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  • 1
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    Herpes Simplex Virus 1 Gene Expression Is Accelerated by Inhibitors of Histone Deacetylases in Rabbit Skin Cells Infected with a Mutant Carrying a cDNA Copy of the Infected-Cell Protein No. 0
    American Society for Microbiology ; 2003
    In:  Journal of Virology Vol. 77, No. 23 ( 2003-12), p. 12671-12678
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 77, No. 23 ( 2003-12), p. 12671-12678
    Abstract: An earlier report showed that the expression of viral genes by a herpes simplex virus 1 mutant [HSV-1(vCPc0)] in which the wild-type, spliced gene encoding infected-cell protein no. 0 (ICP0) was replaced by a cDNA copy is dependent on both the cell type and multiplicity of infection. At low multiplicities of infection, viral gene expression in rabbit skin cells was delayed by many hours, although ultimately virus yield was comparable to that of the wild-type virus. This defect was rescued by replacement of the cDNA copy with the wild-type gene. To test the hypothesis that the delay reflected a dysfunction of ICP0 in altering the structure of host protein-viral DNA complexes, we examined the state of histone deacetylases (HDACs) (HDAC1, HDAC2, and HDAC3). We report the following. (i) HDAC1 and HDAC2, but not HDAC3, were modified in infected cells. The modification was mediated by the viral protein kinase U S 3 and occurred between 3 and 6 h after infection with wild-type virus but was delayed in rabbit skin cells infected with HSV-1(vCPc0) mutant, concordant with a delay in the expression of viral genes. (ii) Pretreatment of rabbit skin cells with inhibitors of HDAC activity (e.g., sodium butyrate, Helminthosporium carbonum toxin, or trichostatin A) accelerated the expression of HSV-1(vCPc0) but not that of wild-type virus. We conclude the following. (i) In the interval in which HSV-1(vCPc0) DNA is silent, its DNA is in chromatin-like structures amenable to modification by inhibitors of histone deacetylases. (ii) Expression of wild-type virus genes in these cells precluded the formation of DNA-protein structures that would be affected by either the HDACs or their inhibitors. (iii) Since the defect in HSV-1(vCPc0) maps to ICP0, the results suggest that this protein initiates the process of divestiture of viral DNA from tight chromatin structures but could be replaced by other viral proteins in cells infected with a large number of virions.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.77.23.12671-12678.2003
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2003
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  • 2
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    An Early Regulatory Function Required in a Cell Type-Dependent Manner Is Expressed by the Genomic but Not the cDNA Copy of the Herpes Simplex Virus 1 Gene Encoding Infected Cell Protein 0
    American Society for Microbiology ; 2002
    In:  Journal of Virology Vol. 76, No. 19 ( 2002-10), p. 9744-9755
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 76, No. 19 ( 2002-10), p. 9744-9755
    Abstract: The α0 genes of herpes simplex virus 1 (HSV-1) contain three exons. Earlier studies have shown that the substitution of genomic sequences with a cDNA copy does not alter the capacity of the virus to replicate or establish latent infection. Other studies have demonstrated that HSV-1 may express alternatively spliced forms of α0 transcripts. The studies reported here centered on a mutant HSV-1(vCPc0) strain in which the genomic copies of the α0 gene were replaced with cDNA copies. From our research, we report the following observations. (i) In contrast to events transpiring in cells infected with wild-type virus, the expression of HSV-1(vCPc0) genes was delayed or restricted to α genes for many hours in rabbit skin cells and to a lesser extent in HEp-2 cells but not in Vero cells. This delay in the expression of HSV-1(vCPc0) β or γ genes was also multiplicity of infection dependent. (ii) Exposure to MG132, a proteasomal inhibitor, before infection with wild-type virus had no significant effect on the accumulation of viral proteins in Vero cells and caused an only slight delay in viral gene expression in rabbit skin cells in a multiplicity of infection-dependent fashion. The drug had no effect when it was added to the medium 3 h after infection. (iii) Rabbit skin or HEp-2 cells exposed to MG132 3 h after infection with the HSV-1(vCPc0) mutant accumulated only α proteins. This restriction was cell type dependent but not multiplicity of infection dependent. (iv) Both the delay in the expression of β and γ genes and the effect of MG132 added to the medium 3 h after infection were rescued by restoration of the intron 1 sequences in the HSV-1(vCPc0) mutant. However, cells transduced by baculoviruses expressing intron 1 RNA did not complement the HSV-1(vCPc0) mutant, suggesting that the function of intron 1 is in cis rather than in trans . We came to the following conclusions as a result. (i) Post-α gene expression requires the involvement of the proteasomal pathway in a cell type-dependent manner. Consistent with this requirement, the proapoptotic functions of MG132 are blocked in cells infected before exposure to the drug but not after exposure. (ii) A function encoded by the α0 gene that is absent from the cDNA copy is required for viral gene expression in a cell type- and multiplicity of infection-dependent fashion. The absence of this master function delays but does not ultimately block viral gene expression in the cell lines tested here.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.76.19.9744-9755.2002
