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The Journal of general virology2003; 84(Pt 9); 2317-2322; doi: 10.1099/vir.0.19297-0

Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100.

Abstract: Non-structural protein 1 (nsp1), the N-terminal subunit of the replicase polyprotein of the arterivirus Equine arteritis virus (EAV), is essential for viral subgenomic mRNA synthesis, but fully dispensable for genome replication. However, at the molecular level, the role of nsp1 in EAV subgenomic mRNA synthesis is poorly understood. A yeast two-hybrid screen did not reveal interactions between EAV nsp1 and other viral non-structural proteins or the nucleocapsid protein, although both nsp1 and the nucleocapsid protein were found to form homomers. Subsequently, a yeast two-hybrid screen of a HeLa cell cDNA library was performed using nsp1 as bait. Remarkably, this analysis revealed (potential) interactions between EAV nsp1 and factors that are involved in host cell transcriptional regulation. The interaction of nsp1 with one of these proteins, p100, a transcription co-activator that also interacts with regulatory proteins of other viruses, was confirmed by mutual co-immunoprecipitation from lysates of EAV-susceptible mammalian cells.
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Publication Date: 2003-08-15 PubMed ID: 12917451DOI: 10.1099/vir.0.19297-0Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research investigates the role of non-structural protein 1 (nsp1) in the arterivirus Equine arteritis virus (EAV) in the production of viral subgenomic mRNA. By utilizing yeast two-hybrid screens, the interaction between nsp1 and cellular transcription co-factor p100—an integral part of host cell transcriptional regulation—was revealed and confirmed through mutual co-immunoprecipitation.

Understanding nsp1 and its Role in EAV

  • The study delves into the importance of nsp1, a component of the EAV replicase polyprotein, in the infectious process.
  • While nsp1’s role in the synthesis of viral subgenomic mRNA is deemed crucial, it is considered unnecessary for genome replication.
  • This research seeks to uncover and explore the aspects of nsp1’s function at a molecular level, which as of yet remains ill-defined.

Protein Interactions Analysis: Yeast Two-Hybrid Screen

  • The researchers utilized a yeast two-hybrid screening system to appraise any possible interactions between nsp1 and other non-structural proteins or the nucleocapsid protein of EAV.
  • This test did not reveal any potential interactions involving nsp1, although the experiment did affirm that both nsp1 and the nucleocapsid protein could form homomers, indicating similar structures.

Identifying Interactions with Host Cell Factors

  • In a subsequent experiment, the team conducted an additional yeast two-hybrid screen with a library of HeLa cell cDNA, harnessing nsp1 as a bait protein.
  • This screen interestingly revealed a potential interaction between nsp1 and various factors directly tied to host cell transcriptional regulation.

Discovering nsp1-p100 Interaction

  • Notably, the study disclosed a specific interaction between nsp1 and the cellular transcription co-factor p100.
  • This interaction was tested and confirmed through a process known as mutual co-immunoprecipitation from lysates of EAV-susceptible mammalian cells.
  • The p100 protein is a co-activator in transcription and has been identified as interacting with the regulatory proteins of other viruses, underscoring the potential interplay between viral and host replication mechanisms.

Cite This Article

APA
Tijms MA, Snijder EJ. (2003). Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100. J Gen Virol, 84(Pt 9), 2317-2322. https://doi.org/10.1099/vir.0.19297-0

Publication

The Journal of general virology
ISSN: 0022-1317
NlmUniqueID: 0077340
Country: England
Language: English
Volume: 84
Issue: Pt 9
Pages: 2317-2322

Researcher Affiliations

Tijms, Marieke A
  • Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, LUMC E4-P, PO Box 9600, 2300 RC Leiden, The Netherlands.
Snijder, Eric J
  • Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, LUMC E4-P, PO Box 9600, 2300 RC Leiden, The Netherlands.

MeSH Terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Equartevirus / metabolism
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Nucleocapsid Proteins / metabolism
  • RNA, Messenger / biosynthesis
  • RNA, Viral / biosynthesis
  • Trans-Activators / metabolism
  • Viral Nonstructural Proteins / chemistry
  • Viral Nonstructural Proteins / metabolism

Citations

This article has been cited 24 times.
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