ArticleJournal of virology1999
Eukaryotic initiation factor 4GII (eIF4GII), but not eIF4GI, cleavage correlates with inhibition of host cell protein synthesis after human rhinovirus infection.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 134 citations in OpenAlex.
- Proteolytic dissection of eIF4G reveals the closed-loop mRNP as an architecture for translation repression.bioRxiv : the preprint server for biology · 2026Article
- The multifaceted role of the viral 2A protease in enterovirus replication and antagonism of host antiviral responses.PLoS pathogens · 2025Article
- The Polypyrimidine Tract-Binding Protein Is a Transacting Factor for the Dengue Virus Internal Ribosome Entry Site.Viruses · 2024Article
- Targeting IRES-dependent translation as a novel approach for treating Duchenne muscular dystrophy.RNA biology · 2021Review
- A comparative analysis of parechovirus protein structures with other picornaviruses.Open biology · 2021Article
- eIF4G-driven translation initiation of downstream ORFs in mammalian cells.Nucleic acids research · 2020Article
- Article
- Cleavage and Sub-Cellular Redistribution of Nuclear Pore Protein 98 by Coxsackievirus B3 Protease 2A Impairs Cardioprotection.Frontiers in cellular and infection microbiology · 2019Article
- The mechanistic insight of a specific interaction between 15d-Prostaglandin-J2 and eIF4A suggests an evolutionary conserved role across species.Biology open · 2018Article
- Picornavirus 2A protease regulates stress granule formation to facilitate viral translation.PLoS pathogens · 2018Article
- Human Rhinovirus 3C protease cleaves RIPK1, concurrent with caspase 8 activation.Scientific reports · 2018Article
- The Triticum Mosaic Virus 5' Leader Binds to Both eIF4G and eIFiso4G for Translation.PloS one · 2017Article
- Cleavage of DAP5 by coxsackievirus B3 2A protease facilitates viral replication and enhances apoptosis by altering translation of IRES-containing genes.Cell death and differentiation · 2016Article
- Quantitative Proteomic Analysis of Duck Ovarian Follicles Infected with Duck Tembusu Virus by Label-Free LC-MS.Frontiers in microbiology · 2016Article
- NMR analysis of the interaction of picornaviral proteinases Lb and 2A with their substrate eukaryotic initiation factor 4GII.Protein science : a publication of the Protein Society · 2015Article
- The spliceosome factor SART1 exerts its anti-HCV action through mRNA splicing.Journal of hepatology · 2015Article
- HIV-1 transcripts use IRES-initiation under conditions where Cap-dependent translation is restricted by poliovirus 2A protease.PloS one · 2014Article
- Structural analysis of the DAP5 MIF4G domain and its interaction with eIF4A.Structure (London, England : 1993) · 2013Article
- Enterovirus 71 protease 2Apro targets MAVS to inhibit anti-viral type I interferon responses.PLoS pathogens · 2013Article
- A novel mechanism of eukaryotic translation initiation that is neither m7G-cap-, nor IRES-dependent.Nucleic acids research · 2013Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For many members of the Picornaviridae family, infection of cells results in a shutoff of host protein synthesis. For rhinoviruses and enteroviruses, the shutoff has been explained in part by the cleavage of eukaryotic initiation factor 4GI (eIF4GI), a component of the cap-binding protein complex eIF4F. The cleavage of eIF4GI is mediated by the virus-specific proteinase 2Apro and results in inhibition of cap-dependent, but not cap-independent, translation. The inhibition of host protein synthesis after infection with human rhinovirus 14 (HRV-14) lags behind the cleavage of eIF4GI. Recently, we discovered a functional homolog of eIF4GI, termed eIF4GII, and showed that cleavage of eIF4GII coincides with the shutoff of host cell protein synthesis after poliovirus infection (Gradi et al., Proc. Natl. Acad. Sci. USA 95:11089-11094, 1998). We wished to determine whether eIF4GII cleavage kinetics could also explain the lack of correlation between the kinetics of eIF4GI cleavage and the shutoff of host protein synthesis after rhinovirus infection. In this study, we examined the correlation between human rhinovirus-induced shutoff of host protein synthesis and cleavage of eIF4GI and eIF4GII. In HRV-14-infected HeLa cells, almost no intact eIF4GI could be detected by 4 h postinfection, while only 4% of eIF4GII was cleaved at this time. By 6 h, however, 67% of eIF4GII was cleaved, and this cleavage coincided with a significant (60%) decline of host translation. These results suggest that cleavage of both eIF4GI and eIF4GII is required for HRV-mediated inhibition of host cell protein synthesis and that the cleavage of eIF4GII is the rate-limiting step in the shutoff of host cell protein synthesis after rhinovirus infection.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.