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2002
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  • 3
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    New pore protein produced in cells lysogenic for Escherichia coli phage HK253hrk
    Wiley ; 1987
    In:  European Journal of Biochemistry Vol. 164, No. 1 ( 1987-04), p. 141-145
    Details
    In: European Journal of Biochemistry, Wiley, Vol. 164, No. 1 ( 1987-04), p. 141-145
    Type of Medium: Online Resource
    ISSN: 0014-2956 , 1432-1033
    URL: Issue
    URL: Article
    DOI: 10.1111/ejb.1987.164.issue-1
    DOI: 10.1111/j.1432-1033.1987.tb11005.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1987
    detail.hit.zdb_id: 1398347-7
    detail.hit.zdb_id: 2172518-4
    SSG: 12
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  • 4
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    Lambdoid Coliphage HK139 Integrates Between his and supD
    American Society for Microbiology ; 1982
    In:  Journal of Virology Vol. 44, No. 2 ( 1982-11), p. 716-719
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 44, No. 2 ( 1982-11), p. 716-719
    Abstract: Phage HK139 is UV inducible and λ homoimmune and has the host range of φ80. It can recombine with λ as well as with φ80, and in the prophage form it is found integrated between the loci his and supD.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.44.2.716-719.1982
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1982
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  • 5
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    U S 3 and U S 3.5 Protein Kinases of Herpes Simplex Virus 1 Differ with Respect to Their Functions in Blocking Apoptosis and in Virion Maturation and Egress
    American Society for Microbiology ; 2006
    In:  Journal of Virology Vol. 80, No. 8 ( 2006-04-15), p. 3752-3764
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 80, No. 8 ( 2006-04-15), p. 3752-3764
    Abstract: Previously, we reported that the U S 3 protein kinase blocks apoptosis, that it activates protein kinase A (PKA), that activation of PKA blocks apoptosis in cells infected with a U S 3 deletion mutant, and that an overlapping transcriptional unit encodes a truncated kinase designated U S 3.5. Here, we report the properties of the kinases based on comparisons of herpes simplex virus and baculoviruses expressing U S 3 or U S 3.5 kinase. Specifically, we report the following. (i) Both kinases mediate the phosphorylation of HDAC1, HDAC2, and the PKA regulatory IIα subunit in the absence of other viral proteins. (ii) Both enzymes mediate the phosphorylation of largely identical sets of proteins carrying the phosphorylation consensus site of PKA, but only U S 3 blocks apoptosis, suggesting that it is U S 3 and not PKA that is responsible for the phosphorylation of the proteins bearing the shared consensus phosphorylation site and the antiapoptotic activity. (iii) Both kinases cofractionate with mitochondria. Immune depletion of the U S 3 and U S 3.5 kinases from the cytoplasm removed the kinases from the supernatant fraction, but not from the mitochondrial fraction, and therefore, if the antiapoptotic activity of the U S 3 kinase is expressed in mitochondria, the localization signal and the antiapoptotic functions are located on different parts of the protein. (iv) The U S 3 protein kinase is required for the translocation of virus particles from the nucleus. Although the U L 31 protein is phosphorylated in cells infected with the mutant expressing U S 3.5 kinase, the release of virus particles from nuclei was impeded in some cells, suggesting that the U S 3 kinase affects the modification of the nuclear membrane more efficiently than the U S 3.5 kinase.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.80.8.3752-3764.2006
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2006
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  • 6
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    Temperature-Sensitive Mutations in the Putative Herpes Simplex Virus Type 1 Terminase Subunits pU L 15 and pU L 33 Preclude Viral DNA Cleavage/Packaging and Interaction with pU L 28 at the Nonpermissive Temperature
    American Society for Microbiology ; 2008
    In:  Journal of Virology Vol. 82, No. 1 ( 2008-01), p. 487-494
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 82, No. 1 ( 2008-01), p. 487-494
