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Journal articles on the topic 'VSV-G'

Author: Grafiati

Published: 4 June 2021

Last updated: 29 March 2025

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1

Martinez, Isidoro, Luis L. Rodriguez, Carlos Jimenez, Steven J. Pauszek, and Gail W. Wertz. "Vesicular Stomatitis Virus Glycoprotein Is a Determinant of Pathogenesis in Swine, a Natural Host." Journal of Virology 77, no. 14 (2003): 8039–47. http://dx.doi.org/10.1128/jvi.77.14.8039-8047.2003.

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ABSTRACT There are two major serotypes of vesicular stomatitis virus (VSV), Indiana (VSIV) and New Jersey (VSNJV). We recovered recombinant VSIVs from engineered cDNAs that contained either (i) one copy of the VSIV G gene (VSIV-GI); (ii) two copies of the G gene, one from each serotype (VSIV-GNJGI); or (iii) a single copy of the GNJ gene instead of the GI gene (VSIV-GNJ). The recombinant viruses expressed the appropriate glycoproteins, incorporated them into virions, and were neutralized by antibodies specific for VSIV (VSIV-GI), VSNJV (VSIV-GNJ), or both (VSIV-GNJGI), according to the glycopr

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2

Mattioli, Martina, Renata A. Raele, Gunjan Gautam, et al. "Tuning VSV-G Expression Improves Baculovirus Integrity, Stability and Mammalian Cell Transduction Efficiency." Viruses 16, no. 9 (2024): 1475. http://dx.doi.org/10.3390/v16091475.

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Baculoviral vectors (BVs) derived from Autographa californica multiple nucleopolyhedrovirus (AcMNPV) are an attractive tool for multigene delivery in mammalian cells, which is particularly relevant for CRISPR technologies. Most applications in mammalian cells rely on BVs that are pseudotyped with vesicular stomatitis virus G-protein (VSV-G) to promote efficient endosomal release. VSV-G expression typically occurs under the control of the hyperactive polH promoter. In this study, we demonstrate that polH-driven VSV-G expression results in BVs characterised by reduced stability, impaired morphol

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3

Wollmann, Guido, Vitaliy Rogulin, Ian Simon, John K. Rose, and Anthony N. van den Pol. "Some Attenuated Variants of Vesicular Stomatitis Virus Show Enhanced Oncolytic Activity against Human Glioblastoma Cells relative to Normal Brain Cells." Journal of Virology 84, no. 3 (2009): 1563–73. http://dx.doi.org/10.1128/jvi.02040-09.

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ABSTRACT Vesicular stomatitis virus (VSV) has been shown in laboratory studies to be effective against a variety of tumors, including malignant brain tumors. However, attenuation of VSV may be necessary to balance the potential toxicity toward normal cells, particularly when targeting brain tumors. Here we compared 10 recombinant VSV variants resulting from different attenuation strategies. Attenuations included gene shifting (VSV-p1-GFP/RFP), M protein mutation (VSV-M51), G protein cytoplasmic tail truncations (VSV-CT1/CT9), G protein deletions (VSV-dG-GFP/RFP), and combinations thereof (VSV-

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4

Bachmann, M. F., T. Fehr, G. Freer, H. Hengartner, and R. M. Zinkernagel. "Correlation of tolerogenicity of a viral antigen with its immunogenicity." Journal of Immunology 158, no. 11 (1997): 5106–11. http://dx.doi.org/10.4049/jimmunol.158.11.5106.

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Abstract Induction of B cell tolerance or activation was analyzed with vesicular stomatitis virus (VSV) glycoprotein (G) expressed as a neo-self Ag. A membrane form of VSV-G expressed in all tissues, including the bone marrow, induced unresponsiveness at both the Th and B cell level, whereas a soluble form of VSV-G expressed peripherally in liver and kidney did not tolerize B cells and only reversibly anergized Th cells. Interestingly, a similar correlation was found for activation of mature lymphocytes. When mature normal spleen cells were transferred into the two transgenic mouse lines, the

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5

Arai, Tohru, Kazuyuki Matsumoto, Kanako Saitoh, et al. "A New System for Stringent, High-Titer Vesicular Stomatitis Virus G Protein-Pseudotyped Retrovirus Vector Induction by Introduction of Cre Recombinase into Stable Prepackaging Cell Lines." Journal of Virology 72, no. 2 (1998): 1115–21. http://dx.doi.org/10.1128/jvi.72.2.1115-1121.1998.

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ABSTRACT We report here on stable prepackaging cell lines which can be converted into packaging cell lines for high-titer vesicular stomatitis virus G protein (VSV-G)-pseudotyped retrovirus vectors by the introduction of Cre recombinase-expressing adenovirus. The generated prepackaging cell lines constitutively express the gag-polgenes and contain an inducible transcriptional unit for the VSV-G gene. From this unit, the introduced Cre recombinase excised both a neomycin resistance (Neor) gene and a poly(A) signal flanked by a tandem pair of loxP sequences and induced transcription of the VSV-G

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6

Bonilha, V. L., A. D. Marmorstein, L. Cohen-Gould, and E. Rodriguez-Boulan. "Apical sorting of influenza hemagglutinin by transcytosis in retinal pigment epithelium." Journal of Cell Science 110, no. 15 (1997): 1717–27. http://dx.doi.org/10.1242/jcs.110.15.1717.

