The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication.

@article{Gierman1992TheET,
  title={The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication.},
  author={T. Gierman and R. Frederickson and N. Sonenberg and D. Pickup},
  journal={Virology},
  year={1992},
  volume={188 2},
  pages={
          934-7
        }
}
The ability of vaccinia virus to inhibit processes of cap-dependent translational initiation by inactivating the eukaryotic translation initiation factor 4E (eIF-4E) has been examined. Analyses of the quantities of eIF-4E present in either uninfected mouse L929 cells or vaccinia virus-infected cells showed that during the first 12 hr of virus replication, when there is a marked decrease in host gene expression in infected cells, there is no change in the total amount of eIF-4E present. Analyses… Expand
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Vaccinia virus-mediated inhibition of host protein synthesis involves neither degradation nor underphosphorylation of components of the cap-binding eukaryotic translation initiation factor complex eIF-4F.
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The eIF-4F complex was affinity-purified from human cells infected with vaccinia virus and analyzed by one- and two-dimensional electrophoresis and immunoblotting to examine the possibility that the mechanism of inhibition of host protein synthesis byvaccinia virus involves specific modifications of the cap-binding translation initiation factor complex eIF -4F. Expand
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Neither vesicular stomatitis virus, vaccinia virus, frog virus III, rhinovirus, nor encephalomyocarditis virus caused significantly increased 2α phosphorylation in cells infected by any of the virus infections analyzed. Expand
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It is reported here that overexpression of eIF-4E in NIH 3T3 and Rat 2 fibroblasts causes their tumorigenic transformation as determined by three criteria: formation of transformed foci on a monolayer of cells; anchorage-independent growth; and tumour formation in nude mice. Expand
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Site-directed mutagenesis was used to replace the serine residue at the primary phosphorylation site of human eukaryotic initiation factor (eIF) 4E with an alanine residue, and eIF-4ESer isolated from 48 S initiation complexes consisted predominantly of the phosphorylated form. Expand
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Comparison on SDS-polyacrylamide gels of the in vitro translation products at nonsaturating RNA concentrations with those obtained in vivo by pulse labeling the infected cells showed that essentially all the early in vivo labeled proteins were made upon translation of the early RNA, suggesting that at the late stage of vaccinia virus infection the synthesis of theEarly proteins is subjected to translational control. Expand
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