    Abstract: Terminases comprise essential components of molecular motors required to package viral DNA into capsids in a variety of DNA virus systems. Previous studies indicated that the herpes simplex virus type 1 U L 15 protein (pU L 15) interacts with the pU L 28 moiety of a pU L 28-pU L 33 complex to form the likely viral terminase. In the current study, a novel temperature-sensitive mutant virus was shown to contain a mutation in U L 33 codon 61 predicted to change threonine to proline. At the nonpermissive temperature, this virus, designated ts8-22, replicated viral DNA and produced capsids that became enveloped at the inner nuclear membrane but failed to form plaques or to cleave or package viral DNA. Incubation at the nonpermissive temperature also precluded coimmunoprecipitation of U L 33 protein with its normal interaction partners encoded by U L 28 and U L 15 in ts8-22-infected cells and with pU L 28 in transient-expression assays. Moreover, a temperature-sensitive mutation in U L 15 precluded coimmunoprecipitation of pU L 15 with the U L 28 and U L 33 proteins at the nonpermissive temperature. We conclude that interactions between putative terminase components are tightly linked to successful viral DNA cleavage and packaging.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.01875-07
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2008
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  • 7
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    ICP0 and the U S 3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression
    Proceedings of the National Academy of Sciences ; 2006
    In:  Proceedings of the National Academy of Sciences Vol. 103, No. 26 ( 2006-06-27), p. 9993-9998
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 103, No. 26 ( 2006-06-27), p. 9993-9998
    Abstract: SK-N-SH cells exposed to low ratios of ICP0-null (ΔICP0) mutants of herpes simplex virus per cell express the viral α proteins, but the progression to β and γ gene expression does not ensue. In these restrictive cells, post-α gene expression can be induced after exposure of the infected cells to sodium butyrate, an indication that VP16 brought into cells by the virus and the α gene products made after infection cannot block the silencing of viral post-α genes by histone deacetylases (HDACs). This observation is consistent with evidence reported earlier that ICP0 dissociates HDAC1/2 from the CoREST/REST complex. In permissive U2OS cells, replication is independent of the ratio of ΔICP0 mutant per cell. To determine whether other viral genes are involved in blocking HDACs, we used a surrogate system consisting of baculoviruses carrying viral or cellular genes driven by CMV immediate–early promoter. Expression of these genes requires blocking of histone deacetylation. We report that ( i ) cotransduced U S 3 or U S 3.5 protein kinase substitutes for sodium butyrate in enabling the expression of a reporter gene in restrictive cells and enhancing it in permissive cells; ( ii ) HDAC1 is phosphorylated concomitant with the expression of reporter genes; and ( iii ) the amounts and appearance of HDAC1 are altered in transduced cells expressing U S 3 protein kinase in the absence of other viral proteins. We conclude that the U S 3 protein kinase blocks histone deacetylation by a mechanism distinct from that of ICP0 and that debilitated histone deacetylation contributes to the permissiveness of U2OS cells for ΔICP0 mutants.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.0604142103
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2006
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 8
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    Mapping of Key Functions of the Herpes Simplex Virus 1 U S 3 Protein Kinase: the U S 3 Protein Can Form Functional Heteromultimeric Structures Derived from Overlapping Truncated Polypeptides
    American Society for Microbiology ; 2007
    In:  Journal of Virology Vol. 81, No. 4 ( 2007-02-15), p. 1980-1989
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 81, No. 4 ( 2007-02-15), p. 1980-1989
    Abstract: Earlier studies have shown that the herpes simplex virus (HSV) U S 3 encodes two transcriptional units directing the synthesis of the U S 3 (residues 1 to 481) and U S 3.5 (residues 77 to 481) protein kinases. Both kinases phosphorylate histone deacetylase 1 (HDAC1) and HDAC2 and enable the expression of genes cotransduced into U2OS cells by recombinant baculoviruses, an activity designated the “helper function.” The two kinases differ with respect to antiapoptotic activity. In the studies reported here, we made a series of FLAG-tagged amino- and carboxyl-terminal truncations of U S 3 and these were tested for antiapoptotic activity, phosphorylation of HDAC1, and the helper function. We report the following. (i) HDAC1 phosphorylation and the helper function were expressed in cells transduced by the truncation encoding residues 182 to 481 but not in cells transduced by the truncation encoding residues 189 to 481 or the amino-terminal polypeptides encompassing the first 188 amino acids. (ii) The self-posttranslational modification requires residues 164 to 481. (iii) The antiapoptotic activity requires both the amino-terminal and the carboxyl-terminal domains, of which the truncated protein containing residues 1 to 163 and that containing residues 164 to 481, respectively, were the smallest fragments tested to be effective. The two domains need not be on the same molecule, but they must overlap. The smallest overlapping pair tested was the fragment containing residues 1 to 181 and that containing residues 164 to 481. Consistent with the hypothesis that the effective overlapping truncations form a heteromultimeric structure, antibody to FLAG coprecipitated untagged U S 3 from lysates of cells cotransduced with FLAG-tagged, truncated U S 3 constructs. Although U S 3 has been reported to be a monomeric enzyme, the results indicate that it can form enzymatically active multimeric structures.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.02265-06