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The retinal pigment epithelium is endowed with a unique distribution of certain plasma membrane proteins. Na+,K+-ATPase, for instance, is polarized to the apical surface of RPE, rather than to the basolateral surface as in most other epithelia. To study the sorting pathways of RPE cells, we used temperature sensitive mutants of influenza and vesicular stomatitis virus (VSV) to synchronize the transport of hemagglutinin (HA) and VSV G protein (VSV G) along the biosynthetic pathway of the RPE cell line RPE-J. After HA and VSV G accumulated in the trans-Golgi network of RPE-J cells kept at 20 deg

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7

Abe, Akihiro, Atsushi Miyanohara, and Theodore Friedmann. "Enhanced Gene Transfer with Fusogenic Liposomes Containing Vesicular Stomatitis Virus G Glycoprotein." Journal of Virology 72, no. 7 (1998): 6159–63. http://dx.doi.org/10.1128/jvi.72.7.6159-6163.1998.

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ABSTRACT Exposure of Lipofectin-DNA complexes to the partially purified G glycoprotein of the vesicular stomatitis virus envelope (VSV-G) results in loss of serum-mediated inhibition and in enhanced efficiency of gene transfer. Sucrose density gradient sedimentation analysis indicated that the VSV-G associates physically with the DNA-lipid complex to produce a VSV-G liposome. The ability to incorporate surrogate viral or cellular envelope components such as VSV-G into liposomes may allow more-efficient and possibly targeted gene delivery by lipofection, both in vitro and in vivo.

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8

Ozduman, Koray, Guido Wollmann, Sebastian A. Ahmadi, and Anthony N. van den Pol. "Peripheral Immunization Blocks Lethal Actions of Vesicular Stomatitis Virus within the Brain." Journal of Virology 83, no. 22 (2009): 11540–49. http://dx.doi.org/10.1128/jvi.02558-08.

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ABSTRACT Vesicular stomatitis virus (VSV) is the prototype virus for 75 or more negative-strand RNA viruses in the rhabdovirus family. Some of these viruses, including VSV, can cause neurological impairment or death upon brain infection. VSV has shown promise in the prevention and treatment of disease as a vaccine vector and an oncolytic virus, but infection of the brain remains a concern. Three VSV variants, the wild-type-related VSV-G/GFP and two attenuated viruses, VSV-CT1 and VSV-CT9-M51, were compared for neuroinvasiveness and neuromorbidity. In nonimmunized mice, direct VSV-G/GFP injecti

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9

Jargalsaikhan, Bat-Erdene, Masanaga Muto, Youngeun Been, et al. "The Dual-Pseudotyped Lentiviral Vector with VSV-G and Sendai Virus HN Enhances Infection Efficiency through the Synergistic Effect of the Envelope Proteins." Viruses 16, no. 6 (2024): 827. http://dx.doi.org/10.3390/v16060827.

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A gene delivery system utilizing lentiviral vectors (LVs) requires high transduction efficiency for successful application in human gene therapy. Pseudotyping allows viral tropism to be expanded, widening the usage of LVs. While vesicular stomatitis virus G (VSV-G) single-pseudotyped LVs are commonly used, dual-pseudotyping is less frequently employed because of its increased complexity. In this study, we examined the potential of phenotypically mixed heterologous dual-pseudotyped LVs with VSV-G and Sendai virus hemagglutinin-neuraminidase (SeV-HN) glycoproteins, termed V/HN-LV. Our findings d

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10

Sevier, Carolyn S., Ora A. Weisz, Mollie Davis, and Carolyn E. Machamer. "Efficient Export of the Vesicular Stomatitis Virus G Protein from the Endoplasmic Reticulum Requires a Signal in the Cytoplasmic Tail That Includes Both Tyrosine-based and Di-acidic Motifs." Molecular Biology of the Cell 11, no. 1 (2000): 13–22. http://dx.doi.org/10.1091/mbc.11.1.13.

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The vesicular stomatitis virus (VSV) G protein is a model transmembrane glycoprotein that has been extensively used to study the exocytotic pathway. A signal in the cytoplasmic tail of VSV G (DxE or Asp-x-Glu, where x is any amino acid) was recently proposed to mediate efficient export of the protein from the endoplasmic reticulum (ER). In this study, we show that the DxE motif only partially accounts for efficient ER exit of VSV G. We have identified a six-amino-acid signal, which includes the previously identified Asp and Glu residues, that is required for efficient exit of VSV G from the ER

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11

Kahn, Jeffrey S., Anjeanette Roberts, Carla Weibel, Linda Buonocore, and John K. Rose. "Replication-Competent or Attenuated, Nonpropagating Vesicular Stomatitis Viruses Expressing Respiratory Syncytial Virus (RSV) Antigens Protect Mice against RSV Challenge." Journal of Virology 75, no. 22 (2001): 11079–87. http://dx.doi.org/10.1128/jvi.75.22.11079-11087.2001.

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ABSTRACT Foreign glycoproteins expressed in recombinant vesicular stomatitis virus (VSV) can elicit specific and protective immunity in the mouse model. We have previously demonstrated the expression of respiratory syncytial virus (RSV) G (attachment) and F (fusion) glycoprotein genes in recombinant VSV. In this study, we demonstrate the expression of RSV F and G glycoproteins in attenuated, nonpropagating VSVs which lack the VSV G gene (VSVΔG) and the incorporation of these RSV proteins into recombinant virions. We also show that intranasal vaccination of mice with nondefective VSV recombinan

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12

Rose, Nina F., Anjeanette Roberts, Linda Buonocore, and John K. Rose. "Glycoprotein Exchange Vectors Based on Vesicular Stomatitis Virus Allow Effective Boosting and Generation of Neutralizing Antibodies to a Primary Isolate of Human Immunodeficiency Virus Type 1." Journal of Virology 74, no. 23 (2000): 10903–10. http://dx.doi.org/10.1128/jvi.74.23.10903-10910.2000.

