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Pathogen research abs 1 || Pathogen research abs 2 || Pathogen research abs 3 || Pathogen research abs 4 || Pathogen research abs 5 || Hormone and endocrine research abs 1 || Hormone and endocrine research abs 2 || Hormone and endocrine research abs 3 || Hormone and endocrine research abs 4 || Hormone and endocrine research abs 5 || Follicle and follicular cells research abs 1 || Interferon research abs 1 || Hemoglobin research abs || Stem cell research abs || Nucleic acid research abs || Herpes research abs

Intervirology. 2000;43(3):129-38.
Enhancement of herpes simplex virus-induced polykaryocyte formation by 12-O-tetradecanoyl phorbol 13-acetate: association with the reorganization of actin filaments and cell motility.

Yura Y, Kusaka J, Bando T, Yamamoto S, Yoshida H, Sato M.

Second Department of Oral and Maxillofacial Surgery, Tokushima University School of Dentistry, Tokushima, Japan. yurent.tokushima-u.ac.jp

A morphological change induced by syn- herpes simplex virus type 1 (HSV-1), polykaryocyte formation, was enhanced by treatment with 12-O-tetradecanoyl phorbol 13-acetate (TPA) in A431 cells. TPA treatment decreased the number of stress fibers, but led to the development of spike-like filopodia and actin-containing long projections. Similar reorganization of actin filaments was observed in HSV-1-induced polykaryocytes. The actin filament-disrupting drug cytochalasin D, but not the microtubule-disrupting drug nocodazole, inhibited the effect of TPA on polykaryocyte formation, indicating that the actin microfilament system plays a key role in this event. HSV-1 glycoprotein D (gD) was present in the cytoplasm of HSV-1-infected cells and gD gene-transfected cells; its expression became prominent at long cell projections in the presence of TPA. These findings suggest that the reorganization of actin filaments and cell motility are associated with the enhancing effect of TPA on HSV-1-induced polykaryocyte formation. 2000 S. Karger AG, Basel

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11044806&dopt=Abstract

J Microbiol Immunol Infect. 2000 Sep;33(3):141-8.
Different forms of HSV-1 VP22a within purified virion and infected cells.

Yang CC, Yang YY, Lin KL, Lin SJ.

School of Medical Technology, Chung Shan Medical and Dental College, Taichung, Taiwan, ROC.

Utilizing the monoclonal antibody MCA406, our experimental data suggest that the herpes simplex virus type 1 (HSV-1) protein, VP22a, is present in the purified virus in a different form from that present within infected cells, namely the virion and infected-cell form, respectively. It seems reasonable to suggest that two different forms of VP22a are synthesized during the HSV-1 productive cycle. Using varying quantities of reducing agents, both inter- and intramolecular disulfide linkages were demonstrated in this protein family. Moreover, the VP22a-virion form could not be detected under nonreducing conditions by monoclonal antibody, even in the presence of proteolysis inhibitors, i.e. aprotinin, phenyl-methane-sulfonyl fluoride (PMSF) and soybean trypsin inhibitor. Varying temperature had little effect on the breakdown of VP22a disulfide bonds. A higher molecular-weight band, present in the nonreduced gel tracks, clearly indicates the presence of intermolecular disulfide bonds. Similarly, the appearance of bands of lower apparent molecular weight in the nonreduced tracks suggests the presence of intramolecular disulfide bonding. The VP22a infected-cell form may be modified to the virion form during the capsid-assembly process, prior to full capsid formation.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11045375&dopt=Abstract

J Gene Med. 2000 Sep-Oct;2(5):353-60.
Therapy of peritoneal carcinomatosis from colon cancer with oncolytic adenoviruses.

Wildner O, Morris JC.

Clinical Gene Therapy Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892-1851, USA. wildnerk-berlin.de

BACKGROUND: The major emphasis on the safety of viral vectors for gene delivery has led to the generally accepted approach of disabling their ability to replicate and thus their potential capacity to spread throughout a tumor by consecutive rounds of infection and lysing neighboring cells. METHODS: In this study we evaluated three herpes simplex virus-1 thymidine kinase (HSV-tk) carrying replication-competent adenoviral vectors with and without the Ad5 E1B 55-kDa gene, wild-type adenovirus type 5 (Ad5wt), and a prototypical replication-deficient adenovirus expressing HSV-tk (Ad.TK) for their cytoreductive effects in a peritoneal carcinomatosis model from human HT-29 colon cancer cells in nude mice. RESULTS: The survival of nude mice treated with the replication-defective adenoviral vector Ad.TK was enhanced when followed by GCV. In contrast, administration of GCV diminished the anti-tumor efficacy of the replication-competent HSV-tk expressing vectors. However, the intrinsic oncolytic effect of all replication-competent viruses was superior to that of Ad.TK+GCV. Furthermore, the oncolysis of the E1B 55-kDa-positive viruses was significantly greater than that of the E1B 55-kDa-deleted vector. CONCLUSIONS: The more efficient diffusion of viral particles in the peritoneal cavity, when compared to the microenvironment of solid tumors and the virostatic effects of GCV, most likely antagonized the anticipated enhanced cytotoxicity of the replication-competent vectors from the use of its gene directed enzyme prodrug system. Nevertheless, in a clinical setting, the HSV-tk/GCV system allows efficient termination of viral replication in the case of a runaway infection. The results of this study warrant further evaluation of controllable viral replication as a treatment modality for cancer, especially in combination with conventional therapies (e.g. chemotherapy).

