Vesicular stomatitis virus envelope glycoprotein alterations induced by host cell transformation

Moyer, Sue A.; Summers, Donald F.

doi:10.1016/0092-8674(74)90009-9

Cited by 47 publications

(23 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, it is reasonable to assume that bound carbohydrates are also modified by host cell transformation. Experimental eVIdence in accordance with this expectation has been presented by several laboratories (7,12,16). What is important in transformation might not be anyone specific change of the carbohydrate array but an imbalance of groups resulting from a number of combinations of changes (25).…”

Section: Discussionsupporting

confidence: 55%

“…Enveloped RNA viruses mature at the cell surface and are coated with host cell membrane modified by viral infection. Expectation that viral envelopes are modified by host cell transformation and reflect some properties of transformed cell membrane was experimentally supported by studies on avian oncovirus (12,14, IS), murine oncovirus (7), and VSV (IS, 16). Thus, as a model to study molecular changes accompanied by malignant transformation, the viral envelope seems to be a preferable material.…”

mentioning

confidence: 99%

“…Thus, as a model to study molecular changes accompanied by malignant transformation, the viral envelope seems to be a preferable material. The glycopeptides of VSV have been shown to be altered in polyoma virus-transformed hamster cells (16). The present study investigated whether cell transformation results in an alteration of electrochemical properties of the envelope glycoprotein of VSV, one of the most productive and well characterized enveloped RNA viruses.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Electrochemical Modification of Vesicular Stomatitis Virus Glycoprotein by‐Host Cell Transformation

Miki

1981

Microbiology and Immunology

View full text Add to dashboard Cite

Electrochemical properties of the glycoprotein of vesicular stomatitis virus (VSV) grown in Rous sarcoma virus (RSV)-transformed cells was compared with that of its counterpart grown in nontransformed cells. In DEAE-Sephadex column chromatography, the glycoproteins of VSV derived from transformed cells appeared more heterogeneous and had a tendency to elute with higher concentrations of NaCI than those from nontransformed cells. In isoelectric focussing, the glycoproteins of VSVs derived from transformed and nontransformed cells appeared as multiple components differing in the isoelectric point, and the glycoproteins from virus from transformed cells had isoelectric points that were more acidic than their counterparts from nontransformed cells. These results show that the glycoprotein of VSV consists of populations of molecules differing in charge and their isoelectric points were shifted to the acidic side by host cell transformation.Viral transformation of cells accompanies functional, biochemical, and morphological changes in the cell membrane. The differences have been also observed in the carbohydrates attached to lipids (3,8,22) and to proteins (25) in the membranes of normal and malignant cells. Enveloped RNA viruses mature at the cell surface and are coated with host cell membrane modified by viral infection. Expectation that viral envelopes are modified by host cell transformation and reflect some properties of transformed cell membrane was experimentally supported by studies on avian oncovirus (12, 14, IS), murine oncovirus (7), and VSV (IS, 16). Thus, as a model to study molecular changes accompanied by malignant transformation, the viral envelope seems to be a preferable material. The glycopeptides of VSV have been shown to be altered in polyoma virus-transformed hamster cells (16). The present study investigated whether cell transformation results in an alteration of electrochemical properties of the envelope glycoprotein of VSV, one of the most productive and well characterized enveloped RNA viruses.

show abstract

Section: Discussionsupporting

confidence: 55%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Electrochemical Modification of Vesicular Stomatitis Virus Glycoprotein by‐Host Cell Transformation

Miki

1981

Microbiology and Immunology

View full text Add to dashboard Cite

show abstract

“…The size and composition of the carbohydrate moieties per VSV glycoprotein are variable, depending upon the cell type in which the virions are grown (Burge and Huang, 1970; Etchison and Holland, 1974a). Likewise, the sequence of the carbohydrates within the glycosyl side-chains may exhibit cell depen-dence (Moyer and Summers, 1974). The monosaccharide composition of the oligosaccharide side-chains is similar to that of influenza virus (Etchison and Holland, 1974b), with the exception that sialic acid is present on the termini.…”

Section: Rhabdovirus G Proteinmentioning

confidence: 99%

Membrane Glycoproteins of Enveloped Viruses

Compans

Kemp

1978

Current Topics in Membranes and Transport

View full text Add to dashboard Cite

“…The envelope of a virus that infects a transformed cell retains some properties of the transformed cell membrane (Forchhamer & Turnock, 1978 ;Lai & Duesberg, 1972;Miki & Kuwata, 1976;Miki, 1980;Moyer & Summers, 1974). In this study Sindbis virus, one of the better qharacterized enveloped RNA viruses, was used as a model to study modifications of the cell membrane by host cell transformation.…”

Section: Introductionmentioning

confidence: 99%

Heterogeneity of Sindbis Virus Glycoprotein E1 and its Modification by Host Cell Transformation

Miki

1984

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYThe electrophoretic properties of glycoprotein E1 of Sindbis virus grown in Rous sarcoma virus-transformed cells were compared with those of Sindbis virus grown in untransformed cells. Isoelectric focusing in a gel containing 9-5 M-urea and 2~ Nonidet P40 indicated that the glycoprotein E1 of Sindbis virus from the untransformed cells was electrochemically heterogeneous and consisted of four components, whose isoelectric points (pIs) ranged from 6-2 to 6.7; the E1 of Sindbis virus from the transformed cells contained an additional component with a pI of 6.1. After treatment with neuraminidase the observed charge heterogeneity disappeared regardless of whether the virus had come from the transformed or the untransformed cells. The five components were digested with Pronase and compared by gel filtration on Bio-Gel P-6; the four components with relatively higher pls released high-mannose-type and complex-type oligosaccharides which differed in their content of sialic acid. In contrast, the pI 6-1 component, which existed only in the transformed cell-derived SV glycoprotein El, released only complex-type oligosaccharide. These results indicate that the properties of glycoprotein E1 derived from both cell types are basically similar but that a small proportion of the E1 molecules from the transformed cells, with carbohydrate chains elongated by attachment of sialic acid residues, lacks simple-type oligosaccharides either because they are not attached or because they have been processed to the complex type. Glycoprotein E 2 appeared as at least three components in nonequilibrium pH gradient electrophoresis. However, no significant difference was observed between the cell types.

show abstract

Vesicular stomatitis virus envelope glycoprotein alterations induced by host cell transformation

Cited by 47 publications

References 35 publications

Electrochemical Modification of Vesicular Stomatitis Virus Glycoprotein by‐Host Cell Transformation

Electrochemical Modification of Vesicular Stomatitis Virus Glycoprotein by‐Host Cell Transformation

Membrane Glycoproteins of Enveloped Viruses

Heterogeneity of Sindbis Virus Glycoprotein E1 and its Modification by Host Cell Transformation

Contact Info

Product

Resources

About