ArticleThe Journal of general virology2009
Interaction of Sindbis virus non-structural protein 3 with poly(ADP-ribose) polymerase 1 in neuronal cells.
Article in The Journal of general virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Cell type-dependent induction of type I interferon and PARP1 activation in astrocytes and neurons during chikungunya virus infection.Microbiology spectrum · 2026Article
- Alphavirus nsP3 as a multifunctional orchestrator of virus-host interplay.Journal of virology · 2026Review
- Neurotropic alphavirus infection induces PARP-1 hyperactivation-mediated energy collapse in motor neurons.Journal of virology · 2026Article
- Zinc-finger PARP proteins ADP-ribosylate alphaviral proteins and are required for interferon-γ-mediated antiviral immunity.Science advances · 2025Article
- Identification of mosquito proteins that differentially interact with alphavirus nonstructural protein 3, a determinant of vector specificity.PLoS neglected tropical diseases · 2023Article
- Sindbis Macrodomain Poly-ADP-Ribose Hydrolase Activity Is Important for Viral RNA Synthesis.Journal of virology · 2022Article
- Article
- Review
- Stress granule formation, disassembly, and composition are regulated by alphavirus ADP-ribosylhydrolase activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Virus-Host Interplay Between Poly (ADP-Ribose) Polymerase 1 and Oncogenic Gammaherpesviruses.Frontiers in microbiology · 2021Review
- Article
- Article
- ADP-ribosyl-binding and hydrolase activities of the alphavirus nsP3 macrodomain are critical for initiation of virus replication.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mutation of CD2AP and SH3KBP1 Binding Motif in Alphavirus nsP3 Hypervariable Domain Results in Attenuated Virus.Viruses · 2018Article
- The Enigmatic Alphavirus Non-Structural Protein 3 (nsP3) Revealing Its Secrets at Last.Viruses · 2018Review
- ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Interactions of Alphavirus nsP3 Protein with Host Proteins.Frontiers in microbiology · 2017Review
- Viral Macro Domains Reverse Protein ADP-Ribosylation.Journal of virology · 2016Article
- Alphavirus Encephalomyelitis: Mechanisms and Approaches to Prevention of Neuronal Damage.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2016Review
- Differences in Processing Determinants of Nonstructural Polyprotein and in the Sequence of Nonstructural Protein 3 Affect Neurovirulence of Semliki Forest Virus.Journal of virology · 2015Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The alphavirus non-structural protein 3 (nsP3) has a conserved N-terminal macro domain and a variable highly phosphorylated C-terminal domain. nsP3 forms complexes with cellular proteins, but its role in virus replication is poorly understood and protein interaction domains have not been defined. As the N-terminal macro domain can bind poly(ADP-ribose) (PAR), and PAR polymerase-1 (PARP-1) is activated and autoribosylated during Sindbis virus (SINV) infection, it was hypothesized that PARP-1 and nsP3 may interact. Co-immunoprecipitation studies showed that PARP-1 interacted with nsP3 during SINV infection of NSC34 neuronal cells and was most abundantly present in replication complexes that contained plus- and minus-strand SINV RNAs 10-14 h after infection, prior to PARP-1 activation or automodification with PAR. Treatment with an inhibitor of PARP enzymic activity did not affect the interaction between nsP3 and PARP-1 or SINV replication. Co-expression of individual domains of nsP3 with PARP-1 showed that nsP3 interacted with PARP-1 through the C-terminal domain, not the N-terminal macro domain, and that phosphorylation was not required. It was concluded that PARP-1 interacts with the C-terminal domain of nsP3, is present in replication complexes during virus amplification and may play a role in regulating virus RNA synthesis in neuronal cells.
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