Characterization of Membrane Components of the Erythrocyte Involved in Vesicular Stomatitis Virus Attachment and Fusion at Acidic pH

Mastromarino, Paola; Conti, Cinzia; Goldoni, Paola; Hauttecoeur, Bernard; Orsi, N

doi:10.1099/0022-1317-68-9-2359

Cited by 130 publications

(80 citation statements)

References 19 publications

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“…The results obtained by Mastromarino et al (31) using erythrocytes at acidic pH showed that, besides PS, phosphatidylinositol and GM3 ganglioside also inhibited VSV attachment to cells. Removal of the charged groups from these negatively charged molecules greatly reduced their inhibitory activities, suggesting an important role of electrostatic interactions during cell recognition by VSV.…”

Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 81%

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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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Section: Rhabdovirus Binding To the Cell Surfacementioning

confidence: 81%

“…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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“…As linkage to CS-BoTIM/B did not abolish the viral tropism for muscle cells, the gain in neurotropism could reflect the cooperative binding of targeted lentivirus to the BoNT/B neuronal ecto-acceptor along with vesicular stomatitis virus glycoprotein interaction with phospholipids in the cell membrane. 35 Such a simple mechanism could also explain the enhanced transduction of the CS-BoTIM/B-targeted GFP vector to intramural ganglionic neurons in vivo. Unlike the non-targeted lentivirus, which is more likely to dissipate through systemic clearance from the interstitial tissue of the tracheal wall after injection and yield indiscriminate GFP expression at the SI, the CS-BoTIM/B-linked lentivirus would tend to remain longer in the tissue because of its high-affinity binding to neurons, thereby amplifying production therein of the reporter.…”

Section: Activity Dependence and Selectivity Of Cs-botim/b Entry Intomentioning

confidence: 99%

Innocuous full-length botulinum neurotoxin targets and promotes the expression of lentiviral vectors in central and autonomic neurons

et al. 2011

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Fragments of botulinum neurotoxin (BoNT) have been explored as potential targeting moieties and carriers of biomolecules into neurons, although with lower binding and translocation efficiency compared with intact proteins. This study exploits a detoxified recombinant form of full-length BoNT/B (BoTIM/B) fused with core streptavidin (CS-BoTIM/B) for lentiviral targeting to central and autonomic neurons. CS-BoTIM/B underwent an activity-dependent entry into cultured spinal cord neurons. Coupling CS-BoTIM/B to biotinylated lentivirus-encoding green fluorescent protein (GFP) endowed considerable neuron selectivity to the vector as evident from the preferential expression of the reporter in neurons co-cultured with skeletal muscle cells. CS-BoTIM/ B-guided lentiviral transduction with the expression of a SNARE protein, SNAP-25 (S25), rendered non-susceptible to proteolysis by three BoNT serotypes, yielded a sizable decrease in cleaved S25 upon exposure of spinal cord neurons to these toxins. This was accompanied by synaptic transmission being spared from blockade by BoNT/A or BoNT/E, reflecting adequate translation and functional competence of recombinant multi-toxin-resistant S25. The augmented neurotropism conveyed on the lentivirus by CS-BoTIM/B was also demonstrated in vivo through enhanced expression of a reporter in intramural ganglionic neurons in the rat trachea, after injection of the targeted GFP-encoding lentivirus. Thus, a novel and realistic prospect for gene therapy of peripheral neuropathies is offered in this study through lentiviral targeting to neurons by CS-BoTIM/B.

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“…As the VSV-G envelope is thought to bind to cell surface phospholipids, 27,28 VSV-G -pseudotyped lentivirus vectors have a potential advantage over adenovirus serotype 5 -based vectors in their ability to achieve efficient gene delivery to cancer cells even if they lack specific cell surface proteins that normally act as receptors for virus entry. Furthermore, another advantage of lentivirus vectors is their potential to achieve stable integration and long -term expression of delivered transgenes.…”

Section: Autocrine Inhibition Of Endothelial Cell Growth By Direct Trmentioning

confidence: 99%

Development of lentiviral vectors for antiangiogenic gene delivery

et al. 2001

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Growth and metastasis of malignant tumors requires angiogenesis. Inhibition of tumor -induced angiogenesis may represent an effective cytostatic strategy. We have constructed recombinant self -inactivating lentiviral vectors expressing angiostatin and endostatin, and have tested their antiangiogenic activities. As VSV -G -pseudotyped lentiviral vectors showed low relative transduction titers on bovine aortic and human umbilical vein endothelial cells, it was difficult to achieve significant inhibition of endothelial cell growth by lentivirus -mediated antiangiogenic gene transfer directly to endothelial cells without concomitant vector -associated cytotoxicity. However, lentivirus vectors could efficiently and stably transduce T24 human bladder cancer cells that are relatively resistant to adenovirus infection due to loss of coxsackievirus -adenovirus receptor expression. Long -term expression and secretion of angiostatin and endostatin from lentivirus -transduced T24 cells resulted in significant inhibition of cellular proliferation on coculture with endothelial cells. This report represents the first use of lentivirus -based vectors to deliver the antiangiogenic factors, angiostatin and endostatin, and suggests the potential utility of antiangiogenic gene therapy with lentiviral vectors for the treatment of cancer. Cancer Gene Therapy ( 2001 ) 8, 879 -889

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Characterization of Membrane Components of the Erythrocyte Involved in Vesicular Stomatitis Virus Attachment and Fusion at Acidic pH

Cited by 130 publications

References 19 publications

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

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

Innocuous full-length botulinum neurotoxin targets and promotes the expression of lentiviral vectors in central and autonomic neurons

Development of lentiviral vectors for antiangiogenic gene delivery

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