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ABSTRACT Live recombinant vesicular stomatitis viruses (VSVs) expressing foreign antigens are highly effective vaccine vectors. However, these vectors induce high-titer neutralizing antibody directed at the single VSV glycoprotein (G), and this antibody alone can prevent reinfection and boosting with the same vector. To determine if efficient boosting could be achieved by changing the G protein of the vector, we have developed two new recombinant VSV vectors based on the VSV Indiana serotype but with the G protein gene replaced with G genes from two other VSV serotypes, New Jersey and Chandipu

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13

Maloy, Kevin J., Christoph Burkhart, Tobias M. Junt, et al. "Cd4+ T Cell Subsets during Virus Infection." Journal of Experimental Medicine 191, no. 12 (2000): 2159–70. http://dx.doi.org/10.1084/jem.191.12.2159.

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To analyze the antiviral protective capacities of CD4+ T helper (Th) cell subsets, we used transgenic T cells expressing an I-Ab–restricted T cell receptor specific for an epitope of vesicular stomatitis virus glycoprotein (VSV-G). After polarization into Th1 or Th2 effectors and adoptive transfer into T cell–deficient recipients, protective capacities were assessed after infection with different types of viruses expressing the VSV-G. Both Th1 and Th2 CD4+ T cells could transfer protection against systemic VSV infection, by stimulating the production of neutralizing immunoglobulin G antibodies

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14

Pimplikar, S. W., E. Ikonen, and K. Simons. "Basolateral protein transport in streptolysin O-permeabilized MDCK cells." Journal of Cell Biology 125, no. 5 (1994): 1025–35. http://dx.doi.org/10.1083/jcb.125.5.1025.

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We have reconstituted polarized protein transport in streptolysin O-permeabilized MDCK cells from the TGN to the basolateral surface and to the apical surface. These transport steps are dependent on temperature, energy and exogenously supplied cytosol. Using this in vitro system we show that a whole tail peptide (WT peptide) corresponding to the cytoplasmic tail of a basolaterally sorted protein, the vesicular stomatitis virus glycoprotein (VSV G) inhibits the TGN to basolateral transport but does not affect any other transport step. Inhibition of VSV G transport to basolateral surface by WT p

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15

Yewdell, J. W., J. R. Bennink, M. Mackett, L. Lefrancois, D. S. Lyles, and B. Moss. "Recognition of cloned vesicular stomatitis virus internal and external gene products by cytotoxic T lymphocytes." Journal of Experimental Medicine 163, no. 6 (1986): 1529–38. http://dx.doi.org/10.1084/jem.163.6.1529.

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It has generally been assumed that most if not all CTL specific for vesicular stomatitis virus (VSV)-infected cells recognize the viral glycoprotein (G), an integral membrane protein abundantly expressed on infected cell surfaces. Using recombinant vaccinia viruses containing copies of cloned VSV genes to examine CTL recognition of VSV, we have confirmed that G is recognized by VSV-specific CTL. More interestingly, however, we have also found that nucleocapsid protein (N), an internal virion protein, can be detected on infected cell surfaces using mAb, and serves as a major target antigen for

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16

Gallardo, H. F., C. Tan, D. Ory, and M. Sadelain. "Recombinant Retroviruses Pseudotyped With the Vesicular Stomatitis Virus G Glycoprotein Mediate Both Stable Gene Transfer and Pseudotransduction in Human Peripheral Blood Lymphocytes." Blood 90, no. 3 (1997): 952–57. http://dx.doi.org/10.1182/blood.v90.3.952.952_952_957.

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It is essential for the study of T-cell function and the improvement of adoptive cell therapies to efficiently generate large populations of human primary T cells that reliably express foreign genes. This goal is achieved by using recombinant retroviruses pseudotyped with either the gibbon ape leukemia virus (GaLV) envelope or the vesicular stomatitis virus G (VSV-G) glycoprotein. We show here that both retroviral particles mediate stable gene transfer in CD4+ and in CD8+ peripheral blood lymphocytes cultured under optimized conditions. However, VSV-G–pseudotyped virions may cause transduction

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17

Buonocore, Linda, Keril J. Blight, Charles M. Rice, and John K. Rose. "Characterization of Vesicular Stomatitis Virus Recombinants That Express and Incorporate High Levels of Hepatitis C Virus Glycoproteins." Journal of Virology 76, no. 14 (2002): 6865–72. http://dx.doi.org/10.1128/jvi.76.14.6865-6872.2002.

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ABSTRACT We generated recombinant vesicular stomatitis viruses (VSV) expressing genes encoding hybrid proteins consisting of the extracellular domains of hepatitis C virus (HCV) glycoproteins fused at different positions to the transmembrane and cytoplasmic domains of the VSV G glycoprotein (E1G and E2G). We show that these chimeric proteins are transported to the cell surface and incorporated into VSV virions efficiently. We also generated VSV recombinants in which the gene encoding the VSV G protein was deleted and replaced by one or both of the E1G and E2G genes, together with a green fluor

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18

Hanika, Andrea, Birthe Larisch, Eike Steinmann, Christel Schwegmann-Weßels, Georg Herrler, and Gert Zimmer. "Use of influenza C virus glycoprotein HEF for generation of vesicular stomatitis virus pseudotypes." Journal of General Virology 86, no. 5 (2005): 1455–65. http://dx.doi.org/10.1099/vir.0.80788-0.

