Differences in resistance to herpes simplex virus type 1 (HSV-1) among oligodendroglia derived from different strains of mice are determined after viral adsorption but prior to the expression of immediate early (IE) genes

1997 ◽  
Vol 3 (3) ◽  
pp. 197-205 ◽  
Author(s):  
Eva E. Thomas ◽  
Allen S. Lau ◽  
Brenda Morrison ◽  
Seung U. Kim ◽  
Lome F. Kastrukoff
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Immediate Early ◽  
Different Strains ◽  
Simplex Virus ◽  
Viral Adsorption ◽  
Hsv 1

scholarly journals Recruitment of the Transcriptional Coactivator HCF-1 to Viral Immediate-Early Promoters during Initiation of Reactivation from Latency of Herpes Simplex Virus Type 1

2009 ◽  
Vol 83 (18) ◽  
pp. 9591-9595 ◽  
Author(s):  
Zackary W. Whitlow ◽  
Thomas M. Kristie
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Rna Polymerase Ii ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Immediate Early ◽  
Transcriptional Coactivator ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT The transcriptional coactivator host cell factor 1 (HCF-1) is critical for the expression of immediate-early (IE) genes of the alphaherpesviruses herpes simplex virus type 1 (HSV-1) and varicella-zoster virus. HCF-1 may also be involved in the reactivation of these viruses from latency as it is sequestered in the cytoplasm of sensory neurons but is rapidly relocalized to the nucleus upon stimulation that results in reactivation. Here, chromatin immunoprecipitation assays demonstrate that HCF-1 is recruited to IE promoters of viral genomes during the initiation of reactivation, correlating with RNA polymerase II occupancy and IE expression. The data support the model whereby HCF-1 plays a pivotal role in the reactivation of HSV-1 from latency.

scholarly journals Herpes Simplex Virus Type 1 Immediate-Early Gene Expression Is Required for the Induction of Apoptosis in Human Epithelial HEp-2 Cells

2004 ◽  
Vol 78 (1) ◽  
pp. 224-239 ◽  
Author(s):  
Christine M. Sanfilippo ◽  
Fungai N. W. Chirimuuta ◽  
John A. Blaho
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Early Gene ◽  
Immediate Early ◽  
Induction Of Apoptosis ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT Wild-type herpes simplex virus type 1 (HSV-1) induces apoptosis in human epithelial HEp-2 cells, but infected cell proteins produced later in infection block the process from killing the cells. Thus, HSV-1 infection in the presence of the translational inhibitor cycloheximide (CHX) results in apoptosis. Our specific goal was to gain insight as to the viral feature(s) responsible for triggering apoptosis during HSV-1 infection. We now report the following. (i) No viral protein synthesis or death factor processing was detected after infection with HSV-1(HFEMtsB7) at 39.5°C; this mutant virus does not inject its virion DNA into the nucleus at this nonpermissive temperature. (ii) No death factor processing or apoptotic morphological changes were detected following infection with UV-irradiated, replication-defective viruses possessing transcriptionally active incoming VP16. (iii) Addition of the transcriptional inhibitor actinomycin D prevented death factor processing upon infection with the apoptotic, ICP27-deletion virus HSV-1(vBSΔ27). (iv) Apoptotic morphologies and death factor processing were not observed following infection with HSV-1(d109), a green fluorescent protein-expressing recombinant virus possessing deletions of all five immediate-early (IE) (or α) genes. (v) Finally, complete death factor processing was observed upon infection with the VP16 transactivation domain-mutant HSV-1(V422) in the presence of CHX. Based on these findings, we conclude that (vi) the expression of HSV-1 α/IE genes is required for the viral induction of apoptosis and (vii) the transactivation activity of VP16 is not necessary for this induction.

scholarly journals Differential Functions of Interferon-Upregulated Sp100 Isoforms: Herpes Simplex Virus Type 1 Promoter-Based Immediate-Early Gene Suppression and PML Protection from ICP0-Mediated Degradation

