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)

An abortive infection of a rabbit cornea cell line (RC-60) by vesicular stomatitis virus (VSV), yielding less than 1 PFU/cell, was converted to a productive infection, yielding 1,900 PFU/cell, when cells were superinfected with vaccinia. Studies on the synthesis of VSV-directed RNA in RC-60 cells suggest that the abortive infection by VSV alone may be due in part to (i) a limited production of 40S virion RNA and (ii) a markedly reduced activity of virion-bound transcriptase activity in RC-60 cells compared to the activity in mouse L cells, a permissive host for VSV. No recognizable VSV structures, except a small amount of viral core structures, were produced by the abortive infection. In contrast, double infection of RC-60 cells with VSV and vaccinia in the presence of hydroxyurea resulted in the production of infective B particles of VSV. Although the function supplied by vaccinia responsible for the productive replication of VSV in double infected RC-60 cells has not been identified, metabolic inhibitor studies indicate that continuous vaccinia-dependent RNA synthesis is required for maximal production of infective VSV. The possibility is considered that vaccinia may supply a product or function required for VSV replication which is ordinarily supplied by the host but which is lacking in RC-60 cells.
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PMID:Abortive infection of a rabbit cornea cell line by vesicular stomatitis virus: conversion to productive infection by superinfection with vaccinia virus. 16 5

Glycoprotein mRNA (G mRNA) of vesicular stomatitis virus is synthesized in the cytosol fraction of infected HeLa cells. Shortly after synthesis, this mRNA associates with 40S ribosomal subunits and subsequently forms 80S monosomes in the cytosol fraction. The bulk of labeled G mRNA is then found in polysomes associated with the membrane, without first appearing in the subunit or monomer pool of the membrane-bound fraction. Inhibition of the initiation of protein synthesis by pactamycin or muconomycin A blocks entry of newly synthesized G m RNA into membrane-bound polysomes. Under these circumstances, labeled G mRNA accumulates into the cytosol. Inhibition of the elongation of protein synthesis by cucloheximide, however, allows entry of 60 percent of newly synthesized G mRNA into membrane-bound polysomes. Furthermore, prelabeled G mRNA associated with membrane-bound polysomes is released from the membrane fraction in vivo by pactamycin or mucomycon A and in vitro by 1mM puromycin - 0.5 M KCI. This release is not due to nonspecific effects of the drugs. These results demonstrate that association of G mRNA with membrane-bound polysomes is dependent upon polysome formation and initiation of protein synthesis. Therefore, direct association of the 3' end of G mRNA with the membrane does not appear to be the initial event in the formation of membrane-bound polysomes.
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PMID:Studies on the mechanism for entry of vesicular stomatitis virus glycoprotein G mRNA into membrane-bound polyribosome complexes. 19 7

Nucleotide sequences of the ribosome-protected translation initiation sites from the vesicular stomatitis virus (VSV) M and L protein mRNAs have been determined, completing the sequences of the sites from all the VSV mRNAs. A low level of protection at two internal AUG-containing sites in the N mRNA is also described. Small homologies are evident among some of the sites, but there are no obvious features common to all the sites other than a single AUG codon. In contrast, a large homology between the VSV M mRNA site and the alfalfa mosaic virus coat mRNA site (Koper-Zwarthoff et al., 1977) is noted. This homology suggests the existence of a common ancestral gene for these two apparently unrelated viruses. For each VSV mRNA species, the smallest sites protected in either the 40S or 80S initiation complexes are identical. These sites always contained the initiation codon, but only contained the capped 5' end in those mRNAs having the 5' end near the initiation site. If 40S ribosomes bind to the capped 5' end, either they do not protect it from nuclease digestion or the protection is only transitory in some VSV mRNAs. Consideration of the structures of the ribosome binding sites suggests that the differential effects of hypertonic shock on translation (Nuss and Koch, 1976) may be related to the distance between the 5' end of the mRNA and the initiation codon.
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PMID:Complete sequences of the ribosome recognition sites in vesicular stomatitis virus mRNAs: recognition by the 40S and 80S complexes. 20 78

