ArticleJournal of virology2020
Ribosomal Protein L13 Promotes IRES-Driven Translation of Foot-and-Mouth Disease Virus in a Helicase DDX3-Dependent Manner.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 59 citations in OpenAlex.
- eIF3 musketeers: loyal in health, rogue in disease, and redeemed by therapeutic targeting.The EMBO journal · 2026Review
- RNA helicase DDX5 regulates the translation and genomic replication of foot-and-mouth disease virus.Journal of virology · 2026Article
- Ribosome heterogeneity and specialization in musculoskeletal physiology and pathology.JBMR plus · 2026Article
- At the crossroads of immunity and hijacking: dual roles of DDX proteins during host-virus interactions.Frontiers in cellular and infection microbiology · 2026Review
- Ribosomal protein L35 negatively regulates FMDV replication by recruiting AMFR to promote the ubiquitination and degradation of VP2.Journal of virology · 2025Article
- Integrated multiomics reveals host-virus coadaptation in persistent foot-and-mouth disease virus infection.Cellular and molecular life sciences : CMLS · 2025Article
- Ins and outs of IRES elements: function and significance.Biochemical Society transactions · 2025Review
- Review
- DDX3 Regulates the Cap-Independent Translation of the Japanese Encephalitis Virus via Its Interactions with PABP1 and the Untranslated Regions of the Viral Genome.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- CD44 mediates the internalization of foot-and-mouth disease virus through macropinocytosis.Veterinary research · 2025Article
- Heat shock protein A1 inhibits the replication of foot-and-mouth disease virus by degrading viral RNA polymerase 3D through chaperone-mediated autophagy.Journal of virology · 2025Article
- Nuclear Accumulation of Bm65 Aggregate Is Blocked by Mutations in the Nuclear Export Sequence of Bm65.Viruses · 2025Article
- The Influence of Extra-Ribosomal Functions of Eukaryotic Ribosomal Proteins on Viral Infection.Biomolecules · 2024Review
- VP3 protein of Senecavirus A promotes viral IRES-driven translation and attenuates innate immunity by specifically relocalizing hnRNPA2B1.Journal of virology · 2024Article
- Pseudorabies virus manipulates mitochondrial tryptophanyl-tRNA synthetase 2 for viral replication.Virologica Sinica · 2024Article
- Nuclear ribonucleoprotein RALY downregulates foot-and-mouth disease virus replication but antagonized by viral 3C protease.Microbiology spectrum · 2024Article
- Article
- Foot-and-mouth disease virus downregulates vacuolar protein sorting 28 to promote viral replication.Journal of virology · 2023Article
- Advances and Breakthroughs in IRES-Directed Translation and Replication of Picornaviruses.mBio · 2023Review
- Proteomic screening identifies RPLp2 as a specific regulator for the translation of coronavirus.International journal of biological macromolecules · 2023Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Internal ribosome entry site (IRES)-driven translation is a common strategy among positive-sense, single-stranded RNA viruses for bypassing the host cell requirement of a 5' cap structure. In the current study, we identified the ribosomal protein L13 (RPL13) as a critical regulator of IRES-driven translation of foot-and-mouth disease virus (FMDV) but found that it is not essential for cellular global translation. RPL13 is also a determinant for translation and infection of Seneca Valley virus (SVV) and classical swine fever virus (CSFV), and this suggests that its function may also be conserved in unrelated IRES-containing viruses. We further showed that depletion of DEAD box helicase DDX3 disrupts binding of RPL13 to the FMDV IRES, whereas the reduction in RPL13 expression impairs the ability of DDX3 to promote IRES-driven translation directly. DDX3 cooperates with RPL13 to support the assembly of 80S ribosomes for optimal translation initiation of viral mRNA. Finally, we demonstrated that DDX3 affects the recruitment of the eukaryotic initiation factor eIF3 subunits e and j to the viral IRES. This work provides the first connection between DDX3 and eIF3e/j and recognition of the role of RPL13 in modulating viral IRES-dependent translation. This previously uncharacterized process may be involved in selective mRNA translation.
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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.