A Role for Bovine Herpesvirus 1 (BHV-1) Glycoprotein E (gE) Tyrosine Phosphorylation in Replication of BHV-1 Wild-Type Virus but Not BHV-1 gE Deletion Mutant Virus

Shaw, Amy; Braun, L. J.; Frew, T.; Hurley, David J.; Rowland, Raymond R.R.; Chase, Christopher

doi:10.1006/viro.1999.0164

Cited by 16 publications

(26 citation statements)

References 39 publications

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“…After a 24-h incubation, the cells were analyzed for the expression of LDH, as an indicator of cell death. The LDH assay was performed using the CytoTox 96 non-radioactive kit (Promega) as per earlier studies (22).…”

Section: Cells-hmvec-d Cells Were Propagated In Egmmentioning

confidence: 99%

Cell Membrane-bound Kaposi's Sarcoma-associated Herpesvirus-encoded Glycoprotein B Promotes Virus Latency by Regulating Expression of Cellular Egr-1

Dyson

Traylen

Akula

2010

Journal of Biological Chemistry

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One of the important questions in the field of virus research is about the balance between latent and lytic cycles of replication. Kaposi's sarcoma-associated herpesvirus (KSHV) remains predominantly in a latent state, with only 1-3% of cells supporting a lytic replication at any time. KSHV glycoprotein B (gB) is expressed not only on the virus envelope but also on the surfaces of the few cells supporting lytic replication. Using co-culture experiments, we determined that expression of KSHV gB on as few as 1-2% of human dermal microvascular endothelial cells resulted in a 10-fold inhibition of expression of ORF50, a viral gene critical for the onset of lytic replication. Also, we demonstrate that such a profound inhibitory effect of gB on the lytic cycle of virus replication is by repressing the ability of Egr-1 (early growth response-1) to bind and activate the ORF50 promoter. In general, virus-encoded late stage structural proteins, such as gB, are said to play major roles in virus entry and egress. The present report provides initial evidence supporting a role for membrane-associated gB expressed in a minimal number of cells to promote virus latency. These findings may have ramifications leading to a better understanding of the role of virusencoded structural proteins not only in KSHV-related diseases but also in other viruses causing latent infections.

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Section: Cells-hmvec-d Cells Were Propagated In Egmmentioning

confidence: 99%

Cell Membrane-bound Kaposi's Sarcoma-associated Herpesvirus-encoded Glycoprotein B Promotes Virus Latency by Regulating Expression of Cellular Egr-1

Dyson

Traylen

Akula

2010

Journal of Biological Chemistry

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“…Blocking tyrosine phosphorylation of glycoprotein E (gE), an envelope protein, reduces viral replication (19). Removing tyrosine phosphorylation of VP22 decreases the amount of VP22 incorporated into virions (20).…”

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confidence: 99%

Phosphorylation of Bovine Herpesvirus 1 VP8 Plays a Role in Viral DNA Encapsidation and Is Essential for Its Cytoplasmic Localization and Optimal Virion Incorporation

