Herpes Simplex Virus-Induced Expression of 70 kDa Heat Shock Protein (HSP70) Requires Early Protein Synthesis But Not Viral DNA Replication

1994 ◽  
Vol 38 (4) ◽  
pp. 321-325 ◽  
Author(s):  
Kappei Kobayashi ◽  
Eriko Ohgitani ◽  
Yasuyuki Tanaka ◽  
Masakazu Kita ◽  
Jiro Imanishi
Keyword(s):  
Protein Synthesis ◽  
Herpes Simplex Virus ◽  
Dna Replication ◽  
Herpes Simplex ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Viral Dna ◽  
Viral Dna Replication ◽  
Early Protein ◽  
Simplex Virus

scholarly journals Pocket Protein p130/Rb2 Is Required for Efficient Herpes Simplex Virus Type 1 Gene Expression and Viral Replication

2001 ◽  
Vol 75 (15) ◽  
pp. 7149-7160 ◽  
Author(s):  
Ginger L. Ehmann ◽  
Heather A. Burnett ◽  
Steven L. Bachenheimer
Keyword(s):  
Cell Cycle ◽  
Herpes Simplex Virus ◽  
Dna Replication ◽  
Herpes Simplex ◽  
Progeny Virus ◽  
Viral Dna ◽  
Viral Dna Replication ◽  
Pocket Protein ◽  
Simplex Virus

ABSTRACT We have reported previously that herpes simplex virus type 1 (HSV-1) infection disrupts normal progression of the mammalian cell cycle, causing cells to enter a G1-like state. Infected cells were characterized by a decline in cyclin-dependent kinase 2 (CDK2) activities, loss of hyperphosphorylated retinoblastoma protein (pRb), accumulation of E2F-pocket protein complexes, and failure to initiate cellular DNA replication. In the present study, we investigated the role of the pocket proteins pRb, p107, and p130 in HSV-1-dependent cell cycle inhibition and cyclin kinase regulation by infecting murine 3T3 cells derived from wild-type (WT) mouse embryos or embryos with deletions of pRb (pRb−/−), p107 (p107−/−), p130 (p130−/−), or both p130 and p107 (p130−/−/p107−/−). With respect to CDK2 inhibition, viral protein accumulation, viral DNA replication, and progeny virus yield, WT, pRb−/−, and p107−/− cells were essentially identical. In contrast, after infection of p130−/− cells, we observed no inhibition of CDK2 activity, a 5- to 6-h delay in accumulation of viral proteins, an impaired ability to form viral DNA replication compartments, and reduced viral DNA synthesis. As a result, progeny virus yield was reduced 2 logs compared to that in WT cells. Notably, p130−/−/p107−/− double-knockout cells had a virus replication phenotype intermediate between those of the p107−/− and p130−/− cells. We conclude from these studies that p130 is a key factor in regulating aspects of cell cycle progression, as well as the timely expression of viral genes and replication of viral DNA.

scholarly journals Conformational Changes in the Herpes Simplex Virus ICP8 DNA-Binding Protein Coincident with Assembly in Viral Replication Structures

2003 ◽  
Vol 77 (13) ◽  
pp. 7467-7476 ◽  
Author(s):  
Susan L. Uprichard ◽  
David M. Knipe
Keyword(s):  
Herpes Simplex Virus ◽  
Dna Replication ◽  
Herpes Simplex ◽  
Dna Binding ◽  
Conformational Changes ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Viral Dna ◽  
Viral Dna Replication ◽  
Simplex Virus

ABSTRACT The herpes simplex virus (HSV) single-stranded DNA-binding protein, ICP8, is required for viral DNA synthesis. Before viral DNA replication, ICP8 colocalizes with other replication proteins at small punctate foci called prereplicative sites. With the onset of viral genome amplification, these proteins become redistributed into large globular replication compartments. Here we present the results of immunocytochemical and biochemical analysis of ICP8 showing that various antibodies recognize distinct forms of ICP8. Using these ICP8-specific antibodies as probes for ICP8 structure, we detected a time-dependent appearance and disappearance of ICP8 epitopes in immunoprecipitation assays. Immunofluorescence staining of ICP8 in cells infected with different HSV mutant viruses as well as cells transfected with a limited number of viral genes demonstrated that these and other antigenic changes occur coincident with ICP8 assembly at intranuclear replication structures. Genetic analysis has revealed a correlation between the ability of various ICP8 mutant proteins to form the 39S epitope and their ability to bind to DNA. These results support the hypothesis that ICP8 undergoes a conformational change upon binding to other HSV proteins and/or to DNA coincident with assembly into viral DNA replication structures.

scholarly journals The UL15 protein of herpes simplex virus type 1 is necessary for the localization of the UL28 and UL33 proteins to viral DNA replication centres

2008 ◽  
Vol 89 (7) ◽  
pp. 1709-1715 ◽  
Author(s):  
Martin R. Higgs ◽  
Valerie G. Preston ◽  
Nigel D. Stow
Keyword(s):  
Herpes Simplex Virus ◽  
Dna Replication ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Viral Dna ◽  
Viral Dna Replication ◽  
Simplex Virus ◽  
Hsv 1

The UL15, UL28 and UL33 proteins of herpes simplex virus type 1 (HSV-1) are thought to comprise a terminase complex responsible for cleavage and packaging of the viral genome into pre-assembled capsids. Immunofluorescence studies confirmed that shortly after infection with wild-type HSV-1 these three proteins localize to viral DNA replication compartments within the nucleus, identified by the presence of the single-stranded DNA-binding protein, ICP8. In cells infected with either UL28- or UL33-null mutants, the other two terminase proteins also co-localized with ICP8. In contrast, neither UL28 nor UL33 was detectable in replication compartments following infection with a UL15-null mutant, although Western blot analysis showed they were present in normal amounts in the infected cells. Provision of UL15 in a complementing cell line restored the ability of all three proteins to localize to replication compartments. These data indicate that UL15 plays a key role in localizing the terminase complex to DNA replication compartments, and that it can interact independently with UL28 and UL33.

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