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Influenza C virus contains two envelope glycoproteins: CM2, a putative ion channel protein; and HEF, a unique multifunctional protein that performs receptor-binding, receptor-destroying and fusion activities. Here, it is demonstrated that expression of HEF is sufficient to pseudotype replication-incompetent vesicular stomatitis virus (VSV) that lacks the VSV glycoprotein (G) gene. The pseudotyped virus showed characteristic features of influenza C virus with respect to proteolytic activation, receptor usage and cell tropism. Chimeric glycoproteins composed of HEF ectodomain and VSV-G C-termina

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Gallardo, H. F., C. Tan, D. Ory, and M. Sadelain. "Recombinant Retroviruses Pseudotyped With the Vesicular Stomatitis Virus G Glycoprotein Mediate Both Stable Gene Transfer and Pseudotransduction in Human Peripheral Blood Lymphocytes." Blood 90, no. 3 (1997): 952–57. http://dx.doi.org/10.1182/blood.v90.3.952.

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Abstract It is essential for the study of T-cell function and the improvement of adoptive cell therapies to efficiently generate large populations of human primary T cells that reliably express foreign genes. This goal is achieved by using recombinant retroviruses pseudotyped with either the gibbon ape leukemia virus (GaLV) envelope or the vesicular stomatitis virus G (VSV-G) glycoprotein. We show here that both retroviral particles mediate stable gene transfer in CD4+ and in CD8+ peripheral blood lymphocytes cultured under optimized conditions. However, VSV-G–pseudotyped virions may cause tra

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Maloy, Kevin J., Christoph Burkhart, Giulia Freer, et al. "Qualitative and Quantitative Requirements for CD4+ T Cell-Mediated Antiviral Protection." Journal of Immunology 162, no. 5 (1999): 2867–74. http://dx.doi.org/10.4049/jimmunol.162.5.2867.

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Abstract CD4+ Th cells deliver the cognate and cytokine signals that promote the production of protective virus-neutralizing IgG by specific B cells and are also able to mediate direct antiviral effector functions. To quantitatively and qualitatively analyze the antiviral functions of CD4+ Th cells, we generated transgenic mice (tg7) expressing an MHC class II (I-Ab)-restricted TCR specific for a peptide derived from the glycoprotein (G) of vesicular stomatitis virus (VSV). The elevated precursor frequency of naive VSV-specific Th cells in tg7 mice led to a markedly accelerated and enhanced cl

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Carneiro, Fabiana A., M. Lucia Bianconi, Gilberto Weissmüller, Fausto Stauffer, and Andrea T. Da Poian. "Membrane Recognition by Vesicular Stomatitis Virus Involves Enthalpy-Driven Protein-Lipid Interactions." Journal of Virology 76, no. 8 (2002): 3756–64. http://dx.doi.org/10.1128/jvi.76.8.3756-3764.2002.

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ABSTRACT Vesicular stomatitis virus (VSV) infection depends on the fusion of viral and cellular membranes, which is mediated by virus spike glycoprotein G at the acidic environment of the endosomal compartment. VSV G protein does not contain a hydrophobic amino acid sequence similar to the fusion peptides found among other viral glycoproteins, suggesting that membrane recognition occurs through an alternative mechanism. Here we studied the interaction between VSV G protein and liposomes of different phospholipid composition by force spectroscopy, isothermal titration calorimetry (ITC), and flu

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Plutner, H., H. W. Davidson, J. Saraste, and W. E. Balch. "Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: role of the P58 containing compartment." Journal of Cell Biology 119, no. 5 (1992): 1097–116. http://dx.doi.org/10.1083/jcb.119.5.1097.

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The glycoside digitonin was used to selectively permeabilize the plasma membrane exposing functionally and morphologically intact ER and Golgi compartments. Permeabilized cells efficiently transported vesicular stomatitis virus glycoprotein (VSV-G) through sealed, membrane-bound compartments in an ATP and cytosol dependent fashion. Transport was vectorial. VSV-G protein was first transported to punctate structures which colocalized with p58 (a putative marker for peripheral punctate pre-Golgi intermediates and the cis-Golgi network) before delivery to the medial Golgi compartments containing a

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Kahl, Christoph A., Jon Marsh, Joanne Fyffe, David A. Sanders, and Kenneth Cornetta. "Human Immunodeficiency Virus Type 1-Derived Lentivirus Vectors Pseudotyped with Envelope Glycoproteins Derived from Ross River Virus and Semliki Forest Virus." Journal of Virology 78, no. 3 (2004): 1421–30. http://dx.doi.org/10.1128/jvi.78.3.1421-1430.2004.

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ABSTRACT Ross River virus (RRV) and Semliki Forest virus (SFV) are two alphaviruses that have a high degree of amino acid homology, as well as a very broad host range. We show here that envelope glycoproteins derived from both viruses can pseudotype human immunodeficiency virus type 1 (HIV-1)-derived lentivirus vectors. Both RRV and SFV glycoproteins considerably expand the host range of the lentivirus vector, and vectors can be efficiently concentrated by ultracentrifugation. A systematic analysis comparing the alphaviral glycoproteins to the vesicular stomatitis virus glycoprotein (VSV-G) re

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Mangor, J. T., S. A. Monsma, M. C. Johnson, and G. W. Blissard. "A GP64-Null Baculovirus Pseudotyped with Vesicular Stomatitis Virus G Protein." Journal of Virology 75, no. 6 (2001): 2544–56. http://dx.doi.org/10.1128/jvi.75.6.2544-2556.2001.

