herpes genitalis/phosphatase

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A conserved domain of herpes simplex virus ICP34.5 regulates protein phosphatase complex in mammalian cells.

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ICP34.5, encoded by herpes simplex virus 1, is a protein phosphatase 1 (PP1) regulatory subunit that mediates dephosphorylation of the alpha subunit of translation initiation factor 2 (eIF2alpha). However, the mechanism of its action remains poorly understood. Here, we show that amino acid

Alkaline phosphodiesterase I and alkaline phosphatase I in plasma membranes of herpes simplex virus type 1 transformed hamster cells.

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Plasma membrane extracts from Herpes simplex virus type 1 transformed hamster embryo fibroblasts were chromatographed on Lens culinaris lectin coupled to Sepharose (LcH-Sepharose) and analysed by dodecyl sulphate polyacrylamide gel electrophoresis. Coomassie blue-staining revealed two major protein

Effects of herpes simplex virus vectors encoding poreless TRPV1 or protein phosphatase 1α in a rat cystitis model induced by hydrogen peroxide.

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Enhanced afferent excitability is considered to be an important pathophysiological basis of interstitial cystitis/bladder pain syndrome (IC/BPS). In addition, transient receptor potential vanilloid-1 (TRPV1) receptors are known to be involved in afferent sensitization. Animals with hydrogen peroxide

Isoenzymes of lactate dehydrogenase, acid phosphatase, alkaline phosphatase and peroxidase in monkey kidney cell cultures inoculated with herpes virus type 1.

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The variation of lactate dehydrogenase, peroxidase, acid and alkaline phosphatase isoenzymes was studied in VERO cells inoculated with infectant and UV-inactivated herpes simplex virus type 1 (HSV--1). Infectant HSV--1 induced quantitative and qualitative modifications in isoenzyme patterns within

An N-terminal arginine-rich cluster and a proline-alanine-threonine repeat region determine the cellular localization of the herpes simplex virus type 1 ICP34.5 protein and its ligand, protein phosphatase 1.

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The ICP34.5 protein facilitates herpes simplex virus replication by binding and activating protein phosphatase 1 (PP1) by means of a very conserved C-terminal GADD34-like region. Natural variants of the ICP34.5 differing in the number of arginines in an Arg-rich cluster at the N terminus and the

Reversible decrease of fluoride resistant acid phosphatase-positive neurons after herpes simplex virus infection.

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Herpes simplex virus (HSV) frequently infects human sensory ganglion neurons, and similar infections have been reported in experimental animals. Reported here is an investigation of in vivo neuronal function after HSV infection. It was observed that the proportion of fluoride resistant acid

The interaction of herpes simplex virus 1 regulatory protein ICP22 with the cdc25C phosphatase is enabled in vitro by viral protein kinases US3 and UL13.

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Earlier studies have shown that ICP22 and the U(L)13 protein kinase but not the U(S)3 kinase are required for optimal expression of a subset of late (gamma(2)) genes exemplified by U(L)38, U(L)41, and U(S)11. In primate cells, ICP22 mediates the disappearance of inactive isoforms of cdc2 and

The effect of herpes simplex virus vector-mediated gene therapy of protein phosphatase 1α on bladder overactivity and nociception.

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We studied the effect of herpes simplex virus (HSV) vectors-based gene transfer of protein phosphatase 1α (PP1α) on bladder hypersensitivity in rats.Using adult female Sprague-Dawley rats, non-replicating HSV vectors carrying PP1α or green fluorescent

Role of cellular phosphatase cdc25C in herpes simplex virus 1 replication.

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Earlier studies have shown that in herpes simplex virus 1-infected cells, ICP22 upregulates the accumulation of a subset of gamma(2) proteins exemplified by the products of the U(L)38, U(L)41, and U(S)11 genes. The ICP22-dependent process involves degradation of cyclins A and B1, the stabilization

The inactivation of herpes simplex virus by phosphatase enzymes.

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Tissue phosphatases which are present in virus suspensions were found to contribute in considerable measure to the inactivation of herpes simplex virus. Phosphatase inhibitors and phosphatase substrates have been found to prolong the survival of the virus. Exogenous phosphatases, both acid and

Influence of 2,4,6-triamino-pyrimidyl-5-azobenzene on the activities of acid phosphatase, alkaline phosphatase and lactate dehydrogenase in cell cultures infected with herpes simplex virus type 1.

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Treatment of VERO cells with 2,4,6-triamino-pyridimyl-5-azobenzene (10 gamma/ml) one hour after inoculation of herpes simplex virus type 1 limits the influence of the virus infection, consisting in the enchancement of the activities of alkaline phosphatase, acid phosphatase and LDH (especially of

The gamma134.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells.

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The carboxyl-terminal domain of the gamma134.5 protein of the herpes simplex virus 1 binds to protein phosphatase 1alpha (PP1) and is required to prevent the shut-off of protein synthesis resulting from phosphorylation of the alpha subunit of eIF-2 by the double-stranded RNA-activated protein

Oncolytic herpes simplex virus armed with xenogeneic homologue of prostatic acid phosphatase enhances antitumor efficacy in prostate cancer.

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Prostate cancer is one of the most prevalent cancers in men. Replication-competent oncolytic herpes simplex virus (oHSV) vectors are a powerful antitumor therapy that can exert at least two effects: direct cytocidal activity that selectively kills cancer cells and induction of antitumor immunity. In

ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2alpha (eIF2alpha) and protein phosphatase 1.

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The ICP34.5 protein of herpes simplex virus type 1 is a neurovirulence factor that plays critical roles in viral replication and anti-host responses. One of its functions is to recruit protein phosphatase 1 (PP1) that leads to the dephosphorylation of the α subunit of translation initiation factor

The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase.

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In human cells infected with herpes simplex virus 1 the double-stranded RNA-dependent protein kinase (PKR) is activated but phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2) and total shutoff of protein synthesis is observed only in cells infected with

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