pH-dependent fusion between the Semliki Forest virus membrane and liposomes.

White, Judy; Helenius, Ari

doi:10.1073/pnas.77.6.3273

Cited by 322 publications

(234 citation statements)

References 22 publications

(14 reference statements)

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“…For example, liposomes were used to show that Semliki Forest virus fusion requires cholesterol in the target membrane (White & Helenius, 1980;Kielian & Helenius, 1984) and acidic pH to induce the fusion reaction White & Helenius, 1980). Stegmann et al (1985) used liposomes to show that the low pH-induced conformational change in the haemagglutinin (HA) protein, in itself, is not sufficient to trigger fusion activity.…”

Section: Discussionmentioning

confidence: 99%

“…For example, the requirement for cholesterol in Semliki Forest virus fusion with target membranes was shown by the use of liposomes (White & Helenius, 1980;Kielian & Helenius, 1984). Liposomes allow rigorous kinetic characterization of the fusion process (Nir et al, 1986a), enable the target composition to be manipulated to identify the dependence of viral fusion on target membrane lipids and incorporated receptors (Hsu et aL, 1983;Stegmann et al, 1985Stegmann et al, , 1989Klappe et al, 1986), and allow for the direct comparison of the fusion characteristics of different viruses.…”

Section: Introductionmentioning

confidence: 99%

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Fusion of simian immunodeficiency virus with liposomes and erythrocyte ghost membranes: effects of lipid composition, pH and calcium

Larsen

Alford²,

Young³

et al. 1990

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Fusion of simian immunodeficiency virus with liposomes and erythrocyte ghost membranes: effects of lipid composition, pH and calcium

Larsen

Alford²,

Young³

et al. 1990

Journal of General Virology

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“…After fusion the G proteins are oriented in the plasma membrane with their glycosylated portions towards the outside (46). The nucleocapsid, consisting of the viral RNA and associated proteins, is introduced into the cytoplasm.…”

Section: Implantation Of the Vsv G Protein By Fusionmentioning

confidence: 99%

Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin-Darby canine kidney cells. I. Morphological evidence.

Matlin¹,

Bainton²,

Pesonen³

et al. 1983

The Journal of Cell Biology

104

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The G protein of vesicular stomatitis virus was implanted in the apical plasma membrane of Madin-Darby canine kidney cells by low pH-dependent fusion of the viral envelope with the cellular membrane. The amount of fusion as determined by removal of unfused virions, either by tryptic digestion or by EDTA treatment at 0°C, was 22-24% of the cell-bound virus radioactivity. Upon incubation of cells after implantation, the amount of G protein as detected by immunofluorescence diminished on the apical membrane and appeared within 30 min on the basolateral membrane. At the same time some G protein fluorescence was also seen in intracellular vacuoles. The observations by immunofluorescence were confirmed and extended by electron microscopy. Using immunoperoxidase localization, G protein was seen to move into irregularly shaped vacuoles (endosomes) and multivesicular bodies and to appear on the basolateral plasma membrane. These results suggest that the apical and basolateral domains of Madin-Darby canine kidney cells are connected by an intracellular route.In most cells the plasma membrane is continuously endocytosed (36) and the loss of surface membrane must be balanced by retrieval of membrane from inside the cell. Membrane recycling poses a special problem in epithelial cells because the plasma membrane is polarized; it is divided into apical and basolateral domains with distinct protein and lipid compositions (35). If the plasma membrane is continuously recycling, an important question is how the apical and basolateral domains preserve their unique compositions. If the apical and the basolateral recycling routes are separated, randomization of the cell surface would of course be prevented. If, however, they connect at some point in the cell, continuous sorting of apical and basolateral proteins would have to take place.In an attempt to map the membrane traffic routes to and from the cell surface in epithelial cells, we are using the MadinDarby canine kidney (MDCK) cell line as our experimental system (7, 16). These cells display both structural and functional polarity when grown in culture (24, 32). The microvillar

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“…These viruses enter cells by adsorptive endocytosis, and the release of their nucleocapsids into the cytosol is facilitated by low pH (6 or slightly below) (51,52). This release can be blocked by amines or monensin, and the block can be overcome by exposure of cells to a low-pH environment, in a manner analogous to overcoming resistance to diphtheria toxin (19,29,52 The evidence provided by these studies indicates that neither the toxins nor the viruses that we have studied require exposure to the lysosomal compartment for their active component to enter the cytosol.…”

mentioning

confidence: 99%

“…In recent years there has been increasing evidence that although diphtheria toxin is a protein foreign to mammalian cells, it shares a common route of entry into sensitive target cells with physiologically important proteins like lowdensity lipoprotein (1), a2-macroglobulin (53), hormones (3,30), growth factors (15,16), and also some viruses (19,51). Diphtheria toxin binds, through its B fragment (50), to specific receptors on the cell surface and then enters the cell in endocytic vesicles (12,14).…”

mentioning

confidence: 99%

Binding and uptake of diphtheria toxin by toxin-resistant Chinese hamster ovary and mouse cells.

Didsbury¹,

Moehring²,

Moehring³

1983

Mol. Cell. Biol.

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We investigated two phenotypically distinct types of diphtheria toxin-resistant mutants of Chinese hamster cells and compared their resistance with that of naturally resistant mouse cells. All are resistant due to a defect in the process of internalization and delivery of toxin to its target in the cytosol, elongation factor 2. By cell hybridization studies, analysis of cross-resistance, and determination of specific binding sites for 125I-labeled diphtheria toxin, we showed that these cell strains fall into two distinct complementation groups. The Dipr group encompasses Chinese hamster strains that are resistant only to diphtheria toxin, as well as mouse LM cells. These strains possess a normal complement of high-affinity binding sites for diphtheria toxin, but these receptors are unable to deliver active toxin fragment A to the cytosol. Cells of the DPVr group have a broader spectrum of resistance, including Pseudomonas exotoxin A and several enveloped viruses as well as diphtheria toxin. In these studies, which investigate the resistance of these cells to diphtheria toxin, we demonstrate that they possess a reduced number of specific binding sites for this toxin and behave, phenotypically, like cells treated with the proton ionophore monensin. Their resistance is related to a defect in a mechanism required for release of active toxin from the endocytic vesicle.

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pH-dependent fusion between the Semliki Forest virus membrane and liposomes.

Cited by 322 publications

References 22 publications

Fusion of simian immunodeficiency virus with liposomes and erythrocyte ghost membranes: effects of lipid composition, pH and calcium

Fusion of simian immunodeficiency virus with liposomes and erythrocyte ghost membranes: effects of lipid composition, pH and calcium

Transepithelial transport of a viral membrane glycoprotein implanted into the apical plasma membrane of Madin-Darby canine kidney cells. I. Morphological evidence.

Binding and uptake of diphtheria toxin by toxin-resistant Chinese hamster ovary and mouse cells.

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