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Vesicular stomatitis virus G protein

Cannon, K. S., Hebert, D. N., and Helenius, A. (1996). Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin. J. Biol. Chem. 271, 14280-14284. [Pg.340]

Tabas, I., Schlesinger, S. Komfeld, S. (1978) Processing of High Mannose Oligosaccharides to Form Complex Type Oligosaccharides on the Newly Synthesised Polypeptides of the Vesicular Stomatitis Virus G Protein and the IgG Heavy Chain , Journal of Biological Chemistry, 253, 716-22... [Pg.337]

Atkinson, P. H., and J. T. Lee, Co-translational excision of a-glucose and a-mannose in nascent vesicular stomatitis virus G protein, J. Cell Biol, 1984, 98, 2245-2249. [Pg.1234]

Kang MS, Elbein AD. Alterations in the structure of the oligosaccharide of vesicular stomatitis virus G protein by swainsonine./. Virol. 1983 46(l) 60-69. [Pg.1206]

Rose, J. K., and Gallione, C. J., 1981, Nucleotide sequence of the mRNA s encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions, J. Virol. 39 519. [Pg.292]

Other mutants of Chinese-hamster ovary-cells having decreased amounts of lipid-linked oligosaccharides are known, although they are less well characterized. G-Protein of vesicular stomatitis virus grown in one of these mutants appeared to contain fewer, but full-sized rather than truncated, oligosaccharide side-chains. There may be insufficient amounts of oligosaccharide precursor available for transfer to nascent glycoproteins.172... [Pg.313]

The nucleotide form of ribavirin does not manifest its antiviral activity simply by lowering the GTP levels, but may indeed participate directly in binding to specific G proteins (124). Ribavirin has recently been studied as an inhibitor of vesicular stomatitis virus and La Crosse virus (125). Of the phosphorylated forms of the drug, ribavirin-5 -diphosphate was by far the most potent inhibitor of viral replication for these two viruses. [Pg.312]

In both procedures, a gene encoding an abundant membrane glycoprotein (G protein) from vesicular stomatitis virus (VSV) Is Introduced Into cultured mammalian cells either by transfection or simply by Infecting the cells with the virus. The treated cells, even those that are not specialized for secretion, rapidly synthesize the VSV G protein on the ER like normal cellular secretory proteins. Use of a mutant encoding a temperature-sensitive VSV G protein allows researchers to turn subsequent protein transport on and off. At the restrictive temperature of 40 °C, newly made VSV G protein Is misfolded and therefore retained within the ER by quality control mechanisms discussed in Chapter 16, whereas at the permissive temperature of 32 C, the accumulated... [Pg.703]

Turco, S.J. Pickard, J.L. (1982) Altered G-protein Glycosylation in Vesicular Stomatitis Virus-infected Glucose-deprived Baby Hamster Kidney Cells , Journal of Biological Chemistry, 257, 8674-9... [Pg.338]

As a transport marker we use the temperature-sensitive membrane protein ts-045-G from the vesicular stomatitis virus (ZUberstein etal., 1980). This transmembrane protein has the feature of accumulating in the ER at 39.5°, but moves vectoriaUy through the secretory pathway to the plasma membrane (PM) at the permissive temperature of 32°, where an antibody recognizing an external epitope can be used to detect it. This has the principal advantage that transport in individual cells is highly synchronized. [Pg.7]

BARS concentration by some 5-fold to 15-fold, based on the calculations that the intracellnlar concentration is around 20 //g/ml and on the assumption that 5-10% of the cell volume is injected. Prior to injection, the protein is mixed with 0.4 mg/ml fluorescein isothiocyanate (FITC)- or tetramethyl-rhodamine B isothiocyanate (TRITC)-labeled dextran (Molecnlar Probes) as a marker for the microinjected cells (Bonazzi et al., 2005). To give an example, in stndies of basolateral and apical transport (using the vesicular stomatitis virus glycoprotein and p75, respectively), the proteins were microinjected 1 h after the beginning of the 20° incubation in the transport assay. After injection, the cells were allowed to recover for 1 h before proceeding with the experimental protocol (Bonazzi et al, 2005). The BARS (p50-2) and dynamin (DYN2) antibodies were injected at 4.5 mg/ ml, 3 h before farther experimental procedures. [Pg.311]

Davis, N. L., and Wertz, G. W., 1982, Synthesis of vesicular stomatitis virus negative-strand RNA in vitro Dependence on viral protein synthesis, J. Virol. 41 821. [Pg.285]

Kurilla, M. G., and Keene, J. D., 1984, The leader RNA of vesicular stomatitis virus is bound by a cellular protein reactive with anti-La lupus antibodies. Cell 34 837. [Pg.288]

Mellon, M. G., and Emerson, S. U., 1978, Rebinding of transcriptase components (L and NS proteins) to the nucleocapsid template of vesicular stomatitis virus, J. Virol. 27 560. [Pg.290]

Morrison, T. G., and Lodish, H. F., 1975, Sites of synthesis of membrane and nonmembrane proteins of vesicular stomatitis virus, J. Biol. Chem. 250 6955. [Pg.290]

Nishioka, Y., Jones, G., and Silverstein, S., 1983, Inhibition by vesicular stomatitis virus of herpes simplex virus directed protein synthesis. Virology 124 238. [Pg.291]

Wertz, G. W., and Youngner, J. S., 1972, Inhibition of protein synthesis in L cells infected with vesicular stomatitis virus, J. Virol. 9 85. [Pg.296]


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See also in sourсe #XX -- [ Pg.234 ]




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