ArticleJournal of virology2006
Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed.
- STING1 negatively regulates translation and replication of foot-and-mouth disease virus independently of interferon and is antagonized by the viral proteins 3C and 2B.Virologica Sinica · 2026Article
- Article
- Picornavirus 3C Proteins Intervene in Host Cell Processes through Proteolysis and Interactions with RNA.Viruses · 2023Review
- Insights into Polyprotein Processing and RNA-Protein Interactions in Foot-and-Mouth Disease Virus Genome Replication.Journal of virology · 2023Article
- Allosteric regulation of Senecavirus A 3Cpro proteolytic activity by an endogenous phospholipid.PLoS pathogens · 2023Article
- The RNA pseudoknots in foot-and-mouth disease virus are dispensable for genome replication, but essential for the production of infectious virus.PLoS pathogens · 2022Article
- Picornaviruses: A View from 3A.Viruses · 2021Review
- Foot-and-Mouth Disease Virus 3B Protein Interacts with Pattern Recognition Receptor RIG-I to Block RIG-I-Mediated Immune Signaling and Inhibit Host Antiviral Response.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Article
- Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity.Scientific reports · 2019Article
- (F)uridylylated Peptides Linked to VPg1 of Foot-and- Mouth Disease Virus (FMDV): Design, Synthesis and X-Ray Crystallography of the Complexes with FMDV RNA-Dependent RNA Polymerase.Molecules (Basel, Switzerland) · 2019Article
- Development of a fluorescence-based method for the rapid determination of Zika virus polymerase activity and the screening of antiviral drugs.Scientific reports · 2019Article
- Modifications to the Foot-and-Mouth Disease Virus 2A Peptide: Influence on Polyprotein Processing and Virus Replication.Journal of virology · 2018Article
- Genetic economy in picornaviruses: Foot-and-mouth disease virus replication exploits alternative precursor cleavage pathways.PLoS pathogens · 2017Article
- Determinants of the VP1/2A junction cleavage by the 3C protease in foot-and-mouth disease virus-infected cells.The Journal of general virology · 2017Article
- Both cis and trans Activities of Foot-and-Mouth Disease Virus 3D Polymerase Are Essential for Viral RNA Replication.Journal of virology · 2016Article
- Biological function of Foot-and-mouth disease virus non-structural proteins and non-coding elements.Virology journal · 2016Review
- Long-Range Communication between Different Functional Sites in the Picornaviral 3C Protein.Structure (London, England : 1993) · 2016Article
- Review
- Article
Corrections and comments
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6 authors.
Funding
Abstract
The uridylylation of the VPg peptide primer is the first stage in the replication of picornavirus RNA. This process can be achieved in vitro using purified components, including 3B (VPg) with the RNA dependent RNA polymerase (3Dpol), the precursor 3CD, and an RNA template containing the cre/bus. We show that certain RNA sequences within the foot-and-mouth disease virus (FMDV) 5' untranslated region but outside of the cre/bus can enhance VPg uridylylation activity. Furthermore, we have shown that the FMDV 3C protein alone can substitute for 3CD, albeit less efficiently. In addition, the VPg precursors, 3B(3)3C and 3B(123)3C, can function as substrates for uridylylation in the absence of added 3C or 3CD. Residues within the FMDV 3C protein involved in interaction with the cre/bus RNA have been identified and are located on the face of the protein opposite from the catalytic site. These residues within 3C are also essential for VPg uridylylation activity and efficient virus replication.
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