Pseudorabies virus early protein 0 transactivates the viral gene promoters.

@article{Watanabe1995PseudorabiesVE,
  title={Pseudorabies virus early protein 0 transactivates the viral gene promoters.},
  author={S. Watanabe and E. Ono and Y. Shimizu and H. Kida},
  journal={The Journal of general virology},
  year={1995},
  volume={76 ( Pt 11)},
  pages={
          2881-5
        }
}
Pseudorabies virus (PRV) early protein 0 (EP0) contains the RING finger domain with homology to the immediate-early (IE) protein ICP0 of herpes simplex virus type 1 (HSV-1). EP0 was detected by indirect immunofluorescence in the nuclei of the cells transfected with EP0 expression plasmid as is the case in cells infected with PRV. In transient expression assays, EP0 transactivated the PRV IE, thymidine kinase (TK) and glycoprotein X (gX) promoters, indicating that EP0, like ICP0 of HSV-1, is a… Expand
Pseudorabies virus (PRV) early protein 0 activates PRV gene transcription in combination with the immediate-early protein IE180 and enhances the infectivity of PRV genomic DNA.
TLDR
Results may indicate that EP0 in the virions acts as an important transactivator to express the immediate-early gene efficiently in the first stage of infection, and IE180 and EP0 expressed after the infection cooperatively activate the early and late gene expression in the later stage of infections. Expand
Structure of the infected cell protein 0 gene of canine herpesvirus
TLDR
The RING finger domain and acidic transcriptional activation domain were found at the N-terminus and within the middle region in the deduced amino acid sequence, respectively, suggesting that the CICP0, like the ICP0 of herpes simplex virus 1, is a transactivating protein. Expand
Inhibition of pseudorabies virus replication by a dominant-negative mutant of early protein 0 expressed in a tetracycline-regulated system.
TLDR
The present results suggest that the EP0 mutant may not alter the efficiency of the viral gene transcription but rather translation efficiency ofThe viral mRNA. Expand
Mapping of transregulatory domains of pseudorabies virus early protein 0 and identification of its dominant-negative mutant
TLDR
Pseudorabies virus (PRV) early protein 0 (EP0) is a transactivator containing the RING finger domain, and the mutant consisting of amino acids 1 to 113 exhibited a dominant-negative property. Expand
Promoter activity of sequence located upstream of the pseudorabies virus early protein 0 gene.
TLDR
Results indicate that the EP0 gene may be transcribed from the TATA-less promoter that responds to Sp1, a strong transactivator of PRV. Expand
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TLDR
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TLDR
Findings provide evidence that PRV can stimulate the expression of topoisomerase I and that the stimulation is mediated at least by IE180 and EP0 proteins of PRV at the transcriptional level. Expand
Identification of the molecular determinants for nuclear import of PRV EP0
TLDR
The subcellular localization pattern and molecular determinants for the nuclear import of EP0 were investigated and EP0 was demonstrated to predominantly target the nucleus in both PRV infected- and plasmid-transfected cells. Expand
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TLDR
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Resistance to pseudorabies virus infection in transformed cell lines expressing a soluble form of porcine herpesvirus entry mediator C.
TLDR
It is demonstrated that a soluble form of porcine HveC is able to exert a significant antiviral effect against pseudorabies virus and other alphaherpesvirus infection in vitro. Expand
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References

SHOWING 1-10 OF 23 REFERENCES
Identification and zinc dependence of the bovine herpesvirus 1 transactivator protein BICP0
TLDR
In situ immunoadsorbent assays using antisera against synthetic oligopeptides demonstrated that BICP0 accumulates in nuclei of BHV-1-infected cells, as expected for an IE gene product involved in gene regulation. Expand
Characterization of a potent varicella-zoster virus-encoded trans-repressor
TLDR
It is shown that the protein product from gene 61 of varicella-zoster virus (VZV) can repress the function of the VZV encoded trans-activators on putative viral immediate-early, early, and late gene promoters, and suggested that the ORF61 protein product can mediate down-regulation of VZv gene expression. Expand
Varicella-zoster virus open reading frame 61 protein is functionally homologous to herpes simplex virus type 1 ICP0
TLDR
Results indicate that, despite marked differences in their sequences and in effects on their cognate promoters in transient expression assays, VZV ORF61 protein is the functional homolog of HSV-1 ICP0. Expand
Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA
TLDR
VZV ORF 61 can stimulate expression of HSV-1 and VZV genes at an early stage in the viral replicative cycle and that ORF61 has an important role in VZv gene regulation. Expand
A truncated form of herpes simplex virus type 1 immediate-early protein Vmw110 is expressed in a cell type dependent manner.
TLDR
It is shown that this predicted truncated Vmw110 protein is expressed during normal HSV-1 infection, and that it must be translated from IE-1 pre-mRNAs which retain the in-frame stop codon in the second intron. Expand
Analysis of the functional domains of herpes simplex virus type 1 immediate-early polypeptide Vmw110.
  • R. Everett
  • Biology, Medicine
  • Journal of molecular biology
  • 1988
TLDR
The results show that mutations in different domains of the Vmw110 polypeptide can have different effects on function in the presence or absence of Vmmw175; that mutations can affect the pattern of immunofluorescent intranuclear staining of V mw110; and that deletions in the region of a particular highly basic region of the polyPEptide result in failure of Vw110 to be transported into the nucleus. Expand
Cloning of the latency gene and the early protein 0 gene of pseudorabies virus
  • A. Cheung
  • Medicine, Biology
  • Journal of virology
  • 1991
TLDR
The deduced amino acid sequence revealed the presence of cysteine-rich zinc finger domain similar to that of the immediate-early gene ICP0 of herpes simplex virus type 1 and the gene 61 polypeptide of varicella-zoster virus. Expand
Pseudorabies virus immediate-early gene overlaps with an oppositely oriented open reading frame: characterization of their promoter and enhancer regions.
TLDR
The immediate-early (IE) gene of pseudorabies virus (PRV) has recently been sequenced for two virus strains and sequence analysis has been extended by 5 kb from each end of the IE gene to investigate IE gene regulation and to examine the genome segment reported to encode latency-related transcripts in opposite polarity. Expand
The RING finger domain of the varicella-zoster virus open reading frame 61 protein is required for its transregulatory functions.
TLDR
Results indicate that the RING finger domain is required for the transregulatory functions of ORF61, and amino acid substitution mutants in the Ringing finger abolished the transactivating activity of the full-length ORF 61 protein. Expand
Three trans-acting regulatory proteins of herpes simplex virus modulate immediate-early gene expression in a pathway involving positive and negative feedback regulation
TLDR
Results provide direct evidence for a negative autoregulatory role of IE175K protein on its own expression at the transcriptional level and demonstrate differences in functional properties of the IE 175K and IE110K proteins, which it is speculated may reflect different mechanisms of action of the two proteins. Expand
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