ArticleJournal of virology2012
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed.
- Poliovirus 3Dpol polymerase region is essential for cleavage of poliovirus 3AB in vivo.PLoS pathogens · 2026Article
- CBX4 facilitates EV71 replication by SUMOylation and stabilizing 3D polymerase.Frontiers in microbiology · 2026Article
- Review
- Small Interfering RNAs Targeting VP4, VP3, 2B, or 3A Coding Regions of Enterovirus A71 Inhibit Viral Replication In Vitro.Biomedicines · 2025Article
- Sequences and Structures of Viral Proteins Linked to the Genomes (VPg) of RNA Viruses.Viruses · 2025Review
- Insight into the Life Cycle of Enterovirus-A71.Viruses · 2025Review
- Down-regulated TAB1 suppresses the replication of Coxsackievirus B5 via activating the NF-κB pathways through interaction with viral 3D polymerase.Virology journal · 2023Article
- Insights into In Vitro Adaptation of EV71 and Analysis of Reduced Virulence by In Silico Predictions.Vaccines · 2023Article
- Multiple Viral Protein Genome-Linked Proteins Compensate for Viral Translation in a Positive-Sense Single-Stranded RNA Virus Infection.Journal of virology · 2022Article
- Host Restrictive Factors Are the Emerging Storm Troopers Against Enterovirus: A Mini-Review.Frontiers in immunology · 2022Review
- Protein Nucleotidylylation in +ssRNA Viruses.Viruses · 2021Review
- A comparative analysis of parechovirus protein structures with other picornaviruses.Open biology · 2021Article
- Analysis of the Complete Genomes of Enterovirus 71 Subtypes in China.The Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2021Article
- Enterovirus 71 induces neural cell apoptosis and autophagy through promoting ACOX1 downregulation and ROS generation.Virulence · 2020Article
- An Extended Primer Grip of Picornavirus Polymerase Facilitates Sexual RNA Replication Mechanisms.Journal of virology · 2020Article
- Article
- Activity-Based Protein Profiling Identifies ATG4B as a Key Host Factor for Enterovirus 71 Proliferation.Journal of virology · 2019Article
- Monoclonal antibody against EV71 3DBMC immunology · 2019Article
- The Strategy of Picornavirus Evading Host Antiviral Responses: Non-structural Proteins Suppress the Production of IFNs.Frontiers in microbiology · 2018Review
- Enterovirus A71 Proteins: Structure and Function.Frontiers in microbiology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VPg uridylylation is essential for picornavirus RNA replication. The VPg uridylylation reaction consists of the binding of VPg to 3D polymerase (3D(pol)) and the transfer of UMP by 3D(pol) to the hydroxyl group of the third amino acid Tyr of VPg. Previous studies suggested that different picornaviruses employ distinct mechanisms during VPg binding and uridylylation. Here, we report a novel site (Site-311, located at the base of the palm domain of EV71 3D(pol)) that is essential for EV71 VPg uridylylation as well as viral replication. Ala substitution of amino acids (T313, F314, and I317) at Site-311 reduced the VPg uridylylation activity of 3D(pol) by >90%. None of the Site-311 mutations affected the RNA elongation activity of 3D(pol), which indicates that Site-311 does not directly participate in RNA polymerization. However, mutations that abrogated VPg uridylylation significantly reduced the VPg binding ability of 3D(pol), which suggests that Site-311 is a potential VPg binding site on enterovirus 71 (EV71) 3D(pol). Mutation of a polymerase active site in 3D(pol) and Site-311 in 3D(pol) remarkably enables trans complementation to restore VPg uridylylation. In contrast, two distinct Site-311 mutants do not cause trans complementation in vitro. These results indicate that Site-311 is a VPg binding site that stabilizes the VPg molecule during the VPg uridylylation process and suggest a two-molecule model for 3D(pol) during EV71 VPg uridylylation, such that one 3D(pol) presents the hydroxyl group of Tyr3 of VPg to the polymerase active site of another 3D(pol), which in turn catalyzes VPg→VPg-pU conversion. For genome-length RNA, the Site-311 mutations that reduced VPg uridylylation were lethal for EV71 replication, which indicates that Site-311 is a potential antiviral target.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.