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ABSTRACT The Autographa californica multiple nucleopolyhedrovirus (AcMNPV) GP64 protein is an essential virion protein that is involved in both receptor binding and membrane fusion during viral entry. Genetic studies have shown that GP64-null viruses are unable to move from cell to cell and this results from a defect in the assembly and production of budded virions (BV). To further examine requirements for virion budding, we asked whether a GP64-null baculovirus, vAc64−, could be pseudotyped by introducing a heterologous viral envelope protein (vesicular stomatitis virus G protein [VSV-G]) int

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Rahkila, P., V. Luukela, K. Väänänen, and K. Metsikkö. "Differential Targeting of Vesicular Stomatitis Virus G Protein and Influenza Virus Hemagglutinin Appears During Myogenesis of L6 Muscle Cells." Journal of Cell Biology 140, no. 5 (1998): 1101–11. http://dx.doi.org/10.1083/jcb.140.5.1101.

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Exocytic organelles undergo profound reorganization during myoblast differentiation and fusion. Here, we analyzed whether glycoprotein processing and targeting changed during this process by using vesicular stomatitis virus (VSV) G protein and influenza virus hemagglutinin (HA) as models. After the induction of differentiation, the maturation and transport of the VSV G protein changed dramatically. Thus, only half of the G protein was processed and traveled through the Golgi, whereas the other half remained unprocessed. Experiments with the VSV tsO45 mutant indicated that the unprocessed form

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Schlehuber, Lisa D., and John K. Rose. "Prediction and Identification of a Permissive Epitope Insertion Site in the Vesicular Stomatitis Virus Glycoprotein." Journal of Virology 78, no. 10 (2004): 5079–87. http://dx.doi.org/10.1128/jvi.78.10.5079-5087.2004.

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ABSTRACT We developed a rational approach to identify a site in the vesicular stomatitis virus (VSV) glycoprotein (G) that is exposed on the protein surface and tolerant of foreign epitope insertion. The foreign epitope inserted was the six-amino-acid sequence ELDKWA, a sequence in a neutralizing epitope from human immunodeficiency virus type 1. This sequence was inserted into six sites within the VSV G protein (Indiana serotype). Four sites were selected based on hydrophilicity and high sequence variability identified by sequence comparison with other vesiculovirus G proteins. The site showin

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Bergmann, J. E., and P. J. Fusco. "The M protein of vesicular stomatitis virus associates specifically with the basolateral membranes of polarized epithelial cells independently of the G protein." Journal of Cell Biology 107, no. 5 (1988): 1707–15. http://dx.doi.org/10.1083/jcb.107.5.1707.

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Using monoclonal antibodies and indirect immunofluorescence microscopy, we investigated the distribution of the M protein in situ in vesicular stomatitis virus-(VSV) infected MDCK cells. M protein was observed free in the cytoplasm and associated with the plasma membrane. Using the ts045 mutant of VSV to uncouple the synthesis and transport of the VSV G protein we demonstrated that this distribution was not related to the presence of G protein on the cell surface. Sections of epon-embedded infected cells labeled with antibody to the M protein and processed for indirect horseradish peroxidase i

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Anderson, Dina B., Sylvie Laquerre, William F. Goins, Justus B. Cohen, and Joseph C. Glorioso. "Pseudotyping of Glycoprotein D-Deficient Herpes Simplex Virus Type 1 with Vesicular Stomatitis Virus Glycoprotein G Enables Mutant Virus Attachment and Entry." Journal of Virology 74, no. 5 (2000): 2481–87. http://dx.doi.org/10.1128/jvi.74.5.2481-2487.2000.

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ABSTRACT The use of herpes simplex virus (HSV) vectors for in vivo gene therapy will require the targeting of vector infection to specific cell types in certain in vivo applications. Because HSV glycoprotein D (gD) imparts a broad host range for viral infection through recognition of ubiquitous host cell receptors, vector targeting will require the manipulation of gD to provide new cell recognition specificities in a manner designed to preserve gD's essential role in virus entry. In this study, we have determined whether an entry-incompetent HSV mutant with deletions of all Us glycoproteins, i

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Rubinstein, Menachem. "Is Lgr4 essential for VSV– and VSV-G–pseudotyped lentiviral vector entry to cells?" Journal of Biological Chemistry 293, no. 1 (2018): 112. http://dx.doi.org/10.1074/jbc.l117.000471.

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Betancourt, Dillon, Juan Carlos Ramos, and Glen N. Barber. "Retargeting Oncolytic Vesicular Stomatitis Virus to Human T-Cell Lymphotropic Virus Type 1-Associated Adult T-Cell Leukemia." Journal of Virology 89, no. 23 (2015): 11786–800. http://dx.doi.org/10.1128/jvi.01356-15.

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ABSTRACTAdult T cell leukemia/lymphoma (ATL) is an aggressive cancer of CD4/CD25+T lymphocytes, the etiological agent of which is human T-cell lymphotropic virus type 1 (HTLV-1). ATL is highly refractory to current therapies, making the development of new treatments a high priority. Oncolytic viruses such as vesicular stomatitis virus (VSV) are being considered as anticancer agents since they readily infect transformed cells compared to normal cells, the former appearing to exhibit defective innate immune responses. Here, we have evaluated the efficacy and safety of a recombinant VSV that has

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Publicover, Jean, Elizabeth Ramsburg, and John K. Rose. "A Single-Cycle Vaccine Vector Based on Vesicular Stomatitis Virus Can Induce Immune Responses Comparable to Those Generated by a Replication-Competent Vector." Journal of Virology 79, no. 21 (2005): 13231–38. http://dx.doi.org/10.1128/jvi.79.21.13231-13238.2005.

