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Journal of virology2018; 92(7); e01997-17; doi: 10.1128/JVI.01997-17

Roles of the 5′ Untranslated Region of Nonprimate Hepacivirus in Translation Initiation and Viral Replication.

Abstract: The 5' untranslated region (UTR) of hepatitis C virus (HCV), which is composed of four domains (I, II, III, and IV) and a pseudoknot, is essential for translation and viral replication. Equine nonprimate hepacivirus (EHcV) harbors a 5' UTR consisting of a large 5'-terminal domain (I); three additional domains (I', II, and III), which are homologous to domains I, II, and III, respectively, of HCV; and a pseudoknot, in the order listed. In this study, we investigated the roles of the EHcV 5' UTR in translation and viral replication. The internal ribosome entry site (IRES) activity of the EHcV 5' UTR was lower than that of the HCV 5' UTR in several cell lines due to structural differences in domain III. Domains I and III of EHcV were functional in the HCV 5' UTR in terms of IRES activity and the replication of the subgenomic replicon (SGR), although domain II was not exchangeable between EHcV and HCV for SGR replication. Furthermore, the region spanning domains I and I' of EHcV (the 5'-proximal EHcV-specific region) improved RNA stability and provided the HCV SGR with microRNA 122 (miR-122)-independent replication capability, while EHcV domain I alone improved SGR replication and RNA stability irrespective of miR-122. These data suggest that the region spanning EHcV domains I and I' improves RNA stability and viral replication regardless of miR-122 expression. The 5'-proximal EHcV-specific region may represent an inherent mechanism to facilitate viral replication in nonhepatic tissues. EHcV is the closest viral homolog to HCV among other hepaciviruses. HCV exhibits a narrow host range and liver-specific tropism, while epidemiological reports suggest that EHcV infects the liver and respiratory organs in horses, donkeys, and dogs. However, the mechanism explaining the differences in host or organ tropism between HCV and EHcV is unknown. In this study, our data suggest that the 5' untranslated region (UTR) of EHcV is composed of an internal ribosome entry site (IRES) element that is functionally exchangeable with HCV IRES elements. Furthermore, the 5'-proximal EHcV-specific region enhances viral replication and RNA stability in a miR-122-independent manner. Our data suggest that the region upstream of domain II in the EHcV 5' UTR contributes to the differences in tissue tropism observed between these hepaciviruses.
Copyright © 2018 American Society for Microbiology.
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Publication Date: 2018-03-14 PubMed ID: 29343570PubMed Central: PMC5972865DOI: 10.1128/JVI.01997-17Google 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.

The research study investigates the role of the equine nonprimate hepacivirus (EHcV) 5′ untranslated region (UTR) in translation and viral replication. It reveals crucial differences between EHcV and Hepatitis C virus (HCV), suggesting a potential difference in tissue tropism among hepaciviruses.

Study Objective and Background

  • The purpose of this study was to examine the roles of the 5′ untranslated region (UTR) of equine nonprimate hepacivirus (EHcV) in the initial stages of protein synthesis (translation) and virus replication.
  • Understanding these roles is critical because they might influence the Hepacivirus’s ability to infect various organs (tissue tropism). The 5′ UTR of Hepatitis C virus (HCV), a kind of Hepacivirus, has previously been identified as critical for these processes.
  • HCV has a narrow host range and primarily infects the liver, while EHcV is known to infect the liver and respiratory organs of horses, donkeys, and dogs. The differing characteristics of the viruses’ 5′ UTRs might explain these differences in host and tissue tropism.

Key Findings

  • Researchers found that the Internal Ribosome Entry Site (IRES) activity of the EHcV 5′ UTR was lower than that of the HCV 5′ UTR due to structural differences. IRES activity refers to a pathway that allows certain viruses to hijack a host cell’s machinery to translate viral proteins.
  • However, they noted that not all domains of the 5′ UTR were equally interchangeable between the two viruses. While domains I and III of EHcV worked in the HCV 5′ UTR for IRES activity and replication, domain II wasn’t exchangeable for subgenomic replicon (SGR) replication. SGR replication is a part of the viral replication process.
  • Importantly, the region spanning domains I and I’ of EHcV enhances RNA stability and provides the HCV SGR with microRNA 122 (miR-122)-independent replication capability. microRNA are small non-coding RNA molecules that play key roles in regulating gene expressions.
  • The same region could improve viral replication and RNA stability irrespective of the presence of miR-122, suggesting it may have inherent mechanisms promoting viral replication in nonhepatic tissues.

Conclusions and Implications

  • The findings suggest that differences in the 5′ untranslated region (UTR) of EHcV and HCV could explain the observed differences in tissue tropism between these Hepaciviruses.
  • This study’s insights may facilitate the development of treatments targeting the 5′ UTR and may contribute to our understanding of viral tropism, potentially leading to more effective preventative and therapeutic measures.

Cite This Article

APA
Tanaka T, Otoguro T, Yamashita A, Kasai H, Fukuhara T, Matsuura Y, Moriishi K. (2018). Roles of the 5′ Untranslated Region of Nonprimate Hepacivirus in Translation Initiation and Viral Replication. J Virol, 92(7), e01997-17. https://doi.org/10.1128/JVI.01997-17

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 92
Issue: 7
PII: e01997-17

Researcher Affiliations

Tanaka, Tomohisa
  • Department of Microbiology, Graduate School of Medical Science, University of Yamanashi, Yamanashi, Japan.
Otoguro, Teruhime
  • Department of Microbiology, Graduate School of Medical Science, University of Yamanashi, Yamanashi, Japan.
Yamashita, Atsuya
  • Department of Microbiology, Graduate School of Medical Science, University of Yamanashi, Yamanashi, Japan.
Kasai, Hirotake
  • Department of Microbiology, Graduate School of Medical Science, University of Yamanashi, Yamanashi, Japan.
Fukuhara, Takasuke
  • Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Matsuura, Yoshiharu
  • Department of Molecular Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Moriishi, Kohji
  • Department of Microbiology, Graduate School of Medical Science, University of Yamanashi, Yamanashi, Japan kmoriishi@yamanashi.ac.jp.

MeSH Terms

  • 5' Untranslated Regions / physiology
  • A549 Cells
  • HEK293 Cells
  • Hepacivirus / physiology
  • Humans
  • MicroRNAs / genetics
  • MicroRNAs / metabolism
  • Peptide Chain Initiation, Translational / physiology
  • RNA Stability / physiology
  • RNA, Viral / genetics
  • RNA, Viral / metabolism
  • Viral Proteins / biosynthesis
  • Virus Replication / physiology

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Citations

This article has been cited 4 times.
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