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

---

Query: UMLS:C0038362 (stomatitis)
8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The endogenous transcriptase present in purified vesicular stomatitis (VS) virions was solubilized with a Triton X-100 high-salt solution. The polymerase activity was purified on glycerol gradients and by phosphocellulose column chromatography; the viral proteins present in the active enzyme fractions were identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis. It was demonstrated that L protein, but not NS protein, was required for in vitro RNA synthesis on the VS viral nucleocapsid template. Solubilized L protein rebinds to the ribonucleoprotein template when the transcription complex is reconstituted, and the RNA synthesized in vitro by purified L protein hybridizes to virion RNA. Cyanogen bromide peptide fingerprints indicate that the large L protein is a unique polypeptide chain. It is concluded that the L protein functions as the transcriptase, and the nucleocapsid NS protein is not essential for in vitro RNA synthesis.
...
PMID:L protein requirement for in vitro RNA synthesis by vesicular stomatitis virus. 435 10

The ribonucleoprotein-dependent RNA transcriptase in vesicular stomatitis B virions of four temperature-sensitive (ts) mutants belonging to complementation group I was analyzed in vitro at permissive (31 C) and restrictive (39 C) temperatures. The RNA-synthesizing activity of all four ts mutants was more labile at 39 C than was the transcriptive activity of wild-type (wt) virions. In order to locate the temperature-sensitive transcription defect in the mutants, wt and ts mutant virions were fractionated by Triton X-100-high salt solubilizer into a sedimentable ribonucleoprotein template and a nonsedimentable enzyme fraction, each of which alone had little or no transcriptive activity. The template- and enzyme-containing fractions of wt virions were then tested for their capacity to restore transcriptive activity at 39 C to corresponding template and enzyme preparations of ts mutant virions. Recombination of wt template and ts enzymes resulted in no significant restoration of capacity to synthesize RNA at restrictive temperature. In contrast, transcriptive function at 39 C was reconstituted by recombining the wt enzyme with the template component of ts mutants. It appears, therefore, that the enzyme, rather than the template, is the temperature-sensitive component of the transcription complex of group I vesicular stomatitis virus mutants.
...
PMID:Location of the transcription defect in group I temperature-sensitive mutants of vesicular stomatitis virus. 435 28

The presence of a virion-associated RNA-dependent RNA polymerase in five serologically distinct rhabdovirus isolates (vesicular stomatitis virus [VSV] Indiana, VSV New Jersey, Cocal, Chandipura, and Piry viruses) has been demonstrated. The enzyme for each virus has been shown to be a transcriptase capable of synthesizing in vitro RNA which is complementary to the viral genome. By sequence analyses it has been shown that, for each rhabdovirus, transcription is multiply initiated with specific 5' nucleotide sequences. The results indicate that, for all five viruses, the initiation of transcription involves similar sequences (e.g., pppApCpGp..., pppGpCp..., and possibly one or two other sequences), suggesting relatedness and some genome conservation among these viruses.
...
PMID:RNA transcription by the virion polymerases of five rhabdoviruses. 436 67

Heterologous viral interference is induced by Sindbis virus against vesicular stomatitis virus (VSV) in a manner analogous to intrinsic interference with Newcastle disease virus replication. Interference in both systems (i) depends upon early expression of the inducing virus genome, (ii) shows similar kinetics of induction, (iii) does not involve interferon action, and (iv) appears to be manifest as an all-or-none effect. VSV can be added to the list of viruses blocked by intrinsic interference. Sindbis virus-induced intrinsic interference with VSV replication is not mediated through homotypic interference by defective interfering particles; rather, T-particle and B-particle synthesis is inhibited. Significantly, intrinsic interference has no effect on primary transcription directed by the virion-associated transcriptase in VSV-challenged cells. However, Sindbis virus appears to induce interference with the VSV-RNA synthesized subsequent to primary transcription, namely, that which is dependent on protein synthesis. Thus, the target of intrinsic interference appears to be a reaction subsequent to primary transcription but prior to the appearance of protein synthesis-dependent VSV RNA, secondary transcription.
...
PMID:Mechanism of Sindbis virus-induced intrinsic interference with vesicular stomatitis virus replication. 436 26

We analyzed cell extracts from BHK(21) cells infected with vesicular stomatitis virus (VSV) and rabies virus for in vitro RNA polymerase activity. Cells infected with VSV B virions exhibited several complexes with in vitro RNA polymerase activity in sucrose gradients. These complexes synthesize VSV transcriptase product (4 to 18S) polyadenylated in RNA complementary to virion RNA. Cells infected with a high multiplicity of B virions and T particles show only one RNA polymerase complex active in vitro. This complex sediments at 110S and makes only small (2S) RNA. Carrier BHK(21) cells persistently noncytopathically infected with VSV contain several complexes active in RNA polymerase, but both exhibit very low activity. Cytoplasms of cells noncytopathically infected with rabies virus also show very low levels of a complex containing RNA polymerase activity. No transcriptase nor any other in vitro polymerase activity could be found associated with purified rabies virions, although they do carry out primary transcription in cells treated with actinomycin D and cycloheximide before infection.
...
PMID:Transcribing complexes in cells infected by vesicular stomatitis virus and rabies virus. 436 91