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2007
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  • 9
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    The Carboxyl-Terminal Domain of RNA Polymerase II Is Phosphorylated by a Complex Containing cdk9 and Infected-Cell Protein 22 of Herpes Simplex Virus 1
    American Society for Microbiology ; 2005
    In:  Journal of Virology Vol. 79, No. 11 ( 2005-06), p. 6757-6762
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 79, No. 11 ( 2005-06), p. 6757-6762
    Abstract: The infected-cell protein 22 (ICP22), a regulatory protein encoded by the α22 gene of herpes simplex virus 1, is required for the optimal expression of a set of late viral proteins that includes the products of the U S 11, U L 38, and U L 41 genes. ICP22 has two activities. Thus, ICP22 and the U L 13 protein kinase mediate the activation of cdc2 and degradation of its partners, cyclins A and B. cdc2 and its new partner, the DNA polymerase accessory factor (U L 42), bind topoisomerase IIα in an ICP22-dependent manner. In addition, ICP22 and U L 13 mediate an intermediate phosphorylation of the carboxyl terminus of RNA polymerase II (RNA POL II). Here we report another function of ICP22. Thus, ICP22 physically interacts with cdk9, a constitutively active cyclin-dependent kinase involved in transcriptional regulation. A protein complex containing ICP22 and cdk9 phosphorylates in vitro the carboxyl-terminal domain of RNA POL II in a viral U S 3 protein kinase-dependent fashion. Finally, the carboxyl-terminal domain of RNA POL II fused to glutathione S -transferase is phosphorylated in reaction mixtures containing complexes pulled down with ICP22 or cdk9 immune precipitated from lysates of wild-type parent virus or ΔU L 13 but not ΔU S 3 mutant-infected cells. The experiments described here place ICP22 and cdk9 in a complex with the carboxyl-terminal domain of RNA POL II. At the same time we confirm the requirement of ICP22 and the U L 13 protein kinase in the posttranslational modification of RNA POL II that alters its electrophoretic mobility, although U S 3 kinase appears to play a role in a cell-type-dependent fashion.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.79.11.6757-6762.2005
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2005
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  • 10
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    U S 3 Protein Kinase of Herpes Simplex Virus 1 Blocks Caspase 3 Activation Induced by the Products of U S 1.5 and U L 13 Genes and Modulates Expression of Transduced U S 1.5 Open Reading Frame in a Cell Type-Specific Manner
    American Society for Microbiology ; 2002
    In:  Journal of Virology Vol. 76, No. 2 ( 2002-01-15), p. 743-754
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 76, No. 2 ( 2002-01-15), p. 743-754
    Abstract: The coding domain of the herpes simplex virus type 1 (HSV-1) α22 gene encodes two proteins, the 420-amino-acid infected-cell protein 22 (ICP22) and U S 1.5, a protein colinear with the carboxyl-terminal domain of ICP22. In HSV-1-infected cells, ICP22 and U S 1.5 are extensively modified by the U L 13 and U S 3 viral protein kinases. In this report, we show that in contrast to other viral proteins defined by their properties as α proteins, U S 1.5 becomes detectable and accumulated only at late times after infection. Moreover, significantly more U S 1.5 protein accumulated in cells infected with a mutant lacking the U L 13 gene than in cells infected with wild-type virus. To define the role of viral protein kinases on the accumulation of U S 1.5 protein, rabbit skin cells or Vero cells were exposed to recombinant baculoviruses that expressed U S 1.5, U L 13, or U S 3 proteins under a human cytomegalovirus immediate-early promoter. The results were as follows. (i) Accumulation of the U S 1.5 protein was reduced by concurrent expression of the U L 13 protein kinase and augmented by concurrent expression of the U S 3 protein kinase. The magnitude of the reduction or increase in the accumulation of the U S 1.5 protein was cell type dependent. The effect of U L 13 kinase appears to be specific inasmuch as it did not affect the accumulation of glycoprotein D in cells doubly infected by recombinant baculoviruses expressing these genes. (ii) The reduction in accumulation of the U S 1.5 protein was partially due to proteasome-dependent degradation. (iii) Both U S 1.5 and U L 13 proteins activated caspase 3, indicative of programmed cell death. (iv) Concurrent expression of the U S 3 protein kinase blocked activation of caspase 3. The results are concordant with those published elsewhere (J. Munger and B. Roizman, Proc. Natl. Acad. Sci. USA 98:10410–10415, 2001) that the U S 3 protein kinase can block apoptosis by degradation or posttranslational modification of BAD.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.76.2.743-754.2002
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2002
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