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Dissection of a novel nuclear localization signal in open reading frame 29 of varicella-zoster virus.

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Open reading frame 29 (ORF29) of varicella-zoster virus (VZV) encodes a 120-kDa single-stranded DNA binding protein (ORF29p) that is not packaged in the virion and is expressed during latency. During lytic infection, ORF29p is localized primarily to infected cell nuclei. In contrast, ORF29p is found

Disruption of the varicella-zoster virus dUTPase and the adjacent ORF9A gene results in impaired growth and reduced syncytia formation in vitro.

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Varicella-zoster virus (VZV) open reading frame 8 (ORF8) is predicted to encode the viral dUTPase and the adjacent gene, ORF9A, is thought to encode a membrane protein homologous to HSV-1 UL49.5. A fusion protein, in which the amino portion of glutathione-S-transferase was fused to amino acids 5 to

Comparison of varicella-zoster virus ORF47 protein kinase and casein kinase II and their substrates.

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ORF47, a serine/threonine protein kinase encoded by varicella-zoster virus (VZV), has often been compared to the ubiquitous cellular kinase, casein kinase II (CKII). However, no direct comparison of the two protein kinases has been carried out. Herein, we show that the ORF47 kinase was resistant to

Highly purified recombinant varicella Zoster virus thymidine kinase is a homodimer.

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Recombinant varicella zoster virus (VZV) thymidine kinase (TK) was isolated in a fast and gentle two-step procedure from Escherichia coli. The TK was expressed as a PreScission-cleavable fusion protein and purified by glutathione and ATP affinity chromatography, yielding homogeneous, highly pure VZV

Characterization of Varicella-Zoster virus glycoprotein K (open reading frame 5) and its role in virus growth.

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Varicella-zoster virus (VZV) is an alphaherpesvirus that is the causative agent of chickenpox and herpes zoster. VZV open reading frame 5 (ORF5) encodes glycoprotein K (gK), which is conserved among alphaherpesviruses. While VZV gK has not been characterized, and its role in viral replication is

Varicella-zoster virus Fc receptor component gI is phosphorylated on its endodomain by a cyclin-dependent kinase.

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Varicella-zoster virus (VZV) glycoprotein gI is a type 1 transmembrane glycoprotein which is one component of the heterodimeric gE:gI Fc receptor complex. Like VZV gE, VZV gI was phosphorylated in both VZV-infected cells and gI-transfected cells. Preliminary studies demonstrated that a serine

Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope.

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The cytoplasmic tails of all three major varicella-zoster virus (VZV) glycoproteins, gE, gH, and gB, harbor functional tyrosine-based endocytosis motifs that mediate internalization. The aim of the present study was to examine whether endocytosis from the plasma membrane is a cellular route by which

Localization of varicella-zoster virus gene 21 protein in virus-infected cells in culture.

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Although four varicella-zoster virus (VZV) genes have been shown to be transcribed in latently infected human ganglia, their role in the development and maintenance of latency is unknown. To study these VZV transcripts, we decided first to localize their expression products in productively infected

Varicella-zoster virus gene 63 encodes an immediate-early protein that is abundantly expressed during latency.

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Varicella-zoster virus (VZV) gene 63 encodes a protein with a predicted molecular mass of 30.5 kDa which has amino acid similarities with the immediate-early (IE) protein 22 (ICP-22) of herpes simplex virus type 1. In order to study the expression of this protein during lytic and latent infection,

Identification of an immediate-early gene in the Marek's disease virus long internal repeat region which encodes a unique 14-kilodalton polypeptide.

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Marek's disease virus (MDV) is an oncogenic avian herpesvirus whose genomic structure is similar to those of herpes simplex virus and varicella-zoster virus. Repeat regions of the MDV genome have been intensively investigated because of a potential relationship to MDV oncogenicity and abundant

Impaired oxidative status as a potential predictor in clinical manifestations of herpes zoster.

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Oxidative stress, caused by an imbalance between reactive oxygen species and antioxidants, is related to many dermatologic diseases. Increased reactive oxygen species is also associated with various decreased T-cell immune responses. The incidence and severity of herpes zoster (HZ), which is caused

Identification of a dimerization domain in the C-terminal segment of the IE110 transactivator protein from herpes simplex virus.

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The 775-amino-acid IE110 (or ICP0) phosphoprotein of herpes simplex virus (HSV) functions as an accessory transcription factor during the lytic cycle and plays a critical role in reactivation from latent infection. By immunofluorescence analysis, IE110 localizes in a novel pattern consisting of

The bovine herpesvirus type 1 UL3.5 open reading frame encodes a virion structural protein.

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The bovine herpesvirus type 1 (BHV-1) open reading frame (ORF) UL3.5 is similar to ORFs found in pseudorabies virus, infectious laryngotracheitis virus, equine herpesvirus type 1, and varicella zoster virus, but clearly absent from herpes simplex virus. The published sequence for this ORF predicts a

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