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Home / Equine Research Bank / J Virol / Analysis of Venezuelan equine encephalitis virus capsid prot...
Journal of virology2007; 81(24); 13552-13565; doi: 10.1128/JVI.01576-07

Analysis of Venezuelan equine encephalitis virus capsid protein function in the inhibition of cellular transcription.

Abstract: The encephalitogenic New World alphaviruses, including Venezuelan (VEEV), eastern (EEEV), and western equine encephalitis viruses, constitute a continuing public health threat in the United States. They circulate in Central, South, and North America and have the ability to cause fatal disease in humans and in horses and other domestic animals. We recently demonstrated that these viruses have developed the ability to interfere with cellular transcription and use it as a means of downregulating a cellular antiviral response. The results of the present study suggest that the N-terminal, approximately 35-amino-acid-long peptide of VEEV and EEEV capsid proteins plays the most critical role in the downregulation of cellular transcription and development of a cytopathic effect. The identified VEEV-specific peptide C(VEE)33-68 includes two domains with distinct functions: the alpha-helix domain, helix I, which is critically involved in supporting the balance between the presence of the protein in the cytoplasm and nucleus, and the downstream peptide, which might contain a functional nuclear localization signal(s). The integrity of both domains not only determines the intracellular distribution of the VEEV capsid but is also essential for direct capsid protein functioning in the inhibition of transcription. Our results suggest that the VEEV capsid protein interacts with the nuclear pore complex, and this interaction correlates with the protein's ability to cause transcriptional shutoff and, ultimately, cell death. The replacement of the N-terminal fragment of the VEEV capsid by its Sindbis virus-specific counterpart in the VEEV TC-83 genome does not affect virus replication in vitro but reduces cytopathogenicity and results in attenuation in vivo. These findings can be used in designing a new generation of live, attenuated, recombinant vaccines against the New World alphaviruses.
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Publication Date: 2007-10-03 PubMed ID: 17913819PubMed Central: PMC2168819DOI: 10.1128/JVI.01576-07Google 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 article explores how Venezuelan equine encephalitis virus (VEEV) has developed its capability to interrupt cellular transcription, which is part of its strategy to inhibit cellular antiviral responses. It particularly focuses on a specific region of VEEV and Eastern equine encephalitis virus (EEEV) capsid proteins and their role in suppressing cellular transcription and causing cellular damage.

Investigating Capsid Proteins of Alphaviruses

  • The focus of the study is on the encephalitogenic New World alphaviruses. These alphaviruses, including VEEV, EEEV, circulate in the Americas and can cause fatal diseases in humans and other animals like horses.
  • The study dives into how these viruses are capable of inhibiting cellular transcription, a process fundamental to cellular operation and a key part of the cellular antiviral response.
  • The research concentrates on exploring the capsid proteins of these viruses—specifically an approximately 35-amino-acid-long segment at the N-terminal of the VEEV and EEEV capsid proteins.

Identifying Functional Domains

  • The research identifies two distinct functional domains within a VEEV-specific peptide. The first, an alpha-helix domain, is crucial for balancing the presence of the peptide in the cytoplasm and nucleus of a cell.
  • The second domain appears to contain a functional nuclear localization signal—possibly leading the capsid protein to the nucleus.
  • The study highlights that the integrity of both domains is important for the proper localization and functioning of the VEEV capsid proteins in cellular transcription inhibition.

Interactions and Influence of Capsid Proteins

  • The article states that VEEV capsid proteins interact with the nuclear pore complex—a gateway for molecular traffic into and out of the nucleus—that can lead to transcriptional shutoff and eventual cell death.
  • Interestingly, when replacing the N-terminal fragment of the VEEV capsid with its Sindbis virus-specific counterpart in the VEEV genome, the researchers observed that this modification did not affect virus replication in the lab but resulted in a reduction of cellular damage and an attenuation of the virus in a living system.

Implications for Future Vaccine Design

  • The findings of the study can be significantly valuable for designing new vaccines against the New World alphaviruses. The ability to alter the VEEV genome to reduce its damaging effects presents an opportunity to develop live, attenuated, recombinant vaccines—ones that use a living but weakened version of the virus. This method has the potential to stimulate a robust immune response while avoiding heavy disease symptoms.

Cite This Article

APA
Garmashova N, Atasheva S, Kang W, Weaver SC, Frolova E, Frolov I. (2007). Analysis of Venezuelan equine encephalitis virus capsid protein function in the inhibition of cellular transcription. J Virol, 81(24), 13552-13565. https://doi.org/10.1128/JVI.01576-07

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 81
Issue: 24
Pages: 13552-13565

Researcher Affiliations

Garmashova, Natalia
  • Department of Microbiology and Immunology, University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 77555-1019, USA.
Atasheva, Svetlana
    Kang, Wenli
      Weaver, Scott C
        Frolova, Elena
          Frolov, Ilya

            MeSH Terms

            • Animals
            • Capsid Proteins / genetics
            • Capsid Proteins / metabolism
            • Capsid Proteins / pharmacology
            • Cell Survival
            • Cricetinae
            • Cytopathogenic Effect, Viral
            • Encephalitis Virus, Venezuelan Equine / genetics
            • Encephalitis Virus, Venezuelan Equine / metabolism
            • Encephalitis Virus, Venezuelan Equine / pathogenicity
            • Encephalomyelitis, Venezuelan Equine / mortality
            • Encephalomyelitis, Venezuelan Equine / pathology
            • Encephalomyelitis, Venezuelan Equine / virology
            • Female
            • Immunization
            • Mice
            • Mutation
            • Proteins / genetics
            • Proteins / metabolism
            • Transcription, Genetic / drug effects

            Grant Funding

            • U54 AI057156 / NIAID NIH HHS
            • R01 AI050537-04 / NIAID NIH HHS
            • R21 AI050537 / NIAID NIH HHS
            • AI050537 / NIAID NIH HHS
            • R01 AI050537 / NIAID NIH HHS

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