Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Six temperature-sensitive (ts) mutants of vesicular stomatitis virus (VSV) isolated from the central nervous system (CNS) following injection with ts G31 (III) all possessed a post-transcriptional defect, not found in the initial virus, that affects the stability of viral RNA transcripts. Examination of viral RNA metabolism in mouse neuroblastoma (N-18) cells revealed that RNA synthesis of the CNS isolates was decreased considerably at elevated temperatures (up to 80 or 90% at 39 degrees C). In addition, analysis of the RNA transcripts suggested that little if any normal-sized transcripts were made in cells infected with these CNS isolates at either 37 degrees C or 39 degrees C. The RNA deficiencies did not appear to be the result of a temperature-sensitive lability of virion transcriptase as examined by in vitro transcriptase assays. However, when N-18 cells infected with one of the CNS isolates, ts G31 BP, were first preincubated at the permissive temperature of 31 degrees C for 3 h and then shifted to 39 degrees C, RNA synthesis proceeded at a rate comparable to that of 31 degrees C. The viral mRNA species synthesized following the temperature shift also contained normal sized tracts of poly(A) RNA, suggesting that neither the viral transcriptase nor its polyadenylate synthetase was thermally labile. However, for any of the six CNS isolates, all species of viral RNA synthesized in cells that were first preincubated at 31 degrees C degraded rapidly when the cells were shifted to 39 degrees C. In contrast little or no RNA degradation of either 42S progeny RNA or mRNA species was detected in the wild-type VSV, ts G31 or three other VSV mutants that are defective in some aspect of viral RNA metabolism: [ts G11 (I), ts G22 (II), ts G41 (IV)]. The apparent phenotype alteration in the stability of viral RNA in all of these CNS isolates is discussed in terms of the possible genotypic changes that may have occurred as well a the unique CNS disease that accompanies infection by these viruses.
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PMID:RNA degradation defect in central nervous system isolates of vesicular stomatitis virus. 616 98

The relationship between the in vitro phosphorylation of vesicular stomatitis virus (VSV) proteins and virion uncoating was examined. Activation of the VSV virion kinase with low concentrations of melittin, the active peptide component of bee venom, in the presence of gamma-[32P] ATP resulted in the phosphorylation of virion proteins. Following the in vitro phosphorylation of VSV proteins in the presence of melittin and deoxyadenosine triphosphate, the virion envelope was disrupted based on the accessibility of the internal ribonucleoprotein core (RNP) to the heavy metal stain, uranyl acetate, as determined by electron microscopic observation. The RNP structure was not observed in unphosphorylated virions treated with melittin and uranyl acetate. Phosphorylated virions treated with uranyl acetate subsequently lost the capacity for transcription whereas unphosphorylated virions treated with the stain retained transcriptase activity. These observations suggest that phosphorylation of VSV proteins may contribute to virion uncoating by disrupting the virus envelope.
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PMID:Phosphorylation of vesicular stomatitis virus proteins as a possible contributing factor in virion uncoating. 617 11

Ehrlich ascites tumour(EAT) cells were infected with vesicular stomatitis virus (VSV) within the peritoneal cavity of mice and used to prepare milligram quanities of purified virus. The protein pattern, endogenous transcriptase activity, and specific infectivity of this virus were comparable to viral preparations from HeLa and BHK cells. A total of 2-4 x 10(11) p.f.u. of VSV were obtained routinely from one mouse. The initial high concentration of VSV grown in EAT cells in the peritoneal cavity of mice facilitates virus isolation and allows its purification by a single gradient centrifugation step.
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PMID:A rapid procedure for the production and purification of vesicular stomatitis virus. 618 19

Soluble transcriptase containing the L and the NS proteins was isolated from purified vesicular stomatitis virus and its binding with the template ribonucleoprotein containing the N protein-RNA complex was studied with respect to its ability to initiate and synthesize RNA in vitro. By using u.v.-irradiated template reconstituted with soluble transcriptase, it was shown that the synthesis of leader RNA and other small initiated mRNA sequences continued while full-length mRNA synthesis decreased by 90%. In the presence of ATP and CTP, the reconstituted complex synthesized polyphosphorylated oligonucleotides which include AC, AAC and AACA which represent 5'-terminal sequences transcribed from the leader template and genes coding for mRNAs. In the presence of arabinosyl ATP, an inhibitor of RNA synthesis in vitro, the synthesis of leader RNA was found to be inhibited considerably more than other small initiated mRNA sequences. Reconstitution of RNA synthesis with soluble transcriptase and template in the presence of viral matrix (M) protein at low ionic condition resulted in virtual cessation of leader RNA synthesis, although the synthesis of small initiated N mRNA, 11 to 14 bases, continued. These results suggest that transcriptase can bind at multiple sites on the genome template and initiate RNA chains.
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PMID:Interaction of L and NS proteins of vesicular stomatitis virus with its template ribonucleoprotein during RNA synthesis in vitro. 619 59