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ABSTRACT Live attenuated vaccine vectors based on recombinant vesicular stomatitis virus (VSV) are effective in several viral disease models. In this study, we asked if a VSV vector capable of only a single cycle of replication might be an effective alternative to replication-competent VSV vectors. We compared the cellular immune responses to human immunodeficiency virus (HIV) envelope protein (Env) expressed by replication-competent and single-cycle VSV vectors and also examined the antibody response to Env. The single-cycle vector was grown by complementation with VSV G protein and then test

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Barquero, Andrea A., Laura E. Alché, and Celia E. Coto. "Block of vesicular stomatitis virus endocytic and exocytic pathways by 1-cinnamoyl-3,11-dihydroxymeliacarpin, a tetranortriterpenoid of natural origin." Journal of General Virology 85, no. 2 (2004): 483–93. http://dx.doi.org/10.1099/vir.0.19343-0.

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Previously, it has been shown that 1-cinnamoyl-3,11-dihydroxymeliacarpin (CDM), a natural compound isolated from leaf extracts of Melia azedarach L., inhibits the vesicular stomatitis virus (VSV) multiplication cycle when added before or after infection. Here, we have established that the lack of VSV protein synthesis in CDM pre-treated Vero cells is ascribed to the inhibition of an initial step during virus multiplication, although indirect immunofluorescence (IFI) studies confirmed that the binding and uptake of [35S]methionine-labelled VSV was not affected by CDM pre-treatment. Instead, our

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Swinteck, B. Dancho, and Douglas S. Lyles. "Plasma Membrane Microdomains Containing Vesicular Stomatitis Virus M Protein Are Separate from Microdomains Containing G Protein and Nucleocapsids." Journal of Virology 82, no. 11 (2008): 5536–47. http://dx.doi.org/10.1128/jvi.02407-07.

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ABSTRACT Immunogold electron microscopy and analysis were used to determine the organization of the major structural proteins of vesicular stomatitis virus (VSV) during virus assembly. We determined that matrix protein (M protein) partitions into plasma membrane microdomains in VSV-infected cells as well as in transfected cells expressing M protein. The sizes of the M-protein-containing microdomains outside the virus budding sites (50 to 100 nm) were smaller than those at sites of virus budding (approximately 560 nm). Glycoprotein (G protein) and M protein microdomains were not colocalized in

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Reiss, Carol S., Steve S. L. Chen, Alice S. Huang, and Richard Doherty. "VSV G protein induces murine cytolytic T lymphocytes." Microbial Pathogenesis 1, no. 3 (1986): 261–67. http://dx.doi.org/10.1016/0882-4010(86)90050-1.

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Okuma, Kazu, Yoshiharu Matsuura, Hironobu Tatsuo, et al. "Analysis of the molecules involved in human T-cell leukaemia virus type 1 entry by a vesicular stomatitis virus pseudotype bearing its envelope glycoproteins." Journal of General Virology 82, no. 4 (2001): 821–30. http://dx.doi.org/10.1099/0022-1317-82-4-821.

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Cellular entry of human T-cell leukaemia virus type 1 (HTLV-1) was studied by a quantitative assay system using vesicular stomatitis virus (VSV) pseudotypes in which a recombinant VSV (VSVΔG*) containing the gene for green fluorescent protein instead of the VSV G protein gene was complemented with viral envelope glycoproteins in trans. Most of the cell lines tested showed susceptibility to VSVΔG* complemented with either HTLV-1 envelope glycoproteins (VSVΔG*-Env) or VSV G protein (VSVΔG*-G), but not to VSVΔG* alone, indicating that cell-free HTLV-1 could infect many cell types from several spe

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Zhang, Xian-Yang, Vincent F. La Russa, and Jakob Reiser. "Transduction of Bone-Marrow-Derived Mesenchymal Stem Cells by Using Lentivirus Vectors Pseudotyped with Modified RD114 Envelope Glycoproteins." Journal of Virology 78, no. 3 (2004): 1219–29. http://dx.doi.org/10.1128/jvi.78.3.1219-1229.2004.

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ABSTRACT Bone-marrow-derived mesenchymal stem cells (MSCs) have attracted considerable attention as tools for the systemic delivery of therapeutic proteins in vivo, and the ability to efficiently transfer genes of interest into such cells would create a number of therapeutic opportunities. We have designed and tested a series of human immunodeficiency virus type 1 (HIV-1)-based vectors and vectors based on the oncogenic murine stem cell virus to deliver and express transgenes in human MSCs. These vectors were pseudotyped with either the vesicular stomatitis virus G (VSV-G) glycoprotein (GP) or

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Abe, Akihiro, Shin-Tai Chen, Atsushi Miyanohara, and Theodore Friedmann. "In Vitro Cell-Free Conversion of Noninfectious Moloney Retrovirus Particles to an Infectious Form by the Addition of the Vesicular Stomatitis Virus Surrogate Envelope G Protein." Journal of Virology 72, no. 8 (1998): 6356–61. http://dx.doi.org/10.1128/jvi.72.8.6356-6361.1998.

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ABSTRACT In the absence of envelope gene expression, retrovirus packaging cell lines expressing Moloney murine leukemia virus (MLV)gag and pol genes produce large amounts of noninfectious virus-like particles that contain reverse transcriptase, processed Gag protein, and viral RNA (gag-pol RNA particles). We demonstrate that these particles can be made infectious in an in vitro, cell-free system by the addition of a surrogate envelope protein, the G spike glycoprotein of vesicular stomatitis virus (VSV-G). The appearance of infectivity is accompanied by physical association of the G protein wi

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Rahmeh, Amal A., Jianrong Li, Philip J. Kranzusch, and Sean P. J. Whelan. "Ribose 2′-O Methylation of the Vesicular Stomatitis Virus mRNA Cap Precedes and Facilitates Subsequent Guanine-N-7 Methylation by the Large Polymerase Protein." Journal of Virology 83, no. 21 (2009): 11043–50. http://dx.doi.org/10.1128/jvi.01426-09.

