scholarly journals Aberrant intracellular localization of Varicella-Zoster virus regulatory proteins during latency

1998 ◽  
Vol 95 (12) ◽  
pp. 7080-7085 ◽  
Author(s):  
O. Lungu ◽  
C. A. Panagiotidis ◽  
P. W. Annunziato ◽  
A. A. Gershon ◽  
S. J. Silverstein
Keyword(s):  
Varicella Zoster Virus ◽  
Intracellular Localization ◽  
Regulatory Proteins ◽  
Varicella Zoster

Transcriptional mapping of varicella-zoster virus regulatory proteins

Neurology ◽  
1995 ◽  
Vol 45 (Issue 12, Supplement 8) ◽  
pp. S33-S35 ◽  
Author(s):  
P. R. Kinchington ◽  
J.-P. M. Vergnes ◽  
S. E. Turse
Keyword(s):  
Varicella Zoster Virus ◽  
Regulatory Proteins ◽  
Varicella Zoster ◽  
Transcriptional Mapping

scholarly journals BAG3, a Host Cochaperone, Facilitates Varicella-Zoster Virus Replication

2007 ◽  
Vol 81 (14) ◽  
pp. 7491-7503 ◽  
Author(s):  
Christos A. Kyratsous ◽  
Saul J. Silverstein
Keyword(s):  
Varicella Zoster Virus ◽  
Virus Replication ◽  
Latent Infection ◽  
Dna Binding Protein ◽  
Lytic Replication ◽  
Regulatory Proteins ◽  
Varicella Zoster ◽  
Associated Proteins ◽  
Hsp90 Activity ◽  
Interfering Rna

ABSTRACT Varicella-zoster virus (VZV) establishes a lifelong latent infection in the dorsal root ganglia of the host. During latency, a subset of virus-encoded regulatory proteins is detected; however, they are excluded from the nucleus. ORF29p, a single-stranded DNA binding protein, is one of these latency-associated proteins. We searched for cell proteins that interact with ORF29p and identified BAG3. BAG3, Hsp70/Hsc70, and Hsp90 colocalize with ORF29p in nuclear transcription/replication factories during lytic replication of VZV. Pharmacological intercession of Hsp90 activity with ansamycin antibiotics or depletion of BAG3 by small interfering RNA results in inhibition of virus replication. Replication in BAG3-depleted cell lines is restored by complementation with exogenous BAG3. Alteration of host chaperone activity provides a novel means of regulating virus replication.

scholarly journals Varicella-Zoster Virus ORF47 Protein Serine Kinase: Characterization of a Cloned, Biologically Active Phosphotransferase and Two Viral Substrates, ORF62 and ORF63

2001 ◽  
Vol 75 (18) ◽  
pp. 8854-8858 ◽  
Author(s):  
T. K. Kenyon ◽  
J. Lynch ◽  
J. Hay ◽  
W. Ruyechan ◽  
C. Grose
Keyword(s):  
Varicella Zoster Virus ◽  
Kinase Activity ◽  
Biologically Active ◽  
Regulatory Proteins ◽  
Kinase Assay ◽  
Serine Kinase ◽  
Varicella Zoster ◽  
Simplex Virus

ABSTRACT Varicella-zoster virus (VZV) codes for a protein serine kinase called ORF47; the herpes simplex virus (HSV) homolog is UL13. No recombinant alphaherpesvirus serine kinase has been biologically active in vitro. We discovered that preservation of the intrinsic kinase activity of recombinant VZV ORF47 required unusually stringent in vitro conditions, including physiological concentrations of polyamines. In this assay, ORF47 phosphorylated two VZV regulatory proteins: the ORF62 protein (homolog of HSV ICP4) and the ORF63 protein (homolog of HSV ICP22). Of interest, ORF47 kinase also coprecipitated ORF63 protein from the kinase assay supernatant.

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