scholarly journals Inhibiting effect of (RS)-9-[4-hydroxy-2-(hydroxymethyl)butyl]guanine on varicella-zoster virus replication in cell culture.

1987 ◽  
Vol 31 (1) ◽  
pp. 76-80 ◽  
Author(s):  
G Abele ◽  
A Karlstrom ◽  
J Harmenberg ◽  
S Shigeta ◽  
A Larsson ◽  
...  
Keyword(s):  
Cell Culture ◽  
Varicella Zoster Virus ◽  
Virus Replication ◽  
Varicella Zoster ◽  
Inhibiting Effect

scholarly journals Inhibition of varicella-zoster virus replication by an inhibitor of protein myristoylation

1993 ◽  
Vol 74 (6) ◽  
pp. 1181-1184 ◽  
Author(s):  
D. R. Harper ◽  
R. L. Gilbert ◽  
C. Blunt ◽  
R. A. J. McIlhinney
Keyword(s):  
Varicella Zoster Virus ◽  
Virus Replication ◽  
Varicella Zoster ◽  
Protein Myristoylation

Resveratrol inhibition of varicella-zoster virus replication in vitro

2006 ◽  
Vol 72 (3) ◽  
pp. 171-177 ◽  
Author(s):  
John J. Docherty ◽  
Thomas J. Sweet ◽  
Erin Bailey ◽  
Seth A. Faith ◽  
Tristan Booth
Keyword(s):  
Varicella Zoster Virus ◽  
Virus Replication ◽  
Varicella Zoster

Honeysuckle-derived microRNA2911 directly inhibits varicella-zoster virus replication by targeting IE62 gene

2019 ◽  
Vol 25 (4) ◽  
pp. 457-463 ◽  
Author(s):  
Ying Huang ◽  
Huabo Liu ◽  
Xinlei Sun ◽  
Meng Ding ◽  
Gaojian Tao ◽  
...  
Keyword(s):  
Varicella Zoster Virus ◽  
Virus Replication ◽  
Varicella Zoster

scholarly journals Components of Nuclear Domain 10 Bodies Regulate Varicella-Zoster Virus Replication

2009 ◽  
Vol 83 (9) ◽  
pp. 4262-4274 ◽  
Author(s):  
Christos A. Kyratsous ◽  
Saul J. Silverstein
Keyword(s):  
Varicella Zoster Virus ◽  
Virus Replication ◽  
Control Cell ◽  
Host Cells ◽  
Virus Protein ◽  
Protein Accumulation ◽  
Dna Virus ◽  
Varicella Zoster ◽  
Early Protein ◽  
Nuclear Domains

ABSTRACT PML, Sp100, and Daxx are proteins that normally reside within nuclear domains 10 (ND10s). They associate with DNA virus genomes and repress the very early stages of the DNA virus replication cycle. Virus-encoded proteins counteract this innate antiviral response. ICP0, a herpes simplex virus (HSV) immediate-early protein, is necessary and sufficient to dissociate ND10s and target their two major components, PML and Sp100, for proteasomal degradation. In this report, we show that ORF61p, the varicella-zoster virus (VZV) ortholog of ICP0, does not degrade PML and alters Sp100 levels only slightly. Furthermore, we demonstrate that other virus proteins cannot substitute for this lack of function during infection. By using short interfering RNAs, we depleted PML, Sp100, and Daxx and studied their roles in plaquing efficiency, virus protein accumulation, infectious-center titer, and virus spread. The results of these studies show that components of ND10s can accelerate VZV replication but do not ultimately control cell-associated virus titers. We conclude that while both ICP0 and ORF61p activate virus gene expression, they modulate host innate repression mechanisms in two different ways. As a result, HSV and VZV commandeer their host cells by distinct mechanisms to ensure their replication and spread.

Genotyping of varicella-zoster virus strains after serial passages in cell culture

2007 ◽  
Vol 145 (1) ◽  
pp. 80-83 ◽  
Author(s):  
Andreas Sauerbrei ◽  
Anja Philipps ◽  
Roland Zell ◽  
Peter Wutzler
Keyword(s):  
Cell Culture ◽  
Varicella Zoster Virus ◽  
Varicella Zoster ◽  
Virus Strains
Sign in / Sign up

Export Citation Format

Share Document