ArticlePLoS pathogens2011
Re-localization of cellular protein SRp20 during poliovirus infection: bridging a viral IRES to the host cell translation apparatus.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 63 citations in OpenAlex.
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- Isoforms in action: The impact of transcript diversity in phenotype.Genetics and molecular biology · 2026Article
- Subversion of phosphorylated SR proteins by enterovirus A71 in IRES-dependent translation revealed by RNA-interactome analysis.PLoS pathogens · 2025Article
- VP3 protein of Senecavirus A promotes viral IRES-driven translation and attenuates innate immunity by specifically relocalizing hnRNPA2B1.Journal of virology · 2024Article
- Host Subcellular Organelles: Targets of Viral Manipulation.International journal of molecular sciences · 2024Review
- RNA Structure in the 5' Untranslated Region of Enterovirus D68 Strains with Differing Neurovirulence Phenotypes.Viruses · 2023Article
- Oncogenic SRSF3 in health and diseases.International journal of biological sciences · 2023Review
- Elusive Trans-Acting Factors Which Operate with Type I (Poliovirus-like) IRES Elements.International journal of molecular sciences · 2022Review
- Review
- SRSF3 Expression Serves as a Potential Biomarker for Prognostic and Immune Response in Pan-Cancer.Frontiers in oncology · 2022Article
- The RNA-dependent RNA polymerase of enterovirus A71 associates with ribosomal proteins and positively regulates protein translation.RNA biology · 2020Article
- Effects of TDP2/VPg Unlinkase Activity on Picornavirus Infections Downstream of Virus Translation.Viruses · 2020Article
- Translation control of Enterovirus A71 gene expression.Journal of biomedical science · 2020Review
- Emerging Roles of SRSF3 as a Therapeutic Target for Cancer.Frontiers in oncology · 2020Review
- Differential Functions of Splicing Factors in Mammary Transformation and Breast Cancer Metastasis.Cell reports · 2019Article
- Picornaviruses and RNA Metabolism: Local and Global Effects of Infection.Journal of virology · 2019Review
- The mammalian host protein DAP5 facilitates the initial round of translation of Coxsackievirus B3 RNA.The Journal of biological chemistry · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Poliovirus IRES-mediated translation requires the functions of certain canonical as well as non-canonical factors for the recruitment of ribosomes to the viral RNA. The interaction of cellular proteins PCBP2 and SRp20 in extracts from poliovirus-infected cells has been previously described, and these two proteins were shown to function synergistically in viral translation. To further define the mechanism of ribosome recruitment for the initiation of poliovirus IRES-dependent translation, we focused on the role of the interaction between cellular proteins PCBP2 and SRp20. Work described here demonstrates that SRp20 dramatically re-localizes from the nucleus to the cytoplasm of poliovirus-infected neuroblastoma cells during the course of infection. Importantly, SRp20 partially co-localizes with PCBP2 in the cytoplasm of infected cells, corroborating our previous in vitro interaction data. In addition, the data presented implicate the presence of these two proteins in viral translation initiation complexes. We show that in extracts from poliovirus-infected cells, SRp20 is associated with PCBP2 bound to poliovirus RNA, indicating that this interaction occurs on the viral RNA. Finally, we generated a mutated version of SRp20 lacking the RNA recognition motif (SRp20ΔRRM) and found that this protein is localized similar to the full length SRp20, and also partially co-localizes with PCBP2 during poliovirus infection. Expression of this mutated version of SRp20 results in a ∼100 fold decrease in virus yield for poliovirus when compared to expression of wild type SRp20, possibly via a dominant negative effect. Taken together, these results are consistent with a model in which SRp20 interacts with PCBP2 bound to the viral RNA, and this interaction functions to recruit ribosomes to the viral RNA in a direct or indirect manner, with the participation of additional protein-protein or protein-RNA interactions.
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