Sequestration of G3BP coupled with efficient translation inhibits stress granules in Semliki Forest virus infection
| العنوان: | Sequestration of G3BP coupled with efficient translation inhibits stress granules in Semliki Forest virus infection |
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| المؤلفون: | Gerald M. McInerney, Andres Merits, Aleksei Lulla, Margus Varjak, Kai Er Eng, Gunilla B. Karlsson Hedestam, Marc D. Panas |
| المصدر: | Molecular Biology of the Cell |
| بيانات النشر: | American Society for Cell Biology, 2012. |
| سنة النشر: | 2012 |
| مصطلحات موضوعية: | Viral nonstructural protein, viruses, Green Fluorescent Proteins, Immunoblotting, RNA-binding protein, Viral Nonstructural Proteins, Cytoplasmic Granules, Semliki Forest virus, Virus, Cell Line, Mice, Stress granule, stomatognathic system, Stress, Physiological, Viral entry, Protein biosynthesis, Animals, Humans, RNA, Messenger, Poly-ADP-Ribose Binding Proteins, Molecular Biology, Cells, Cultured, Adaptor Proteins, Signal Transducing, Binding Sites, Microscopy, Confocal, biology, DNA Helicases, RNA-Binding Proteins, Articles, Cell Biology, biology.organism_classification, Semliki forest virus, Virology, HEK293 Cells, RNA Recognition Motif Proteins, Cell Biology of Disease, Cell culture, Protein Biosynthesis, Host-Pathogen Interactions, Mutation, Carrier Proteins, RNA Helicases, Protein Binding |
| الوصف: | Semliki Forest virus nsP3 sequesters G3BP to inhibit stress granule formation on viral mRNAs. Furthermore, the efficient translation of viral mRNAs containing a translation enhancer element assists disruption of SGs in infected cells. This work thus describes a novel mechanism for SG disruption. Dynamic, mRNA-containing stress granules (SGs) form in the cytoplasm of cells under environmental stresses, including viral infection. Many viruses appear to employ mechanisms to disrupt the formation of SGs on their mRNAs, suggesting that they represent a cellular defense against infection. Here, we report that early in Semliki Forest virus infection, the C-terminal domain of the viral nonstructural protein 3 (nsP3) forms a complex with Ras-GAP SH3-domain–binding protein (G3BP) and sequesters it into viral RNA replication complexes in a manner that inhibits the formation of SGs on viral mRNAs. A viral mutant carrying a C-terminal truncation of nsP3 induces more persistent SGs and is attenuated for propagation in cell culture. Of importance, we also show that the efficient translation of viral mRNAs containing a translation enhancer sequence also contributes to the disassembly of SGs in infected cells. Furthermore, we show that the nsP3/G3BP interaction also blocks SGs induced by other stresses than virus infection. This is one of few described viral mechanisms for SG disruption and underlines the role of SGs in antiviral defense. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 1059-1524 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72c59b4a3bda639f90d133a7fd0aa6fdTest https://eprints.gla.ac.uk/128304/1/128304.pdfTest |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....72c59b4a3bda639f90d133a7fd0aa6fd |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10591524 |
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