Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We describe the isolation and characterization of conditional lethal amber nonsense mutants of vesicular stomatitis virus (VSV), Indiana serotype. The mutants were isolated from a chemically mutagenized stock of wild-type virus by their ability to grow on genetically engineered cells which express a Xenopus laevis amber suppressor tyrosine tRNA gene (su+ cells) but not on the non-suppressor parental cells (su- cells). Five mutations were assigned to complementation group I (the L gene) and one to complementation group V (the G gene) by complementation analysis using temperature-sensitive mutants representing each of the five VSV cistrons. Four of the group I mutants were observed to synthesize a novel polypeptide species in su+ cells. Immunoprecipitation and immunoblotting studies using monospecific antisera directed against the N and C termini of the VSV L protein showed that the novel polypeptide species contain N terminal- but not C terminal-specific sequences and can thus be considered to be truncated versions of the L protein. In addition a protein which again contained N terminal- but not C terminal-specific sequences could be identified for the fifth group I mutant. Revertants of four of the group I mutants were isolated on the su- cells. The revertants all synthesized normal L protein but not the putative truncated version.
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PMID:Isolation and characterization of conditional lethal amber nonsense mutants of vesicular stomatitis virus. 282 48

In this report, we have asked whether asparagine-linked oligosaccharides added to new sites in the polypeptide backbone of a model plasma membrane glycoprotein, the vesicular stomatitis virus G protein, can promote its intracellular transport. We modified the coding sequence of G protein lacking the two normal consensus sites for glycosylation by oligonucleotide-directed mutagenesis to create new consensus sites. The expression of the mutant proteins was then analyzed in transfected cells. Six of the eight new sites which were introduced were glycosylated, and an oligosaccharide at two of these new sites promoted transport of G protein which lacked the two normal sites. However, the efficiency of this process was reduced compared to the wild-type protein or to the proteins with only one oligosaccharide at either of the normal sites. In addition, an oligosaccharide at two of the other new sites caused inhibition of transport of the wild-type G protein. The data in this and the following report suggest that carbohydrate plays an indirect role in the intracellular transport of G protein.
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PMID:Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane. 283 23

In this report we have extended our studies on a panel of vesicular stomatitis virus G proteins with altered glycosylation sites. These mutant proteins were generated by oligonucleotide-directed mutagenesis of the coding sequence to create new consensus sites for asparagine-linked oligosaccharide addition. We report that the intracellular transport of most of the mutant proteins is temperature-sensitive, implying a polypeptide folding step is affected. In addition, we find that the nonglycosylated G protein and those mutant proteins which lack oligosaccharides at the normal positions are subject to aberrant intermolecular disulfide bonding, leading to the accumulation of large complexes in the endoplasmic reticulum. These results imply that carbohydrate plays an indirect role in the intracellular transport of G protein.
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PMID:Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. 283 24

IFN-gamma is a secreted polypeptide product of stimulated T lymphocytes with immunomodulatory properties as well as antiviral activity. We have investigated the effects of IFN-gamma treatment on a neutralizing antibody response to vesicular stomatitis virus (VSV) when administered in conjunction with immunization using purified envelope glycoprotein "G" of VSV. Administration of rIFN-gamma to mice or cattle at the time of primary immunization with VSV G glycoprotein enhanced the magnitude of a secondary virus-neutralizing antibody response after a booster administration of the same Ag without IFN-gamma treatment. Enhancement was statistically significant and occurred at relatively low doses of IFN-gamma in the absence of any additional adjuvants. Furthermore, cattle treated with IFN-gamma at the time of a single primary immunization were more resistant to VSV challenge than those immunized without IFN-gamma treatment. IFN-gamma treatment in conjunction with a single primary immunization may therefore provide a practical means of enhancing protection from a viral challenge without the use of inflammatory adjuvants or booster immunizations.
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PMID:Enhancement of a secondary antibody response to vesicular stomatitis virus "G" protein by IFN-gamma treatment at primary immunization. 283 43

Wild-type vesicular stomatitis virus-infected cells contained multiple carboxy-terminal fragments of the envelope glycoprotein G. They migrated in 16% polyacrylamide gels with two dominant apparent molecular weights, 14,000 and 9,000. Both fragments were immunoprecipitated by two antibodies, anti-G(COOH) and anti-G(stem), made against the last 15 amino acids at the carboxy terminus and against the first 22 amino acids of the ectodomain adjacent to the transmembrane region of G, respectively. Pulse-chase experiments in the presence and absence of tunicamycin indicated that the higher-molecular-weight fragment, Gal, was generated first, presumably in the rough endoplasmic reticulum, and then apparently chased into the faster-migrating, stable fragment, Ga2. Exposure of infected cells to radioactive palmitic acid labeled Ga2. Ga2 was detected in purified virions. These results show that a polypeptide approximately 71 amino acids long is transported and incorporated into budding virions. What signals are operative and whether this C-terminal fragment of G protein is transported as a complex with other viral or host cell proteins are presently unknown.
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PMID:Membrane anchors of vesicular stomatitis virus: characterization and incorporation into virions. 283 85

