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Home / Equine Research Bank / J Virol / Capsid protein of eastern equine encephalitis virus inhibits...
Journal of virology2007; 81(8); 3866-3876; doi: 10.1128/JVI.02075-06

Capsid protein of eastern equine encephalitis virus inhibits host cell gene expression.

Abstract: Eastern equine encephalitis virus (EEEV) causes sporadic but often severe cases of human and equine neurological disease in North America. To determine how EEEV may evade innate immune responses, we screened individual EEEV proteins for the ability to rescue the growth of a Newcastle disease virus expressing green fluorescent protein (NDV-GFP) from the antiviral effects of interferon (IFN). Only expression of the EEEV capsid facilitated NDV-GFP replication. Inhibition of the antiviral effects of IFN by the capsid appears to occur through a general inhibition of cellular gene expression. For example, the capsid inhibited the expression of several reporter genes under the control of RNA polymerase II promoters. In contrast, capsid did not inhibit expression from a T7 RNA polymerase promoter construct, suggesting that the inhibition of gene expression is specific and is not a simple manifestation of toxicity. The inhibition correlated both with capsid-induced phosphorylation of eukaryotic initiation factor 2 alpha and with capsid-mediated inhibition of cellular mRNA accumulation. Mapping analysis identified the N terminus as the region important for the inhibition of host gene expression, suggesting that this inhibition is independent of capsid protease activity. Finally, when cell lines containing EEEV replicons encoding capsid were selected, replicons consistently acquired mutations that deleted all or part of the capsid, for example, amino acids 18 to 135. Given that the amino terminus of the capsid is required to inhibit host cell gene expression, these data suggest that capsid expression from the replicons is ultimately toxic to host cells, presumably because of its ability to inhibit gene expression.
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Publication Date: 2007-01-31 PubMed ID: 17267491PubMed Central: PMC1866141DOI: 10.1128/JVI.02075-06Google 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.

This research studied how the eastern equine encephalitis virus (EEEV) can avoid immune responses by inhibiting host cell gene expression via its capsid protein.

Introduction

  • The Eastern equine encephalitis virus (EEEV) is responsible for serious neurological diseases in humans and equines in North America. There are sporadic outbreaks of this virus and it’s therefore crucial to understand how it interacts with the host’s immune system.
  • The researchers were particularly interested in understanding how the EEEV might be bypassing the immune responses of the host.

Methodology

  • The researchers conducted a screening of individual EEEV proteins to see if they had the ability to counteract the antiviral effects of interferon (IFN), a protein the body produces in response to a viral infection.
  • They utilized a Newcastle disease virus expressing green fluorescent protein (NDV-GFP) in their assessment. By observing which EEEV proteins facilitated the replication of NDV-GFP, they could identify which were capable of outmanoeuvring the host’s defenses.
  • In this case, only the EEEV capsid was found to facilitate NDV-GFP replication.

Findings

  • The researchers found that the capsid inhibits the antiviral effects of IFN, seemingly due to a general inhibition of cellular gene expression.
  • The capsid of the EEEV was found to hamper the expression of different reporter genes, controlling RNA polymerase II promoters; in contrast it did not suppress the expression from a T7 RNA polymerase promoter construct, signaling that the inhibition is specific and not merely due to toxicity.
  • The inhibition of gene expression was linked to both the capsid-provoked phosphorylation of eukaryotic initiation factor 2 alpha and the capsid’s ability to reduce the accumulation of cellular mRNA.
  • The N terminus of the capsid was the key region for impeding host gene expression, suggesting that this inhibition is detached from capsid protease activity.
  • In various cell lines including EEEV replicons encoding capsid, replicons recurrently acquired mutations which deleted parts or the entirety of the capsid. This observation underlines that the capsid’s expression from the replicons is eventually harmful to host cells due to its capacity to inhibit gene expression.

Conclusion

  • The research reveals that the EEEV manages to shun the host immune response by inhibiting gene expression through its capsid protein, which could be key to understanding and combatting the disease caused by the virus.

Cite This Article

APA
Aguilar PV, Weaver SC, Basler CF. (2007). Capsid protein of eastern equine encephalitis virus inhibits host cell gene expression. J Virol, 81(8), 3866-3876. https://doi.org/10.1128/JVI.02075-06

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 81
Issue: 8
Pages: 3866-3876

Researcher Affiliations

Aguilar, Patricia V
  • Department of Microbiology, Box 1124, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA.
Weaver, Scott C
    Basler, Christopher F

      MeSH Terms

      • Capsid Proteins / immunology
      • Capsid Proteins / physiology
      • Cell Line
      • Chloramphenicol O-Acetyltransferase / analysis
      • Encephalitis Virus, Eastern Equine / immunology
      • Encephalitis Virus, Eastern Equine / physiology
      • Eukaryotic Initiation Factor-2 / metabolism
      • Gene Expression Regulation
      • Genes, Reporter
      • Green Fluorescent Proteins / analysis
      • Humans
      • Interferon-gamma / antagonists & inhibitors
      • Luciferases / analysis
      • Phosphorylation
      • Protein Structure, Tertiary
      • RNA, Messenger / biosynthesis
      • Virus Replication

      Grant Funding

      • U54 AI057158 / NIAID NIH HHS
      • AI057158 / NIAID NIH HHS

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