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ABSTRACT During conventional mRNA cap formation, two separate methyltransferases sequentially modify the cap structure, first at the guanine-N-7 (G-N-7) position and subsequently at the ribose 2′-O position. For vesicular stomatitis virus (VSV), a prototype of the nonsegmented negative-strand RNA viruses, the two methylase activities share a binding site for the methyl donor S-adenosyl-l-methionine and are inhibited by individual amino acid substitutions within the C-terminal domain of the large (L) polymerase protein. This led to the suggestion that a single methylase domain functions for bot

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Luo, Yumei, Detu Zhu, Dang Hoang Lam, et al. "A Double-Switch Cell Fusion-Inducible Transgene Expression System for Neural Stem Cell-Based Antiglioma Gene Therapy." Stem Cells International 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/649080.

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Recent progress in neural stem cell- (NSC-) based tumor-targeted gene therapy showed that NSC vectors expressing an artificially engineered viral fusogenic protein, VSV-G H162R, could cause tumor cell death specifically under acidic tumor microenvironment by syncytia formation; however, the killing efficiency still had much room to improve. In the view that coexpression of another antitumoral gene with VSV-G can augment the bystander effect, a synthetic regulatory system that triggers transgene expression in a cell fusion-inducible manner has been proposed. Here we have developed a double-swit

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Boritz, Eli, Jennifer Gerlach, J. Erik Johnson, and John K. Rose. "Replication-Competent Rhabdoviruses with Human Immunodeficiency Virus Type 1 Coats and Green Fluorescent Protein: Entry by a pH-Independent Pathway." Journal of Virology 73, no. 8 (1999): 6937–45. http://dx.doi.org/10.1128/jvi.73.8.6937-6945.1999.

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ABSTRACT We describe a replication-competent, recombinant vesicular stomatitis virus (VSV) in which the gene encoding the single transmembrane glycoprotein (G) was deleted and replaced by anenv-G hybrid gene encoding the extracellular and transmembrane domains of a human immunodeficiency virus type 1 (HIV-1) envelope protein fused to the cytoplasmic domain of VSV G. An additional gene encoding a green fluorescent protein was added to permit rapid detection of infection. This novel surrogate virus infected and propagated on cells expressing the HIV receptor CD4 and coreceptor CXCR4. Infection w

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Shinozaki, Katsunori, Oliver Ebert, Arief Suriawinata, Swan N. Thung, and Savio L. C. Woo. "Prophylactic Alpha Interferon Treatment Increases the Therapeutic Index of Oncolytic Vesicular Stomatitis Virus Virotherapy for Advanced Hepatocellular Carcinoma in Immune-Competent Rats." Journal of Virology 79, no. 21 (2005): 13705–13. http://dx.doi.org/10.1128/jvi.79.21.13705-13713.2005.

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ABSTRACT Vesicular stomatitis virus (VSV) is a negative-strand RNA virus with intrinsic oncolytic specificity due to substantially attenuated antiviral responses in many tumors. We have recently reported that recombinant VSV vector can be used as an effective oncolytic agent to safely treat multifocal hepatocellular carcinoma (HCC) in the livers of immune-competent rats via hepatic artery infusion. When administered at doses above the maximum tolerated dose (MTD), however, the animals suffered from neurotoxicity and/or acute lethal hepatotoxicity. Since VSV is extremely sensitive to the antivi

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Roberts, Anjeanette, Linda Buonocore, Ryan Price, John Forman, and John K. Rose. "Attenuated Vesicular Stomatitis Viruses as Vaccine Vectors." Journal of Virology 73, no. 5 (1999): 3723–32. http://dx.doi.org/10.1128/jvi.73.5.3723-3732.1999.

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ABSTRACT We showed previously that a single intranasal vaccination of mice with a recombinant vesicular stomatitis virus (VSV) expressing an influenza virus hemagglutinin (HA) protein provided complete protection from lethal challenge with influenza virus (A. Roberts, E. Kretzschmar, A. S. Perkins, J. Forman, R. Price, L. Buonocore, Y. Kawaoka, and J. K. Rose, J. Virol. 72:4704–4711, 1998). Because some pathogenesis was associated with the vector itself, in the present study we generated new VSV vectors expressing HA which are completely attenuated for pathogenesis in the mouse model. The firs

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Robison, Clinton S., and Michael A. Whitt. "The Membrane-Proximal Stem Region of Vesicular Stomatitis Virus G Protein Confers Efficient Virus Assembly." Journal of Virology 74, no. 5 (2000): 2239–46. http://dx.doi.org/10.1128/jvi.74.5.2239-2246.2000.

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ABSTRACT In this report, we show that the glycoprotein of vesicular stomatitis virus (VSV G) contains within its extracellular membrane-proximal stem (GS) a domain that is required for efficient VSV budding. To determine a minimal sequence in GS that provides for high-level virus assembly, we have generated a series of recombinant ΔG-VSVs which express chimeric glycoproteins having truncated stem sequences. The recombinant viruses having chimeras with 12 or more membrane-proximal residues of the G stem, and including the G protein transmembrane-cytoplasmic tail domains, produced near-wild-type

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Fernandez-Sesma, Ana, Richard W. Peluso, Xu Bai, Jerome L. Schulman, David E. Levy, and Thomas M. Moran. "Superantigen-Activated T Cells Redirected by a Bispecific Antibody Inhibit Vesicular Stomatitis Virus Replication In Vitro and In Vivo." Journal of Immunology 160, no. 4 (1998): 1841–49. http://dx.doi.org/10.4049/jimmunol.160.4.1841.