2009 ◽  
Vol 83 (10) ◽  
pp. 5168-5180 ◽  
Author(s):  
Dmitri G. Negorev ◽  
Olga V. Vladimirova ◽  
Gerd G. Maul
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Infection ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Immediate Early ◽  
Sand Domain ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT Cells have intrinsic defenses against virus infection, acting before the innate or the adaptive immune response. Preexisting antiviral proteins such as PML, Daxx, and Sp100 are stored in specific nuclear domains (ND10). In herpes simplex virus type 1 (HSV-1), the immediate-early protein ICP0 serves as a counterdefense through degradation of the detrimental protein PML. We asked whether interferon (IFN)-upregulated Sp100 is similarly antagonized by ICP0 in normal human fibroblasts by using a selective-knockdown approach. We find that of the four Sp100 isoforms, the three containing a SAND domain block the transcription of HSV-1 proteins ICP0 and ICP4 at the promoter level and that IFN changes the differential splicing of the Sp100 transcript in favor of the inhibitor Sp100C. At the protein level, ICP0 activity does not lead to the hydrolysis of any of the Sp100 isoforms. The SAND domain-containing isoforms are not general inhibitors of viral promoters, as the activity of the major immediate-early cytomegalovirus promoter is not diminished, whereas the long terminal repeat of a retrovirus, like the ICP0 promoter, is strongly inhibited. Since we could not find a specific promoter region in the ICP0 gene that responds to the SAND domain-containing isoforms, we questioned whether Sp100 could act through other antiviral proteins such as PML. We find that all four Sp100 isoforms stabilize ND10 and protect PML from ICP0-based hydrolysis. Loss of either all PML isoforms or all Sp100 isoforms reduces the opposite constituent ND10 protein, suggesting that various interdependent mechanisms of ND10-based proteins inhibit virus infection at the immediate-early level.

Cross-reactivity of the anti-PML antibody PG-M3 with the herpes simplex virus type 1 immediate early protein ICP4

Microbiology ◽  
2000 ◽  
Vol 81 (7) ◽  
pp. 1773-1777 ◽  
Author(s):  
Stefanie L. Boulware ◽  
Peter C. Weber
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Cross Reactivity ◽  
Immediate Early ◽  
Early Protein ◽  
Simplex Virus ◽  
Hsv 1

The PML protein is one of the components of ND10, nuclear matrix-associated structures which undergo rapid disintegration at the onset of herpes simplex virus type 1 (HSV-1) infection. This disruption event has been frequently visualized in immunofluorescence assays using the anti-PML mouse monoclonal antibody PG-M3. This antibody was surprisingly found to also stain nuclear virus replication compartments when employed at higher concentrations. This was shown to be due to an unexpected cross-reactivity of the PG-M3 antibody with the HSV-1 immediate early protein ICP4, a known component of replication compartments. The sequences of ICP4 recognized by PG-M3 were found to map to the extreme amino-terminal end of the protein, which includes a 21 amino acid segment that is partially homologous to the peptide of PML that was used to make PG-M3. These results suggest that PG-M3 may no longer represent an appropriate antibody for use in visualizing the fate of PML and ND10 during HSV-1 infection.

scholarly journals Transactivation of Herpes Simplex Virus Type 1 Immediate-Early Gene Expression by Virion-Associated Factors Is Blocked by an Inhibitor of Cyclin-Dependent Protein Kinases

1999 ◽  
Vol 73 (10) ◽  
pp. 8843-8847 ◽  
Author(s):  
Robert Jordan ◽  
Luis Schang ◽  
Priscilla A. Schaffer
Keyword(s):  
Gene Expression ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Immediate Early ◽  
Dependent Protein ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT Initiation of productive infection by human herpes simplex virus type 1 (HSV-1) requires cell cycle-dependent protein kinase (cdk) activity. Treatment of cells with inhibitors of cdks blocks HSV-1 replication and prevents accumulation of viral transcripts, including immediate-early (IE) transcripts (26). Inhibition of IE transcript accumulation suggests that virion proteins, such as VP16, require functional cdks to activate viral transcription. In this report, we show that a cdk inhibitor, Roscovitine, blocks VP16-dependent IE gene expression. In the presence of Roscovitine, the level of virion-induced activation of a transfected reporter gene (the gene encoding chloramphenicol acetyltransferase) linked to the promoter-regulatory region of the ICP0 gene was reduced 40-fold relative to that of untreated samples. Roscovitine had little effect on the interaction of VP16 with VP16-responsive DNA sequences as measured by electrophoretic mobility shift assays. These data indicate that VP16-dependent activation of IE gene expression requires functional cdks and that this requirement is independent of the ability of VP16 to bind to DNA.

