Carbohydrate Composition of Vesicular Stomatitis Virus

McSharry, James J.; Wagner, Robert R.

doi:10.1128/jvi.7.3.412-415.1971

Cited by 50 publications

(21 citation statements)

References 9 publications

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“…The data can also be explained by viral incorporation of L-cell-type carbohydrates in the form of other glycoproteins or glycolipids which would allow for aggregation of cellular H-2 antigen. HeLa cell-grown virus has carbohydrates that reflect that of HeLa cells (3,17) and so would not aggregate L-cell glycoproteins. Work is now in progress to determine definitively whether VSV incorporates host glycoproteins into its viral envelope and to explore in depth the other possibilities mentioned.…”

Section: Discussionmentioning

confidence: 99%

“…It is at this site that the virus finally "buds" off from its host cell, forming an intact virion (5,9,18,25,30). It is believed that the protein components of the viral envelope are entirely virus-specific, whereas the lipid, glycolipid, and possibly the carbohydrate components are host specified (3,8,12,13,17). It is therefore important to establish the manner in which virus-specific envelope proteins are inserted into the preformed host cell membrane and also to follow the fate of host cell membrane protein molecules as virus proteins become associated with the host surface.…”

mentioning

confidence: 99%

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Effect of Vesicular Stomatitis Virus Infection on the Histocompatibility Antigen of L Cells

Hecht

Summers

1972

J Virol

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When mouse L cells are infected for 22 hr with vesicular stomatitis virus (VSV), a ribonucleic acid-containing enveloped virus, greater than 70% of the major histocompatibility antigen (H-2), is no longer detectable by the method of inhibition of immune cytolysis. Infected cells prelabeled with "4C-glucosamine also show a correspondingly greater loss of trichloroacetic acid-insoluble radioactivity than uninfected cells. The loss of H-2 antigenic activity is not due to the viral inhibition of host cell protein synthesis since cells cultured for 18 hr in the presence of cycloheximide have the same amount of H-2 activity as untreated controls. Also, cells infected with encephalomyocarditis virus, a picornavirus, show no loss of H-2 activity at a time when host cell protein synthesis is completely inhibited. VSV structural proteins associated in vitro with uninfected L-cell plasma membranes do not render H-2 sites inaccessible to the assay. Although antibodies may not combine with all the H-2 antigenic sites on the plasma membrane, anti-H-2 serum reacted with L cells before infection does not prevent a normal infection with VSV. H-2 activity can be detected in virus samples purified from the medium of infected L cells; this virus purified after being mixed with L-cell homogenates shows greater H-2 activity than virus purified after being mixed with HeLa cell homogenates. However, VSV made in HeLa cells shows no H-2 activity when mixed with L-cell homogenates.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Effect of Vesicular Stomatitis Virus Infection on the Histocompatibility Antigen of L Cells

Hecht

Summers

1972

J Virol

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“…The virion of vesicular stomatitis (VS) virus is composed of five polypeptide chains (10,12) in addition to ribonucleic acid and cell-derived lipids and glycolipids (6,8). One of the polypeptides is a glycoprotein (the G protein) which contains carbohydrate chains (1,9) and appears to comprise the spikes which protrude from the virion envelope (2,3,7). The glycoprotein can be removed selectively from the surface of the virion by proteolytic enzymes, resulting in loss of ininfectivity, apparently due to degradation of the virion glycoprotein (3,7).…”

mentioning

confidence: 99%

The Glycoprotein of Vesicular Stomatitis Virus Is the Antigen That Gives Rise to and Reacts with Neutralizing Antibody

Kelley

Emerson

Wagner

1972

J Virol

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215

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The glycoprotein, but no other virion protein, of vesicular stomatitis virus was solubilized by the nonionic detergent Triton X-100 in low ionic strength buffer. The solubilized viral glycoprotein induced the synthesis of antibody that formed a single precipitin line with the glycoprotein and that neutralized the infectivity of the virus. The neutralizing activity of the antibody was efficiently blocked by purified glycoprotein.

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“…Shape and size determination may also be controlled by viral proteins at various levels; nucleocapsids, M proteins, or glycoproteins could be the determining factor for different virus groups. The phenomenon of phenotypic mixing of envelope glycoproteins in cells doubly infected with VSV and the parainfluenza virus SV5 clearly demonstrates that the internal proteins and not the glycoproteins determine the particle size and shape of rhabdoviruses McSharry et al, 1971). This conclusion is supported by the observation that particles with the internal proteins of VSV possess the characteristic bullet shape of VSV while containing mixtures of envelope glycoproteins derived from VSV and SV5.…”

Section: Macromolecular Interactions In Membrane Assemblymentioning

confidence: 86%

“…The carbohydrates linked to the G protein of VSV have been studied in detail. The glycoprotein is 9-10% carbohydrate by weight and contains mannose, galactose, N-acetylglucosamine, and neuraminic acid as the major sugar components, with lesser amounts of N-acetylgalactosamine and fucose (McSharry and Wagner, 1971; Burge and Huang, 1970. Etchison and Holland, 1974a).…”

Section: Rhabdovirus G Proteinmentioning

confidence: 99%