Phosphorylation of membrane-associated proteins by protein kinases in the membrane fraction from HeLa S3 cells was rapidly increased when the cells were infected with vesicular stomatitis virus (VSV). SDS-PAGE followed by autoradiography revealed polypeptides with molecular sizes of Mr. 53,000, 44,000, 42,000, 35,000, 30,000 and 27,000 in the kinase fraction from uninfected cells to be highly phosphorylated. Virus-coding NS protein (Mr. 40,000) was phosphorylated when the membrane fraction from virus-infected cells was incubated with [gamma-32P]ATP in the presence of histone H1 and Mg2+. Under these conditions, histone H1 functioned as a stimulator for NS protein phosphorylation by the kinases. One (kinase III) of the membrane-associated kinases was partially purified from HeLa S3 cells using FPLC (type Mono Q) after DEAE-cellulose column chromatography. The enzymatic properties of kinase III were similar to those reported for a polypeptide-dependent protein kinase (protein kinase P), because (a) both kinases highly phosphorylated beta-casein, although no phosphorylation was observed with histones; (b) several endogenous substrates from HeLa S3 cell membrane were phosphorylated by the kinases in the presence of basic proteins, such as histones, protamine and poly-Lys; (c) their activity was insensitive to a low concentration (19 micrograms/ml) of heparin, which highly inhibited casein kinase II activity; and (d) the kinases were extractable from the plasma membrane using Triton X-100. In addition, provided evidence suggests that kinase III may play an important role in an early stage of VSV replication through its specific phosphorylation of NS protein and membrane proteins in virus infected cells.
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PMID:Characterization of a polypeptide-dependent membrane protein kinase that specifically phosphorylates NS protein of vesicular stomatitis virus in vitro. 284 89

The anti-viral mechanism of glycyrrhizin (GL) has been investigated by considering in vitro effects on polypeptide phosphorylation. It was found that GL (i), at low doses, selectively inhibits protein phosphorylation by Kinase P, but has not significant effects on the activities of other kinases (Kinase A, Kinase C and histone kinase); (ii) binds directly to Kinase P and reduces kinase activity in a dose-dependent manner; and (iii) inhibits vesicular stomatitis virus (VSV)-associated kinase activity. These observations strongly suggest that direct binding of GL to the virus causes the direct inactivation of virus-associated kinase and the reduction of the viral infectivity.
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PMID:Inhibitory effect of glycyrrhizin on polypeptide phosphorylation by polypeptide-dependent protein kinase (kinase P) in vitro. 284 32

The heterogeneity in charge of the influenza virus glycoproteins, hemagglutinin (HA) and neuraminidase (NA) is retained, when glycosylation is inhibited by tunicamycin (TM) or 2-deoxyglucose (2-dg). This is in contrast to the charge heterogeneity of the G protein of vesicular stomatitis virus (VSV), which is mainly due to heterogeneous sulfation of the carbohydrate side chains and therefore is abolished by the above mentioned inhibitors of glycosylation. Thus, the charge heterogeneity of influenza virus glycoproteins might be attributable to some as yet unidentified modifications of the polypeptide backbone.
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PMID:Studies on the development of the charge heterogeneity of the influenza virus glycoproteins. 298 58

The roles of the L and NS polypeptides in transcription by vesicular stomatitis virus New Jersey were studied using a mutant, tsE1, which contains a temperature-sensitive transcriptase and an altered NS polypeptide, both phenotypic changes being the consequence of the ts mutation. Mutant tsE1, its revertant (tsE1/R1) and the wild-type virus were dissociated into sub-viral fractions and, after reconstitution of these fractions in all combinations, the transcriptase was assayed in vitro at the permissive (31 degrees C) and restrictive (39 degrees C) temperatures. Reconstitution of the pellet fractions (containing polypeptide N complexed with the virion RNA) and the supernatant fractions (containing polypeptides L and NS) restored transcriptase activity at 31 degrees C in all combinations, but at 39 degrees C transcription was observed only in the presence of the supernatant fractions of wild-type and revertant viruses but not in the presence of the supernatant fractions of tsE1. When the pellet fractions and the L fractions were reconstituted, the transcriptase activity was restored in all combinations both at 31 degrees C and 39 degrees C. However, in vitro transcription at 39 degrees C by reconstituted pellet and L fractions was strongly inhibited when the NS fraction of tsE1 was also added, while addition of the NS fractions of wild-type and revertant viruses had no effect. Since only traces of polypeptide NS were present in the L fractions and none in the pellet fractions, the results strongly suggest that polypeptide L is the transcriptase itself while polypeptide NS exerts some control over transcription.
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PMID:The role of polypeptides L and NS in the transcription process of vesicular stomatitis virus New Jersey using the temperature-sensitive mutant tsE1. 298 93

The complete nucleotide sequence of the NS mRNA of vesicular stomatitis virus (New Jersey serotype) was established from two cDNA clones spanning the entire coding region of the mRNA. The gene is 856 nucleotides long and can code for a polypeptide of 274 amino acids. Comparison with the nucleotide sequence of the NS gene of the Indiana serotype revealed only 41% sequence homology. The deduced amino acid sequences of the NS proteins were only 32% homologous, with no identical stretches of more than five amino acids. However, at the C-terminal domain there was a conserved region of 21 amino acids with greater than 90% homology. Surprisingly, relative hydropathicity plots also demonstrated the presence of a large number of hydrophilic amino acids sequestered similarly over the N-terminal half of the protein. In addition, the total number of serine and threonine residues, presumptive phosphorylation sites, was similar and included seven serine and three threonine residues located at identical positions. It appears that during divergent evolution of these two vesicular stomatitis virus serotypes from a common ancestor, considerable mutation occurred in the main body of the gene but the overall structure of the protein was retained. The function of the NS protein in relation to the evolution of the two viruses is discussed.
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PMID:Vesicular stomatitis virus NS proteins: structural similarity without extensive sequence homology. 298 60


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