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Journal of virology1997; 71(7); 4904-4914; doi: 10.1128/JVI.71.7.4904-4914.1997

The ICP0 protein of equine herpesvirus 1 is an early protein that independently transactivates expression of all classes of viral promoters.

Abstract: To assess the role of the equine herpesvirus type 1 (EHV-1) ICP0 protein (EICP0) in gene regulation, a variety of molecular studies on the EICP0 gene and gene products of both the attenuated cell culture-adapted Kentucky A (KyA) strain and the Ab4p strain were conducted. These investigations revealed that (i) the ICP0 open reading frame (ORF) of the KyA virus strain is 1,257 bp in size and would encode a protein of 419 amino acids, and in comparison to the ICP0 gene (ORF63) of the Ab4p strain of 1,596 bp (E. A. Telford, M. S. Watson, K. McBride, and A. J. Davison, Virology 189:304-316, 1992), it has an internal in-frame deletion of 339 bp; (ii) one early transcript of 1.4 kb predicted to encode the EICP0 protein and a late transcript of 1.8 kb are detected in Northern blot analyses using probes containing the EICP0 ORF; (iii) the KyA EICP0 protein (50 kDa) and the Ab4p EICP0 protein (80 kDa) are expressed as several species of early proteins that are first detected at 3 to 4 h postinfection by Western blot analyses of infected-cell polypeptides, using an antiserum generated to a TrpE fusion protein that harbors amino acids 46 to 153 of the EICP0 protein; and (iv) the EICP0 protein of both EHV-1 strains is a potent transactivator of EHV-1 genes. Transient expression assays using a simian virus 40 expression construct of the EICP0 protein of the KyA strain showed that the EICP0 protein independently transactivated chloramphenicol acetyltransferase reporter constructs under the control of the immediate-early promoter (3.9-fold), the early thymidine kinase promoter (95-fold), the late (gamma1) IR5 promoter (85-fold), and the late (gamma2) glycoprotein K promoter (21-fold). The finding that the EICP0 protein of the KyA virus can function as an activator of gene expression indicates that amino acids corresponding to residues 319 to 431 of the Ab4p EICP0 protein are not essential for EICP0 transactivation of EHV-1 promoters.
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Publication Date: 1997-07-01 PubMed ID: 9188552PubMed Central: PMC191720DOI: 10.1128/JVI.71.7.4904-4914.1997Google 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 study explores the role of the ICP0 protein of Equine Herpesvirus Type 1 (EHV-1) in gene regulation, with a special focus on the variations between the attenuated cell culture-adapted Kentucky A (KyA) strain and the Ab4p strain. It reveals that the EICP0 protein of EHV-1 can independently activate gene expression, despite having an internal in-frame deletion compared to the Ab4p strain’s ICP0 gene.

Methodology and Findings

  • The study opens with an analysis of the genetic specifics of each strain’s ICP0 protein. The KyA strain’s ICP0 open reading frame (ORF) measures 1,257 base pairs (bp) compared to the Ab4p strain’s 1,596 bp. The KyA strain’s EICP0 gene has an internal in-frame deletion of 339 bp in relation to the Ab4p’s ICP0 gene.
  • The researchers identified two transcripts related to the EICP0 protein—a 1.4 kb early transcript and a 1.8 kb late transcript—through Northern blot analyses using probes containing the EICP0 ORF.
  • Three to four hours after infection, early proteins expressed by the KyA and Ab4p EICP0 genes were detected. Western blot analyses discerned these proteins using an antiserum generated to a TrpE fusion protein encoding a fraction of the EICP0 protein.
  • The investigation confirms that EICP0 can effectively transactivate EHV-1 genes, suggesting its crucial role in gene regulation.

Functional Assessment of EICP0

  • Transient expression assays were conducted to evaluate the transactivation capacity of EICP0 from the KyA strain. This process entailed using a simian virus 40 expression construct of the KyA’s EICP0 protein.
  • The results demonstrated that the EICP0 protein could independently transactivate chloramphenicol acetyltransferase reporter constructs governed by four viral promoters.
  • This evidence suggests that within the EICP0 protein, residues 319 to 431, which are missing in the KyA variant due their internal in-frame deletion compared to the Ab4p strain’s gene, are not crucial for the transactivation of EHV-1 promoters.

Cite This Article

APA
Bowles DE, Holden VR, Zhao Y, O'Callaghan DJ. (1997). The ICP0 protein of equine herpesvirus 1 is an early protein that independently transactivates expression of all classes of viral promoters. J Virol, 71(7), 4904-4914. https://doi.org/10.1128/JVI.71.7.4904-4914.1997

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 71
Issue: 7
Pages: 4904-4914

Researcher Affiliations

Bowles, D E
  • Department of Microbiology and Immunology, Louisiana State University Medical Center, Shreveport 71130-3932, USA.
Holden, V R
    Zhao, Y
      O'Callaghan, D J

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Base Sequence
        • Cell Line
        • DNA, Viral
        • Gene Expression Regulation, Viral
        • Genes, Viral
        • Molecular Sequence Data
        • Promoter Regions, Genetic
        • Rabbits
        • Sequence Analysis, DNA
        • Sequence Homology, Amino Acid
        • Sequence Homology, Nucleic Acid
        • Transcriptional Activation
        • Viral Proteins / genetics

        Grant Funding

        • AI-22001 / NIAID NIH HHS

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