Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant
نویسندگان
چکیده
منابع مشابه
A fusion-defective mutant of the vesicular stomatitis virus glycoprotein.
We have recently described an assay in which a temperature-sensitive mutant of vesicular stomatitis virus (VSV; mutant tsO45), encoding a glycoprotein that is not transported to the cell surface, can be rescued by expression of wild-type VSV glycoproteins from cDNA (M. Whitt, L. Chong, and J. Rose, J. Virol. 63:3569-3578, 1989). Here we examined the ability of mutant G proteins to rescue tsO45....
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The carbohydrate structure of the membrane glycoprotein of vesicular stomatitis virus (New Jersey serotype) has been determined on material purified from virions grown in spinner cultures of BHKzl cells in the presence of [3H]glucosamine. The intact 3H-glycoprotein contains 6 residues of N-acetyl-n-neuraminic acid, 6 of D-galactose, 6 of D-mannose, 2 of L-fucose, and 10 of N-acetyl-n-glucosamin...
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The cytoplasmic domains of viral glycoproteins are often involved in specific interactions with internal viral components. These interactions can concentrate glycoproteins at virus budding sites and drive efficient virus budding, or can determine virion morphology. To investigate the role of the vesicular stomatitis virus (VSV) glycoprotein (G) cytoplasmic and transmembrane domains in budding, ...
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A recombinant S segment RNA (Sr) of the prototypic arenavirus lymphocytic choriomeningitis virus (LCMV) where the glycoprotein of vesicular stomatitis virus (VSVG) was substituted for the glycoprotein of LCMV (LCMV-GP) was produced intracellularly from cDNA under the control of a polymerase I promoter. Coexpression of the LCMV proteins NP and L allowed expression of VSVG from Sr. Infection of t...
متن کاملDBC2 is essential for transporting vesicular stomatitis virus glycoprotein.
DBC2 is a tumor suppressor gene linked to breast and lung cancers. Although DBC2 belongs to the RHO GTPase family, it has a unique structure that contains a Broad-Complex/Tramtrack/Bric a Brac (BTB) domain at the C terminus instead of a typical CAAX motif. A limited number of functional studies on DBC2 have indicated its participation in diverse cellular activities, such as ubiquitination, cell...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1989
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.63.9.3569-3578.1989