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11045429&dopt=Abstract

J Gene Med. 2000 Sep-Oct;2(5):379-89.
HSV-1 infected cell proteins influence tetracycline-regulated transgene expression.

Herrlinger U, Pechan PA, Jacobs AH, Woiciechowski C, Rainov NG, Fraefel C, Paulus W, Reeves SA.

Neurology Service, Massachusetts General Hospital and Harvard Medical School, Charlestown 02129, USA. ulrich.herrlingeni-tuebingen.de

BACKGROUND: This study investigates elements of herpes simplex virus type 1 (HSV-1) which influence transgene expression in tetracycline-regulated expression systems. METHODS: Different HSV-1 mutants were used to infect Vero cells that had been transfected with plasmids containing the luciferase gene under the control of tet-off or tet-on tetracycline-regulation systems. RESULTS: The baseline level of luciferase expression was elevated after infection with HSV-1 mutants lacking one or more immediate early genes encoding transactivating factors: ICP27, ICP4 and ICP0. With the tet-off system, not only was baseline expression elevated, but there was a complete loss of induction upon removal of tet when this regulatory system was brought into the cell by infection with helper virus-free amplicon vectors. Elevation of luciferase expression was also observed upon infection with the same HSV-1 mutants following transfection with a plasmid containing only a CMV minimal promoter driving luciferase (pUHC13-3). Only one HSV mutant (14Hdelta3), which bears a disruption in the transactivation domain of VP16 and is deleted for both ICP4 genes, did not increase baseline luciferase expression after transfection of pUHC13-3. The disregulating effects were dependent on virus dose and were not influenced by treatment with interferon (IFN)-alpha, which suppresses viral gene expression. Additional assays involving cotransfection of pUHC13-3 with a plasmid encoding of the HSV-1 transactivating factor ICP4 revealed that ICP4 was the most potent inducer of gene expression from the tetO/CMV minimal promoter. CONCLUSION: These results indicate that proteins encoded in the HSV-1 genome, especially the transactivating immediate early gene products (ICP4, ICP27 and ICP0) and the VP16 tegument protein can activate the tetO/ minimal CMV promoter and thereby interfere with the integrity of tetracycline-regulated transgene expression.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11045432&dopt=Abstract

J Virol. 2002 Dec;76(24):12877-89.
ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.

Chen IH, Sciabica KS, Sandri-Goldin RM.

Department of Microbiology and Molecular Genetics, Medical Sciences I, College of Medicine, University of California, Irvine, CA 92697-4025, USA.

Herpes simplex virus type 1 (HSV-1) protein ICP27 facilitates the export of viral intronless mRNAs. ICP27 shuttles between the nucleus and cytoplasm, which has been shown to require a leucine-rich nuclear export sequence (NES). ICP27 export was reported to be sensitive to the CRM1 inhibitor leptomycin B (LMB) in HSV-1-infected cells but not in Xenopus oocytes, where ICP27 interacts with the export factor Aly/REF to access the TAP export pathway. Here, we show that ICP27 interacts with Aly/REF in HSV-1-infected mammalian cells and that Aly/REF stimulates export of viral intronless RNAs but does not cross-link to these RNAs. During infection, Aly/REF was no longer associated with splicing factor SC35 but moved into structures that colocalized with ICP27, suggesting that ICP27 recruits Aly/REF from spliceosomes to viral intronless RNAs. Further, ICP27 was found to interact in vivo with TAP but not with CRM1. In vitro export assays showed that ICP27 export was not sensitive to LMB but was blocked by a dominant-negative TAP deletion mutant lacking the nucleoporin interaction domain. These data suggest that ICP27 uses the TAP pathway to export viral RNAs. Interestingly, the leucine-rich N-terminal sequence was required for efficient export, even though ICP27 export was LMB insensitive. Thus, this region is required for efficient ICP27 export but does not function as a CRM1-dependent NES.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12438613&dopt=Abstract

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