A 200-fold inhibition in the titer of infectious vesicular stomatitis virus (VSV) was produced in cultures of Ly cells treated with 30 reference units of interferon per milliliter. Virus particle production, as measured by VSV particle-associated transcriptase, or nucleocapsid protein was inhibited by a maximum of tenfold. The glycoprotein and membrane protein content was reduced in VSV derived from interferon-treated cells. Thus interferon-treated cells may have produced VSV particles with low infectivity, which may be related to the reduced amount of glycoprotein incorporated into such particles. These findings resemble those reported in interferon-treated cells infected with murine leukemia viruses.
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PMID:Selective inhibition of glycoprotein and membrane protein of vesicular stomatitis virus from interferon-treated cells. 624 16

The accumulation of ribonucleic acid (RNA) in mouse L-929 cells infected with temperature-sensitive mutants of vesicular stomatitis virus or ultraviolet- (UV-) irradiated virus was studied. At the permissive temperature (30 degrees C infection by all mutants resulted in an inhibition of cellular RNA accumulation. At the nonpermissive temperature (40 degrees C) mutants G114 (I) and G22 (II) failed to inhibit RNA accumulation, but mutants G11 (I), O52 (II), G31 (III), G33 (III), G41 (IV), W10 (IV), O45 (V), and O110 (V) were still active in this respect. In most cases the accumulation of 28S and 18S mature rRNA was inhibited to a greater extent than the synthesis of the 45S rRNA precursor. UV irradiation of wild type virus considerably reduced its capacity to inhibit cellular RNA synthesis. The target size for inactivation of this capacity of the virus was approximately 17% of the viral genome or that corresponding to the N gene. These results indicate that the virion proteins themselves are incapable of inhibiting cellular RNA synthesis and that transcription of approximately 17% of the genome is required. Expression of RNA synthesis inhibition also requires some function of virion NS protein in addition to its transcriptase activity.
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PMID:Inhibition of ribonucleic acid accumulation in mouse L cells infected with vesicular stomatitis virus requires viral ribonucleic acid transcription. 624 56

The 5'-terminal nucleotide sequence from positions 50 to 130 of vesicular stomatitis virus RNA was determined indirectly by using a defective interfering particle RNA which contains covalently linked genomic minus and antigenomic plus sense RNAs. The last 18 nucleotides of the L gene coding for in the viral polymerase were identified and isolated by specific duplex formation between 5' terminally labeled oligonucleotides from a small single-stranded defective interfering particle RNA and L gene mRNA. The L gene ends at position 60 from the 5' terminus of the vesicular stomatitis genome. The data demonstrated that the first seven adenine residues in the polyadenylic acid tail of L gene mRNA may be coded for in the genome and suggested that the viral transcriptase itself may carry out polyadenylation, possibly by chattering at the uridine-rich sequence at the end of the L gene. Analysis of the 5'-terminal sequence of vesicular stomatitis virus genomic RNA revealed that it might fold into a complex secondary structure with possibly 62% of the bases paired.
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PMID:Site on the vesicular stomatitis virus genome specifying polyadenylation and the end of the L gene mRNA. 624 80

A procedure to enrich for the sequences present at the junction between the linked messages in the polycistronic RNAs symthesized in vitro by vesicular stomatitis virus (VSV) is described. Analyses of these sequences show that they contain a precise transcript of both the intercistronic dinucleotide and the pentanucleotide 5'--C-U-G-U-U--3', common to the 5'-end of all VSV cistrons, covalently linked to the 3'-side of the intervening poly(A). The data strongly suggest that the VSV transcriptase polyadenylylates the mRNAs and can then resume direct and precise transcription of the genome-without reinitiation and without skipping nucleotides.
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PMID:Polycistronic vesicular stomatitis virus RNA transcripts. 625 36

We have characterized the interactions between mutant or wild-type M protein and nucleocapsids of vesicular stomatitis virus (VSV) by assaying for inhibition of in vitro transcriptase activity. The interactions are primarily electrostatic in nature: high concentrations of NaCl or poly(L-glutamic acid) reverse the inhibition. These interactions are much weaker in each of the four M protein mutants (complementation group III) tested than in wild-type VSV. Temperature-sensitive revertants were selected from each of the M protein mutants studied. The salt-dependent inhibitory profiles of all the revertants resemble that of wild-type VSV, suggesting that M-nucleocapsid interactions are integrally related to the temperature-sensitive phenotype of group III mutants. These results are discussed in relation to the accompanying paper [Reidler, J.A., Keller, P.M., Elson, E.L., & Lenard, J. (1981) Biochemistry (preceding paper in this issue)] which shows that interaction between M protein and infected cell membranes is increased in all group III mutants studied.
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PMID:Interaction of wild-type and mutant M protein vesicular stomatitis virus with nucleocapsids in vitro. 626 91

Carrier cultures of L cells infected with wild-type vesicular stomatitis virus (VSV0) were initiated without the use of defective-interfering particles or homologous interferon. The cloned viruses recovered from such carrier cultures after passage 21 were characterized as temperature-sensitive. Furthermore, these clones of the mutant showed restricted replication at permissive temperature in HEp-2 cell cultures as compared to the wild-type VSV0. This restrictive replication of the mutant in HEp-2 cells was not due to a defect in the expression of virion-associated primary transcriptase activity in vivo, but due to the marked reduction in virus-specific characterized may govern the synthesis of mutant virus-specific amplified RNA in HEp-2 cells.
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PMID:Host restriction property of a vesicular stomatitis virus mutant isolated from carrier cultures. 627 Feb 62


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