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Abstract A bispecific Ab (BsAb) that binds the TCR on T cells and the G protein of the vesicular stomatitis virus (VSV) can redirect staphylococcal enterotoxin B (SEB)-activated T cells to kill VSV-infected cells and to inhibit VSV replication in vitro. Inhibition of virus replication in our system is dependent upon the specificity of the Ab for the viral protein. IFN-γ does not play a very important role in this phenomenon, which is mainly mediated by the release of Pfp from CD8+ T cells. We have used a Stat1 knockout mouse model in which VSV infection is lethal. Infusion of staphylococcal en

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Tisdale, E. J., J. R. Bourne, R. Khosravi-Far, C. J. Der, and W. E. Balch. "GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex." Journal of Cell Biology 119, no. 4 (1992): 749–61. http://dx.doi.org/10.1083/jcb.119.4.749.

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We have examined the role of ras-related rab proteins in transport from the ER to the Golgi complex in vivo using a vaccinia recombinant T7 RNA polymerase virus to express site-directed rab mutants. These mutations are within highly conserved domains involved in guanine nucleotide binding and hydrolysis found in ras and all members of the ras superfamily. Substitutions in the GTP-binding domains of rab1a and rab1b (equivalent to the ras 17N and 116I mutants) resulted in proteins which were potent trans dominant inhibitors of vesicular stomatitis virus glycoprotein (VSV-G protein) transport bet

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Ikonen, E., R. G. Parton, F. Lafont, and K. Simons. "Analysis of the role of p200-containing vesicles in post-Golgi traffic." Molecular Biology of the Cell 7, no. 6 (1996): 961–74. http://dx.doi.org/10.1091/mbc.7.6.961.

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p200 is a cytoplasmic protein that associates with vesicles budding from the trans-golgi network (TGN). The protein was identified by a monoclonal antibody AD7. We have used this antibody to analyze whether p200 functions in exocytic transport from the TGN to the apical or basolateral plasma membrane in Madin-Darby canine kidney cells. We found that transport of the viral marker proteins, influenza hemagglutinin (HA) to the apical surface or vesicular stomatitis virus glycoprotein (VSV G) to the basolateral surface in streptolysin O-permeabilized cells was not affected when p200 was depleted f

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Oomens, Antonius G. P., Kevin P. Bevis, and Gail W. Wertz. "The Cytoplasmic Tail of the Human Respiratory Syncytial Virus F Protein Plays Critical Roles in Cellular Localization of the F Protein and Infectious Progeny Production." Journal of Virology 80, no. 21 (2006): 10465–77. http://dx.doi.org/10.1128/jvi.01439-06.

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ABSTRACT The importance of the F protein cytoplasmic tail (CT) for replication of human respiratory syncytial virus (HRSV) was examined by monitoring the behavior of viruses expressing F proteins with a modified COOH terminus. The F protein mutant viruses were recovered and amplified under conditions where F protein function was complemented by expression of a heterologous viral envelope protein. The effect of the F protein modifications was then examined in the context of a viral infection in standard cell types (Vero and HEp-2). The F protein modifications consisted of a deletion of the pred

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Sharma, Sanjai, Atsushi Miyanohara, and Theodore Friedmann. "Separable Mechanisms of Attachment and Cell Uptake during Retrovirus Infection." Journal of Virology 74, no. 22 (2000): 10790–95. http://dx.doi.org/10.1128/jvi.74.22.10790-10795.2000.

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ABSTRACT In the absence of viral envelope gene expression, cells expressing human immunodeficiency virus type 1 (HIV-1) gag andpol, accessory HIV functions, and a vector genome RNA produce and secrete large amount of noninfectious virus-like particles (VLPs) into the conditioned medium. After partial purification, such HIV-1 VLPs can be made infectious in cell-free conditions in vitro by complex formation with lipofection reagents or with the G protein of vesicular stomatitis virus (VSV-G). The resulting in vitro-modified HIV-1 particles are able to infect nondividing cells. Infectivity of env

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Ang, Agnes Lee, Tomohiko Taguchi, Stephen Francis, et al. "Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells." Journal of Cell Biology 167, no. 3 (2004): 531–43. http://dx.doi.org/10.1083/jcb.200408165.

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The AP-1B clathrin adaptor complex is responsible for the polarized transport of many basolateral membrane proteins in epithelial cells. Localization of AP-1B to recycling endosomes (REs) along with other components (exocyst subunits and Rab8) involved in AP-1B–dependent transport suggested that RE might be an intermediate between the Golgi and the plasma membrane. Although the involvement of endosomes in the secretory pathway has long been suspected, we now present direct evidence using four independent methods that REs play a role in basolateral transport in MDCK cells. Newly synthesized AP-

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Farr, Glen A., Michael Hull, Ira Mellman, and Michael J. Caplan. "Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells." Journal of Cell Biology 186, no. 2 (2009): 269–82. http://dx.doi.org/10.1083/jcb.200901021.

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Newly synthesized apical and basolateral membrane proteins are sorted from one another in polarized epithelial cells. The trans-Golgi network participates in this sorting process, but some basolateral proteins travel from the Golgi to recycling endosomes (REs) before their surface delivery. Using a novel system for pulse–chase microscopy, we have visualized the postsynthetic route pursued by a newly synthesized cohort of Na,K-ATPase. We find that the basolateral delivery of newly synthesized Na,K-ATPase occurs via a pathway distinct from that pursued by the vesicular stomatitis virus G protein

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