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Home / Equine Research Bank / J Gen Virol / Proteolytic maturation of replicase polyprotein pp1a by the ...
The Journal of general virology2006; 87(Pt 12); 3473-3482; doi: 10.1099/vir.0.82269-0

Proteolytic maturation of replicase polyprotein pp1a by the nsp4 main proteinase is essential for equine arteritis virus replication and includes internal cleavage of nsp7.

Abstract: The positive-stranded RNA genome of the arterivirus Equine arteritis virus (order Nidovirales) encodes the partially overlapping replicase polyproteins pp1a (1727 aa) and pp1ab (3175 aa). Previously, three viral proteinases were reported to cleave these large polyproteins into 12 non-structural proteins (nsps). The chymotrypsin-like viral main proteinase residing in nsp4 is responsible for eight of these cleavages. Processing of the C-terminal half of pp1a (the nsp3-8 region) was postulated to occur following either of two alternative proteolytic pathways (the 'major' and 'minor' pathways). Here, the importance of these two pathways was investigated by using a reverse-genetics system and inactivating each of the cleavage sites by site-directed mutagenesis. For all of these pp1a cleavage sites, mutations that prevented cleavage by the nsp4 proteinase were found to block or severely inhibit EAV RNA synthesis. Furthermore, our studies identified a novel nsp4 cleavage site (Glu-1575/Ala-1576) that is located within nsp7 and is conserved in arteriviruses. The N-terminal nsp7 fragment (nsp7alpha) derived from this cleavage was detected in lysates of both EAV-infected cells and cells transiently expressing pp1a. Mutagenesis of the novel cleavage site in the context of an EAV full-length cDNA clone proved to be lethal, underlining the fact that the highly regulated, nsp4-mediated processing of the C-terminal half of pp1a is a crucial event in the arterivirus life cycle.
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Publication Date: 2006-11-14 PubMed ID: 17098961DOI: 10.1099/vir.0.82269-0Google Scholar: Lookup
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  • Non-U.S. Gov't

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.

The study delves into the role of a specific proteinase, nsp4, in the replication process of the Equine arteritis virus (EAV), a type of arterivirus. It was found that the proteolytic maturation process driven by nsp4 is critical for the virus replication and includes the internal cleavage of a protein known as nsp7.

Theoretical Background

  • The research focuses on Equine arteritis virus (EAV), a type of arterivirus, which has a positive-stranded RNA genome. This genome encodes two polyproteins, pp1a and pp1ab, which are slightly overlapping.
  • These polyproteins undergo cleavage by three viral proteinases into 12 non-structural proteins (nsps), with the nsp4 proteinase being responsible for eight of these breakdowns.
  • Processing of the C-terminal half of pp1a (including the nsp3-8 region) was theorized to proceed through one of two proteolytic pathways, labeled as ‘major’ and ‘minor’.

Experiment and Findings

  • Research was conducted on the relevance of these two proteolytic pathways by utilizing a reverse-genetics system and deactivating each of the cleavage points through site-directed mutagenesis.
  • The outcome displayed that for all pp1a cleavage locations, mutations that hindered cleavage by the nsp4 proteinase resulted in either a complete block or severe inhibition of EAV RNA synthesis.
  • More so, a new nsp4 cleavage site was distinguished within nsp7, revealing itself to be conserved among arteriviruses. The N-terminal nsp7 fragment, or nsp7alpha, is derived from this cleavage and was discoverable in cells infected with EAV or those transiently expressing pp1a.
  • Introducing a mutation to this newly-found cleavage site in the context of an EAV full-length cDNA clone was proven lethal. This result emphasizes the importance of the highly controlled nsp4-mediated processing of the C-terminal half of pp1a in the lifecycle of arteriviruses.

Implication

  • The study underscores the vital role of the nsp4 proteinase in the lifecycle of EAV and arterivirus replication, and identification of its novel cleavage site expands our current understanding of these mechanisms.
  • This work could open doors to further research and potential therapeutic strategies to combat diseases caused by arteriviruses.

Cite This Article

APA
van Aken D, Zevenhoven-Dobbe J, Gorbalenya AE, Snijder EJ. (2006). Proteolytic maturation of replicase polyprotein pp1a by the nsp4 main proteinase is essential for equine arteritis virus replication and includes internal cleavage of nsp7. J Gen Virol, 87(Pt 12), 3473-3482. https://doi.org/10.1099/vir.0.82269-0

Publication

The Journal of general virology
ISSN: 0022-1317
NlmUniqueID: 0077340
Country: England
Language: English
Volume: 87
Issue: Pt 12
Pages: 3473-3482

Researcher Affiliations

van Aken, Danny
  • Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, LUMC E4-P, PO Box 9600, 2300 RC Leiden, The Netherlands.
Zevenhoven-Dobbe, Jessika
  • Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, LUMC E4-P, PO Box 9600, 2300 RC Leiden, The Netherlands.
Gorbalenya, Alexander E
  • Molecular Virology Laboratory, Department of Medical Microbiology, 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, Leiden University Medical Center, LUMC E4-P, PO Box 9600, 2300 RC Leiden, The Netherlands.

MeSH Terms

  • Animals
  • Cell Line
  • Cricetinae
  • Equartevirus / physiology
  • Gene Products, pol / genetics
  • Gene Products, pol / metabolism
  • Mutagenesis, Site-Directed
  • Peptide Hydrolases / metabolism
  • Protein Processing, Post-Translational
  • RNA, Viral / biosynthesis
  • Viral Nonstructural Proteins / metabolism
  • Virus Replication / physiology

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