ArticleJournal of virology2008
The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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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
57 citing papers in PubMed.
- Poliovirus 3Dpol polymerase region is essential for cleavage of poliovirus 3AB in vivo.PLoS pathogens · 2026Article
- The neddylation of the RNA-dependent RNA polymerase 3D of Coxsackievirus B3 promotes viral replication.Journal of virology · 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
- Sequences and Structures of Viral Proteins Linked to the Genomes (VPg) of RNA Viruses.Viruses · 2025Review
- Multiple functions of the nonstructural protein 3D in picornavirus infection.Frontiers in immunology · 2024Review
- Dual role of the foot-and-mouth disease virus 3B1 protein in the replication complex: As protein primer and as an essential component to recruit 3Dpol to membranes.PLoS pathogens · 2023Article
- VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure.International journal of molecular sciences · 2023Article
- A cysteine protease inhibitor GC376 displays potent antiviral activity against coxsackievirus infection.Current research in microbial sciences · 2023Article
- Review
- Protein Nucleotidylylation in +ssRNA Viruses.Viruses · 2021Review
- A comparative analysis of parechovirus protein structures with other picornaviruses.Open biology · 2021Article
- Development of Group B Coxsackievirus as an Oncolytic Virus: Opportunities and Challenges.Viruses · 2021Article
- Picornaviruses: A View from 3A.Viruses · 2021Review
- Structural Biology of the Enterovirus Replication-Linked 5'-Cloverleaf RNA and Associated Virus Proteins.Microbiology and molecular biology reviews : MMBR · 2020Review
- Evolutionary histories of coxsackievirus B5 and swine vesicular disease virus reconstructed by phylodynamic and sequence variation analyses.Scientific reports · 2018Article
- Review
- Insight Into the Interaction Between RNA Polymerase and VPg for Murine Norovirus Replication.Frontiers in microbiology · 2018Article
- Structure and Function of Caliciviral RNA Polymerases.Viruses · 2017Review
- Picornaviral polymerase structure, function, and fidelity modulation.Virus research · 2017Review
- SIRT1 inhibits EV71 genome replication and RNA translation by interfering with the viral polymerase and 5'UTR RNA.Journal of cell science · 2016Article
Corrections and comments
- AssociatedPublication
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA-dependent RNA polymerase (RdRp) is a central piece in the replication machinery of RNA viruses. In picornaviruses this essential RdRp activity also uridylates the VPg peptide, which then serves as a primer for RNA synthesis. Previous genetic, binding, and biochemical data have identified a VPg binding site on poliovirus RdRp and have shown that is was implicated in VPg uridylation. More recent structural studies have identified a topologically distinct site on the closely related foot-and-mouth disease virus RdRp supposed to be the actual VPg-primer-binding site. Here, we report the crystal structure at 2.5-A resolution of active coxsackievirus B3 RdRp (also named 3D(pol)) in a complex with VPg and a pyrophosphate. The pyrophosphate is situated in the active-site cavity, occupying a putative binding site either for the coproduct of the reaction or an incoming NTP. VPg is bound at the base of the thumb subdomain, providing first structural evidence for the VPg binding site previously identified by genetic and biochemical methods. The binding mode of VPg to CVB3 3D(pol) at this site excludes its uridylation by the carrier 3D(pol). We suggest that VPg at this position is either uridylated by another 3D(pol) molecule or that it plays a stabilizing role within the uridylation complex. The CVB3 3D(pol)/VPg complex structure is expected to contribute to the understanding of the multicomponent VPg-uridylation complex essential for the initiation of genome replication of picornaviruses.
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