stomatitis virus (VSV), an oncolytic RNA virus, is capable of replication under hypoxic conditions. In cells undergoing hypoxic stress, VSV infection produced larger amounts of mRNA than under normoxic conditions. However, translation of these mRNAs was reduced at earlier times postinfection in hypoxia-adapted cells than in normoxic cells. At later times postinfection, VSV overcame a hypoxia-associated increase in α subunit of eukaryotic initiation factor 2 (eIF-2α) phosphorylation and initial suppression of viral protein synthesis in hypoxic cells to produce large amounts of viral protein. VSV infection caused the dephosphorylation of the translation initiation factor eIF-4E and inhibited host translation similarly under both normoxic and hypoxic conditions. VSV produced progeny virus to similar levels in hypoxic and normoxic cells and showed the ability to expand from an initial infection of 1% of hypoxic cells to spread through an entire population. In all cases, virus infection induced classical cytopathic effects and apoptotic cell death. When VSV was used to treat tumors established in nude mice, we found VSV replication in hypoxic areas of these tumors. This occurred whether the virus was administered intratumorally or intravenously. These results show for the first time that VSV has an inherent capacity for infecting and killing hypoxic cancer cells. This ability could represent a critical advantage over existing therapies in treating established tumors.

scholarly journals Enzymatic dissection of embryonic cell adhesive mechanisms.

1980 ◽  
Vol 85 (3) ◽  
pp. 766-776 ◽  
Author(s):  
G B Grunwald ◽  
R L Geller ◽  
J Lilien
Keyword(s):  
Protein Synthesis ◽  
Single Cells ◽  
Cluster Formation ◽  
Embryonic Cell ◽  
Embryonic Chick ◽  
Adhesive Systems ◽  
Kinetic Assay ◽  
Tissue Dissociation ◽  
Morphogenetic Potential ◽  
Two Parameters

In this paper we describe a kinetic assay for cell adhesion which measures the formation of cell clusters. Cluster formation is dependent on both calcium and protein synthesis, two parameters essential for the formation of histotypic aggregates. We also describe modifications of the stndard method for trypsinization of tissues which result in populations of single cells that appear to bear intact and functional cell surface adhesive systems. These modifications involve the use of chymotrypsin and the inclusion of calcium during enzyme digestion of tissues with trypsin and chymotrypsin. Using the cluster formation assay and the modified tissue dissociation techniques, we demonstrate the presence of two functionally distinct adhesive systems operating among embryonic chick neural retina cells. These two systems differ in proteolytic sensitivity, protection by calcium against proteolysis, dependence on calcium for function and morphogenetic potential. Cells possessing one of these intact adhesive systems are capable of extensive morphogenetic interactions in the absence of protein synthesis.

scholarly journals Host and Viral Translational Mechanisms during Cricket Paralysis Virus Infection

2009 ◽  
Vol 84 (2) ◽  
pp. 1124-1138 ◽  
Author(s):  
Julianne L. Garrey ◽  
Yun-Young Lee ◽  
Hilda H. T. Au ◽  
Martin Bushell ◽  
Eric Jan
Keyword(s):  
Protein Synthesis ◽  
Viral Protein ◽  
Rna Virus ◽  
Virus Production ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
S2 Cells ◽  
Structural Protein ◽  
Viral Protein Synthesis ◽  
Paralysis Virus

ABSTRACT The dicistrovirus is a positive-strand single-stranded RNA virus that possesses two internal ribosome entry sites (IRES) that direct translation of distinct open reading frames encoding the viral structural and nonstructural proteins. Through an unusual mechanism, the intergenic region (IGR) IRES responsible for viral structural protein expression mimics a tRNA to directly recruit the ribosome and set the ribosome into translational elongation. In this study, we explored the mechanism of host translational shutoff in Drosophila S2 cells infected by the dicistrovirus, cricket paralysis virus (CrPV). CrPV infection of S2 cells results in host translational shutoff concomitant with an increase in viral protein synthesis. CrPV infection resulted in the dissociation of eukaryotic translation initiation factor 4G (eIF4G) and eIF4E early in infection and the induction of deIF2α phosphorylation at 3 h postinfection, which lags after the initial inhibition of host translation. Forced dephosphorylation of deIF2α by overexpression of dGADD34, which activates protein phosphatase I, did not prevent translational shutoff nor alter virus production, demonstrating that deIF2α phosphorylation is dispensable for host translational shutoff. However, premature induction of deIF2α phosphorylation by thapsigargin treatment early in infection reduced viral protein synthesis and replication. Finally, translation mediated by the 5′ untranslated region (5′UTR) and the IGR IRES were resistant to impairment of eIF4F or eIF2 in translation extracts. These results support a model by which the alteration of the deIF4F complex contribute to the shutoff of host translation during CrPV infection, thereby promoting viral protein synthesis via the CrPV 5′UTR and IGR IRES.

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