Infectious B virions of vesicular stomatitis virus were 100% lethal to BHK(21) (baby hamster kidney) cells when infecting alone, and persistent noncytocidal infection could not be achieved with cloned B virions alone. However, a mixture of B virions and homologous, short, defective, interfering particles (T particles) of a temperature-sensitive mutant of the virus regularly established persistently infected, noncytocidal carrier cultures. A long T particle was generated during establishment of the carrier culture; we show that this long T particle can establish and maintain persistent noncytocidal infection even when it infects cells along with virulent wild-type B virions. This long T particle causes the production of wild-type B virions with greatly reduced virion transcriptase (EC 2.7.7.6; RNA nucleotidyltransferase) levels when coinfecting the same cells, so it appears to prevent cytopathology by regulating virus transcription. The implications of these findings for rabies and other slowly progressing noncytocidal infections are discussed.
...
PMID:Persistent noncytocidal vesicular stomatitis virus infections mediated by defective T particles that suppress virion transcriptase. 437 Feb 55

When tested in vitro, certain temperature-sensitive (ts) mutants of vesicular stomatitis virus (VSV) belonging to complementation groups I and IV appear to have defects in the virion-bound polymerase. To obtain further information concerning the nature of these defects, representative mutants were dissociated by the method of S. Emerson and R. Wagner (1972), and their supernatant (S) and pellet (P) fractions were tested for transcriptase activity when combined with the P and S fractions, respectively, of VSV-HR virions. It was found that the S fractions from group I mutants tsW4, 11, 14, 15, and 28 were defective in transcriptase activity, whereas their P fractions were as active as those of VSV-HR. On the other hand, the P fraction derived from virions of the group IV mutant tsW16B showed reduced activity at 25 C and very little activity at 38 C. These results suggest that our group I mutants, like those examined by D. Hunt and R. Wagner (1974), have a defect in the soluble transcriptase enzyme, whereas mutant tsW16B (group IV) has a defect in a sedimentable component required for transcriptase activity, possibly in the ribonucleoprotein template.
...
PMID:Temperature-sensitive mutants of vesicular stomatitis virus: comparison of the in vitro RNA polymerase defects of group I and group IV mutants. 437 Sep 58

TsG16(I) is a temperature-sensitive mutant of vesicular stomatitis virus, Indiana serotype. Our stocks of this mutant overproduce polyadenylic acid in an in vitro transcription system. The overproduction of polyadenylic acid occurs at all temperatures tested (27, 31, 35, and 39 degrees C) and is apparently not due to an alternation in the N protein-RNA template. To characterize the altered moiety in tsG16(I) responsible for this phenotype, virions were fractionated and the polyadenylation phenotype in homologous and heterologous reconstitution assays was determined. The aberrant polyadenylation phenotype correlated with the presence of ts L protein but not ts NS or ts M protein fractions. Results of experiments in which solubilized tsG16(I) and wild-type virion components were mixed indicated that the altered moiety behaved as if present in stoichiometric amounts relative to active L protein. The effects of raising the temperature from 31 to 39 degrees C in such mixes were as would be predicted upon the assumption that the polyadenylation phenotype was associated with a thermosensitive transcriptase component [the L protein of tsG16(I) is known to be thermosensitive]. We conclude that the data strongly support the hypothesis that L is the altered protein responsible for the aberrant polyadenylation phenotype of tsG16(I).
...
PMID:Aberrant polyadenylation by a vesicular stomatitis virus mutant is due to an altered L protein. 609 72

Earlier we reported a reduction to 1/30th-1/100th of the original number of infectious particles in the infectious vesicular stomatitis virus (VSV) released from L cells treated with 10 or 30 reference units of interferon per ml. However, in these cultures virus particle production, as measured by VSV particle-associated viral RNA, virus nucleocapsid protein, and viral transcriptase, was inhibited by less than 10%. Data reported in this paper show that there was a significant reduction in glycoprotein and membrane protein of VSV particles released from interferon-treated cells. Evidence supporting the deficiency of glycoprotein in VSV released from interferon-treated cells was derived from electron microscopic studies. Under conditions where glycoprotein spikes or projections were clearly detectable on the surface of VSV released from cells not treated with interferon, very few spikes were observed on VSV released from interferon-treated cells. These results suggested that interferon-treated cells produced VSV particles with low infectivity and that this low infectivity may be related to the reduced amount of glycoprotein and membrane protein incorporated into such particles.
...
PMID:Interferon-treated cells release vesicular stomatitis virus particles lacking glycoprotein spikes: correlation with biochemical data. 615 48

Earlier, we reported a 30-200-fold reduction in the yield of infectious vesicular stomatitis virus (VSV) released from L cells treated with 10-30 reference units ml-1 of interferon (IFN); however, in these cultures virus particle production, as measured by VSV particle-associated viral RNA, virus nucleocapsid protein and viral transcriptase, was inhibited less than 10-fold. There was biochemical and morphological evidence of a significant reduction in glycoprotein (G) and membrane protein (M) of VSV particles released from IFN-treated cells. We compare here the effects of tunicamycin (TM) and IFN in L cells. Treatment with TM or IFN reduced the production of infectious VSV particles, decreased the amount of G and M proteins in VSV released from treated cells, and inhibited an early step in the formation of asparagine-linked oligosaccharide chains, the incorporation by membrane preparations from treated cells of N-acetylglucosamine into glycolipids with the properties of dolichol derivatives.
...
PMID:Interferon treatment inhibits glycosylation of a viral protein. 615 39


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---