Characterization of rat brain cellular membrane components acting as receptors for vesicular stomatitis virus

Conti, Cinzia; Mastromarino, Paola; Ciuffarella, M. G.; Orsi, N

doi:10.1007/bf01311075

Cited by 13 publications

(7 citation statements)

References 20 publications

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“…Reinfection with retroviruses is usually inhibited in retrovirus producer cells by the high intracellular levels of the retrovirus envelope protein which saturates the retroviral receptor. The receptor for VSV may include phosphatidyl serine, phosphatidyl inositol, and/or GM3 ganglioside (25,26), all of which are abundant components of plasma membrane. The abundance of these molecules may prevent receptor saturation, thereby allowing reinfection to occur.…”

Section: Discussionmentioning

confidence: 99%

Generation of packaging cell lines for pseudotyped retroviral vectors of the G protein of vesicular stomatitis virus by using a modified tetracycline inducible system.

Chen

Iida

Guo

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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We have previously shown that the G protein ofvesicular stomatitis virus (VSV-G) can be incorporated into the virions of retroviruses. Since expression of VSV-G is toxic to most mammalian cells, development of stable VSV-G packaging cell lines requires inducible VSV-G expression. We have modified the tetracycline-inducible system by fusing the ligand binding domain of the estrogen receptor to the carboxy terminus of a tetracycline-regulated transactivator. Using this system, we show that VSV-G expression is tetracyclinedependent and can be modulated by 18-estradiol. Stable packaging cell lines can readily be established and high-titer pseudotyped retroviral vectors can be generated upon induction of VSV-G expression.Retroviral vectors derived from Moloney murine leukemia virus have been used extensively to transduce genes into mammalian cells (1, 2). However, problems such as the inability to infect quiescent cells, low virus titers, and relatively poor infectivity in human cells severely limit the application of retroviral vectors in gene transfer. To overcome some of these problems, we have generated retroviral vectors pseudotyped with the G protein of vesicular stomatitis virus (VSV-G) (3-5). We have shown that the pseudotyped retroviral vectors have an expanded host range and are able to infect many cell types with a greater efficiency than traditional amphotropic retroviral vectors (3-6). Moreover, the pseudotyped virus can be concentrated by ultracentrifugation to titers greater than 109 colony forming units/ml (4). These unique properties of the VSV-G pseudotyped virus not only extend the use of retroviral vectors for genetic studies in previously inaccessible species, but also facilitate more efficient preclinical and clinical studies of the potential for human gene therapy.However, the generation of stable packaging cell lines for pseudotyped retroviral vectors has been difficult because of the toxicity of VSV-G in most mammalian cells (4, 5). To overcome this problem, we have modified the tetracyclineinducible system (7) to regulate the expression of VSV-G. In that system, a chimeric transcription factor, tTA, was produced by combining the repressor of Escherichia coli tetracyclineresistance operon (tetR) and the activation domain of virion protein 16 (VP16) of herpes simplex virus (HSV). This chimeric transactivator can regulate gene expression from a minimal promoter linked to multiple copies of tetO, the binding site for the tetracycline repressor. In the absence of tetracycline, tTA binds the tetO site and activates transcription from the tetO-containing promoter. In the presence of tetracycline, interaction of tTA with the tetO is prevented by its binding to tetracycline, thereby prevents transcription.While the expression of several genes has been reported to be inducible using this system (7-11), establishment of cell lines stably expressing tTA has been difficult, presumably because the activation domain of VP16 is capable of squelching general cellular transcription when expressed in l...

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Section: Discussionmentioning

confidence: 99%

Generation of packaging cell lines for pseudotyped retroviral vectors of the G protein of vesicular stomatitis virus by using a modified tetracycline inducible system.

Chen

Iida

Guo

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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“…Phospholipids from cellular membranes inhibit attachment and infection of rabies virus and VSV (30)(31)(32). Indeed, the VSV host range extends from nearly all mammals to insects, suggesting that the receptor for this virus is a widely distributed molecule.…”

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 99%

Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?

Poian

Carneiro

Stauffer

2005

Braz J Med Biol Res

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Enveloped viruses always gain entry into the cytoplasm by fusion of their lipid envelope with a cell membrane. Some enveloped viruses fuse directly with the host cell plasma membrane after virus binding to the cell receptor. Other enveloped viruses enter the cells by the endocytic pathway, and fusion depends on the acidification of the endosomal compartment. In both cases, virus-induced membrane fusion is triggered by conformational changes in viral envelope glycoproteins. Two different classes of viral fusion proteins have been described on the basis of their molecular architecture. Several structural data permitted the elucidation of the mechanisms of membrane fusion mediated by class I and class II fusion proteins. In this article, we review a number of results obtained by our laboratory and by others that suggest that the mechanisms involved in rhabdovirus fusion are different from those used by the two well-studied classes of viral glycoproteins. We focus our discussion on the electrostatic nature of virus binding and interaction with membranes, especially through phosphatidylserine, and on the reversibility of the conformational changes of the rhabdovirus glycoprotein involved in fusion. Taken together, these data suggest the existence of a third class of fusion proteins and support the idea that new insights should emerge from studies of membrane fusion mediated by the G protein of rhabdoviruses. In particular, the elucidation of the three-dimensional structure of the G protein or even of the fusion peptide at different pH's might provide valuable information for understanding the fusion mechanism of this new class of fusion proteins. Correspondence

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“…The HIV-GFP vector used here was pseudotyped with the VSVG envelope glycoprotein, which confers a broad tropism and increases vector particle stability (Escors and Breckpot, 2010), so it is not surprising that transduction in the hypothalamus is not restricted to neurons. While retroviral infection usually requires interaction between the viral envelope protein and specific receptors on the cell surface, VSVG interacts with phospholipids in the cell membrane to mediate fusion between the cell membrane and the viral envelope, enabling viral entry (Conti et al, 1988; Harrison, 2008; Mastromarino et al, 1987). The primary receptor used by adenoviral vectors is the coxsackie and adenovirus receptor (Bergelson et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Comparison of the efficacy of four viral vectors for transducing hypothalamic magnocellular neurosecretory neurons in the rat supraoptic nucleus

Doherty

Schaack

Sladek

2011

Journal of Neuroscience Methods

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Characterization of rat brain cellular membrane components acting as receptors for vesicular stomatitis virus

Cited by 13 publications

References 20 publications

Generation of packaging cell lines for pseudotyped retroviral vectors of the G protein of vesicular stomatitis virus by using a modified tetracycline inducible system.

Generation of packaging cell lines for pseudotyped retroviral vectors of the G protein of vesicular stomatitis virus by using a modified tetracycline inducible system.

Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?

Comparison of the efficacy of four viral vectors for transducing hypothalamic magnocellular neurosecretory neurons in the rat supraoptic nucleus

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