Brownlie

Snider

Hurk

2016

J Virol

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VP8 is a major tegument protein of bovine herpesvirus 1 (BoHV-1) and is essential for viral replication in cattle. The protein undergoes phosphorylation after transcription through cellular casein kinase 2 (CK2) and a viral kinase, US3. In this study, a virus containing a mutated VP8 protein that is not phosphorylated by CK2 and US3 (BoHV-1-YmVP8) was constructed by homologous recombination in mammalian cells. When BoHV-1-YmVP8-infected cells were observed by transmission electron microscopy, blocking phosphorylation of VP8 was found to impair viral DNA encapsidation, resulting in release of incomplete viral particles to the extracellular environment. Consequently, less infectious virus was produced by the mutant virus than by wild-type (WT) virus. A comparison of mutant and WT VP8 by confocal microscopy revealed that mutant VP8 is nuclear throughout infection while WT VP8 is nuclear early during infection and is associated with the Golgi apparatus at later stages. This, together with the observation that mutant VP8 is present in virions, albeit in smaller amounts, suggests that the incorporation of VP8 may occur at two stages. The first takes place without the need for phosphorylation and before or during nuclear egress of capsids, whereas the second occurs in the Golgi apparatus and requires phosphorylation of VP8. The results indicate that phosphorylated VP8 plays a role in viral DNA encapsidation and in the secondary virion incorporation of VP8. To perform these functions, the cellular localization of VP8 is adjusted based on the phosphorylation status. IMPORTANCEIn this study, phosphorylation of VP8 was shown to have a function in BoHV-1 replication. A virus containing a mutated VP8 protein that is not phosphorylated by CK2 and US3 (BoHV-1-YmVP8) produced smaller numbers of infectious virions than wild-type (WT) virus. The maturation and egress of WT and mutant BoHV-1 were studied, showing a process similar to that reported for other alphaherpesviruses. Interestingly, lack of phosphorylation of VP8 by CK2 and US3 resulted in reduced incorporation of viral DNA into capsids during mutant BoHV-1 infection, as well as lower numbers of extracellular virions. Furthermore, mutant VP8 remained nuclear throughout infection, in contrast to WT VP8, which is nuclear at early stages and Golgi apparatus associated late during infection. This correlates with smaller amounts of mutant VP8 in virions and suggests for the first time that VP8 may be assembled into the virions at two stages, with the latter dependent on phosphorylation. Bovine herpesvirus 1 (BoHV-1), a member of the Alphaherpesviridae, causes infectious bovine rhinotracheitis (IBR) in cattle, as well as conjunctivitis, vulvovaginitis, and balanoposthitis. The herpesvirus particle is composed of a capsid containing the double-stranded DNA genome, which is surrounded by a tegument layer and an envelope containing viral glycoproteins (1). During the herpesvirus life cycle, genome synthesis, capsid assembly, DNA incorporation (2), and primary tegumentation...

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“…SS is capable of inhibiting cytoplasmic and receptor tyrosine kinases (Wilde et al, 1999). It was demonstrated that there are several phosphorylated BHV-1 proteins in infected cells (Shaw et al, 2000;Ren et al, 2001), like in the case of HSV-1 (Aubert et al, 1999), and it may be of interest to investigate whether viral protein phosphorylation might play a role in the induction or prevention of apoptosis in BHV-1-infected cells.…”

Section: Discussionmentioning

confidence: 99%

Selective apoptotic behaviour of bovine herpesvirus 1 in an epithelial-like microenvironment

Baskın

Yazıcı²,

Baskın³

et al. 2005

Acta Veterinaria Hungarica

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Apoptosis seems to play an important role in the pathogenic profile of bovine herpesvirus 1 (BHV-1) infection. Nitric oxide (NO) is also important as a signal molecule. In this study, apoptosis was selectively induced in HEp-2 cells in the early stage [1-3 h postinfection (PI)] of BHV-1 multiplication, and this apoptotic process was realised through the caspase-8, and partially through the caspase-3, pathway. BHV-1 infection inhibited staurosporine-(SS-) induced apoptosis only if the SS was added at 6 h PI. The results of this study showed that the 'NO-apoptosis' relation was realised through the caspase-8 pathway ('outer membrane receptor' pathway) at a later stage of infection in apoptosis induced by BHV-1 + SS. Our previous report (Yazici et al., 2004) and this study together showed that BHV-1 might induce and inhibit cell-type-specific pathways of apoptosis.

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A Role for Bovine Herpesvirus 1 (BHV-1) Glycoprotein E (gE) Tyrosine Phosphorylation in Replication of BHV-1 Wild-Type Virus but Not BHV-1 gE Deletion Mutant Virus

Cited by 16 publications

References 39 publications

Cell Membrane-bound Kaposi's Sarcoma-associated Herpesvirus-encoded Glycoprotein B Promotes Virus Latency by Regulating Expression of Cellular Egr-1

Cell Membrane-bound Kaposi's Sarcoma-associated Herpesvirus-encoded Glycoprotein B Promotes Virus Latency by Regulating Expression of Cellular Egr-1

Phosphorylation of Bovine Herpesvirus 1 VP8 Plays a Role in Viral DNA Encapsidation and Is Essential for Its Cytoplasmic Localization and Optimal Virion Incorporation

Selective apoptotic behaviour of bovine herpesvirus 1 in an epithelial-like microenvironment

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