scholarly journals The UL14 Tegument Protein of Herpes Simplex Virus Type 1 Is Required for Efficient Nuclear Transport of the Alpha Transinducing Factor VP16 and Viral Capsids

2007 ◽  
Vol 82 (3) ◽  
pp. 1094-1106 ◽  
Author(s):  
Yohei Yamauchi ◽  
Kazuya Kiriyama ◽  
Naomi Kubota ◽  
Hiroshi Kimura ◽  
Jiro Usukura ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Immediate Early ◽  
Nuclear Accumulation ◽  
Tegument Protein ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT The protein encoded by the UL14 gene of herpes simplex virus type 1 (HSV-1) and HSV-2 is expressed late in infection and is a minor component of the virion tegument. An UL14-deficient HSV-1 mutant (UL14D) forms small plaques and exhibits an extended growth cycle at low multiplicities of infection (MOI) compared to wild-type virus. Although UL14 is likely to be involved in the process of viral maturation and egress, its precise role in viral replication is still enigmatic. In this study, we found that immediate-early viral mRNA expression was decreased in UL14D-infected cells. Transient coexpression of UL14 and VP16 in the absence of infection stimulated the nuclear accumulation of both proteins. We intended to visualize the fate of VP16 released from the infected virion and constructed UL14-null (14D-VP16G) and rescued (14R-VP16G) viruses that expressed a VP16-green fluorescent protein (GFP) fusion protein. Synchronous high-multiplicity infection of the viruses was performed at 4°C in the absence of de novo protein synthesis. We found that the presence of UL14 in the virion had an enhancing effect on the nuclear accumulation of VP16-GFP. The lack of UL14 did not significantly alter virus internalization but affected incoming capsid transport to the nuclear pore. These observations suggested that UL14 (i) enhanced VP16 nuclear localization at the immediately early phase, thus indirectly regulating the expression of immediate-early genes, and (ii) was associated with efficient nuclear targeting of capsids. The tegument protein UL14 could be part of the machinery that regulates HSV-1 replication.

scholarly journals Long-Term Transgene Expression in Mice Infected with a Herpes Simplex Virus Type 1 Mutant Severely Impaired for Immediate-Early Gene Expression

2000 ◽  
Vol 74 (2) ◽  
pp. 956-964 ◽  
Author(s):  
Ker R. Marshall ◽  
Robin H. Lachmann ◽  
Stacey Efstathiou ◽  
Angela Rinaldi ◽  
Chris M. Preston
Keyword(s):  
Gene Expression ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Immediate Early ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT The role of viral immediate-early (IE) gene expression in herpes simplex virus type 1 (HSV-1) latency was investigated. The HSV-1 multiple mutant in1312, defective for the expression of the virion transactivator VP16 and the IE proteins ICP0 and ICP4, was used as the parent for these studies. The coding sequences of theEscherichia coli lacZ gene, preceded by the encephalomyocarditis virus internal ribosome entry site, were inserted into the region of in1312 that encodes the latency-associated transcripts (LATs) such that transcription of the transgene was controlled by the LAT promoter. This insert has previously been shown to direct long-term latent-phase expression of β-galactosidase in a wild-type HSV-1 genome (R. H. Lachmann and S. Efstathiou, J. Virol. 71, 3197–3207, 1997). The resulting recombinant, in1388, was apathogenic after inoculation into mice via the footpad and did not detectably replicate in dorsal root ganglia (DRG) or footpads. Mutant in1388 established latency in DRG, and β-galactosidase was expressed in increasing numbers of neurons over the first 25 days of infection. During latency, more than 1% of neurons in ganglia that innervate the footpad expressed β-galactosidase, with the number of positive cells remaining constant for at least 5 months. Rescue of the VP16, ICP0, or ICP4 mutations of in1388 did not affect the number of β-galactosidase-expressing neurons detected during latency. The results demonstrate that HSV-1 mutants severely impaired for IE gene expression are capable of establishing latency and efficiently expressing a foreign gene product under control of the LAT promoter.

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