Repression of β-actin synthesis and persistence of ribosomal protein synthesis after infection of HeLa cells by herpes simplex virus type 1 infection are under translational control

1997 ◽  
Vol 256 (3) ◽  
pp. 320-327 ◽  
Author(s):  
A. Greco ◽  
A.-M. Laurent ◽  
J.-J. Madjar
Keyword(s):  
Protein Synthesis ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Ribosomal Protein ◽  
Hela Cells ◽  
Herpes Simplex Virus Type ◽  
Translational Control ◽  
Ribosomal Protein Synthesis ◽  
Simplex Virus

Scopadulciol is an Inhibitor of Herpes Simplex Virus Type 1 and a Potentiator of Aciclovir

1996 ◽  
Vol 7 (2) ◽  
pp. 79-85 ◽  
Author(s):  
Kyoko Hayashi ◽  
Toshimitsu Hayashi
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Antiviral Activity ◽  
Virus Type ◽  
Hela Cells ◽  
Herpes Simplex Virus Type ◽  
Infected Cells ◽  
Simplex Virus ◽  
Hsv 1

The antiviral activity of scopadulciol (SDC), a tetracyclic diterpenoid with a chemical structure related to that of aphidicolin, isolated from Scoparia dulcis, was studied in vitro against herpes simplex virus type 1 (HSV-1). SDC was found to inhibit the virus replication as shown by reduction of virus production. The action was not due to the inhibition of viral DNA polymerase activity and virus penetration, but might involve, at least in part, a virucidal effect. SDC did not suppress the viral protein synthesis of infected cells when added at an early stage of HSV-1 replication, but did when added later. When aciclovir (ACV) and SDC were evaluated in combination for antiviral activity against HSV-1 replication and cytotoxicity, these drugs inhibited viral replication in HeLa cells synergistically, but the same combination did not produce synergistic cytotoxicity in HeLa cells. Studies of the deoxynucleotide pool sizes revealed that SDC increased the intracellular dNTP pools and ACV triphosphate level significantly in infected cells when the cells were treated with the combination. These results could account for the synergistic action between SDC and ACV.

Phosphorylation of ribosomal protein L30 after herpes simplex virus type 1 infection

1995 ◽  
Vol 16 (1) ◽  
pp. 854-859 ◽  
Author(s):  
Denis Simonin ◽  
Jean-Jacques Diaz ◽  
Karine Kindbeiter ◽  
Luc Denoroy ◽  
Jean-Jacques Madjar
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Ribosomal Protein ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Simplex Virus

scholarly journals NF-κB Is Required for Apoptosis Prevention during Herpes Simplex Virus Type 1 Infection

2003 ◽  
Vol 77 (13) ◽  
pp. 7261-7280 ◽  
Author(s):  
Margot L. Goodkin ◽  
Adrian T. Ting ◽  
John A. Blaho
Keyword(s):  
Protein Synthesis ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Infected Cell ◽  
Herpes Simplex Virus Type ◽  
Wild Type ◽  
Tnf Α ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT Wild-type herpes simplex virus type 1 (HSV-1) infection triggers apoptosis in human cells. The subsequent synthesis of infected cell proteins between 3 and 6 h postinfection (hpi) acts to block this process from killing the cells. The factors produced during this window also prevent cell death induced by environmental staurosporine or sorbitol (M. Aubert, J. O'Toole, and J. A. Blaho, J. Virol. 73:10359-10370, 1999). We now report that (i) during the prevention window, HSV-1(F) also inhibited apoptosis induced by tumor necrosis factor alpha (TNF-α) plus cycloheximide (CHX) treatment. While deciphering the mechanism of this inhibition, we observed that (ii) the transcription factor NF-κB translocated from the cytoplasm into the nuclei of infected cells, and (iii) this migration initiated at 3 hpi. (iv) The complete inhibition of protein synthesis at 3 hpi by the addition of CHX precluded NF-κB translocation, while CHX additions at 6 hpi or later did not elicit this effect. This result confirms that infected cell protein synthesis is required for the nuclear import of NF-κB. (v) The detection of NF-κB in nuclei correlated with the ability of HSV-1(F), HSV-1(KOS1.1), or HSV-1(R7032), a replication-competent recombinant virus containing a deletion in the gene encoding the gE glycoprotein, to prevent apoptosis. (vi) NF-κB did not bind its κB DNA recognition site and remained cytoplasmic in cells actively undergoing apoptosis following infection with HSV-1(vBSΔ27), a virus with the key regulatory protein ICP27 deleted. (vii) Prestimulation of NF-κB by the addition of a phorbol ester prevented HSV-1(vBSΔ27)-induced apoptosis. (viii) Retention of NF-κB in the cytoplasm by the addition of a pharmacological antagonist of its release from IκBα led to an increase in death factor processing during HSV-1(F) infection. (ix) A novel HEp-2 clonal cell line, termed IκBαDN, was generated which expresses a dominant-negative form of IκBα. Treatment of IκBαDN cells with TNF-α in the absence of CHX resulted in apoptotic death due to the inability of NF-κB to become activated in these cells. Finally, (x) infection of IκBαDN cells with HSV-1(F) or HSV-1(KOS1.1) resulted in apoptosis, demonstrating that (xi) the nuclear translocation of NF-κB between 3 and 6 hpi (the prevention window) is necessary to prevent apoptosis in wild-type HSV-1-infected human HEp-2 cells.

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