The eukaryotic translation initiation factor 4E is not modified during the course of vaccinia virus replication
Autor: | Nahum Sonenberg, David J. Pickup, Robert M. Frederickson, Todd M. Gierman |
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Rok vydání: | 1992 |
Předmět: |
Gene Expression Regulation
Viral RNA Caps viruses Eukaryotic Initiation Factor-4E Vaccinia virus macromolecular substances In Vitro Techniques Virus Replication environment and public health Virus Mice Eukaryotic translation L Cells Peptide Initiation Factors Virology Initiation factor Animals heterocyclic compounds Poxviridae Electrophoresis Gel Two-Dimensional Orthopoxvirus Phosphorylation biology EIF4E biology.organism_classification Molecular biology enzymes and coenzymes (carbohydrates) Viral replication |
Zdroj: | Virology. 188(2) |
ISSN: | 0042-6822 |
Popis: | 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 of eIF-4E that was metabolically labeled with [32P] and then purified by affinity chromatography using m7GTP-Sepharose 4B, indicated that neither the incorporation of radiolabel into eIF-4E nor the amounts of eIF-4E capable of binding to cap structures changed significantly during virus replication. Immunodetection of phosphorylated and unphosphorylated eIF-4E in cell lysates fractionated by two-dimensional gel electrophoresis showed that the steady-state levels of phosphorylated and unphosphorylated forms of eIF-4E were similar in uninfected and virus-infected cells. These results suggest that vaccinia virus does not gain preferential translation of viral mRNAs over other mRNAs in the cell by reducing either eIF-4E phosphorylation or its ability to bind to the cap structure. |
Databáze: | OpenAIRE |
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