To determine whether defective interfering (DI) particles modulate virulence by initiating a cyclic pattern of virus growth in vivo, adult mice were infected with vesicular stomatitis virus (VSV), both with and without DI particles. A total of 184 mice divided into groups were inoculated intranasally. A majority of mice inoculated only with standard VSV developed paralysis, most of them between days 7 and 9. The addition of DI particles altered the development of paralysis in several ways. When there was significant protection, a few still became paralyzed on days 7 and 9. When overall mortality was unaffected or even slightly increased, the majority of mice became paralyzed between days 7 and 9 as well. Protection could not be predicted based on a single ratio of standard VSV to DI particles or on the absolute amount of DI particles inoculated. Infectious virus recovered from mouse brains at the time of paralysis and incipient death showed considerable variation, although the titer in a majority of the animals was between 10(5) and 10(7) PFU/ml. When the brains of these paralyzed mice were examined for hybridizable VSV RNA, the detection of standard VSV RNA correlated well with infectivity. The amount of DI RNA in the coinfected mice was more variable and independent of the amount of 40S RNA, although DI RNA was usually found when standard RNA was present. Survivors examined between days 14 and 21 did not contain infectious virus or any detectable viral RNA in their brains. Because these results were consistent with the hypothesis of viral cycling in vivo, rather than a gradual accumulation of total infectious virus, mice were coinfected with 10(8) PFU of standard VSV and 10(5) PFU equivalents of DI particles and sacrificed daily thereafter, irrespective of whether they developed paralysis. Infectivity measurements indicated a reproducible cycling pattern of VSV in the mouse brains with a periodicity of about 5 days. This cycling and the detection of DI RNA in brains several days after intranasal inoculation suggest that there is a dynamic continuous interaction between standard VSV and its DI particle beyond the initial site of replication as the virus population spreads into the host animal. Such cycling of virus production before the full development of specific immune responses from the host may have important implications for viral diagnostics and disease transmission.
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PMID:Defective interfering virus particles modulate virulence. 299 62

In an effort to facilitate studies of the reaction involved in the removal of fatty acids from acyl proteins, we have synthesized an octanoic acid ester of doubly blocked serine, specifically octanoyl N-carbobenzoxy-L-serine-benzyl ester (octanoyl boc-serine), and used it as a substrate to guide the purification of an esterase from rat lung. The esterase was purified 228-fold by column chromatography on DE-52 cellulose, hydroxylapatite, octyl-Sepharose, and concanavalin A-Sepharose and by HPLC gel filtration. The final enzyme preparation ran as a single 77,000-Da band when subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and exhibited a single symmetrical peak (sedimentation coefficient, 4.5 S) when centrifuged through a sucrose density gradient (empirical Mr, 63,000). The esterase is an acidic protein, pI 4.1, and is very active against p-nitrophenyl esters comprised of C4-C14 fatty acids; the highest specific activity (26.5 mumol/min/mg) was obtained using p-nitrophenyl caprylate as substrate. The pH optimum of the lung esterase is near 8.0 and the activity on octanoyl boc-serine is maximum when 0.3% (w/v) Myrj-52 is included in the assay medium. The activity of the esterase is not dependent on calcium ions. The enzyme does not remove acyl groups from the G-protein of vesicular stomatitis virus or the proteolipid of bovine brain. The possible role of the esterase in the metabolism of acylated proteins is considered.
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PMID:Isolation and characterization of a fatty acyl esterase from rat lung. 335 57

The temperature-sensitive mutant ts114 of vesicular stomatitis virus is temperature-sensitive in both primary and secondary transcription, but not in the replication of 40S RNA. The synthesis of 40S RNA is specifically inhibited when protein synthesis is shut off. The addition of cycloheximide to cells infected by ts114, rapidly inhibits RNA replication at the permissive and nonpermissive temperatures. However, the addition of cycloheximide at the nonpermissive temperature also results in almost complete recovery of transcription to the level found at the permissive temperature. Other inhibitors of protein synthesis applied at the nonpermissive temperature result in the same recoverability of the apparent temperature-sensitive lesion. Ribonucleic acid products synthesized by ts114 at the nonpermissive temperature in the presence of cycloheximide are identical to virus-specific messenger RNA by the criteria of size and complementarity to virion RNA. When mutant-infected cells are shifted to the nonpermissive temperature, incubated for a period of time, and then treated with cycloheximide, the ratio of transcriptive to replicative activity varies depending on the time at which radioactive precursor is added to cells. This suggests an interdependence between replication and transcription during virus-specific RNA synthesis.
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PMID:RNA synthesis of vesicular stomatitis virus. V. Interactions between transcription and replication. 435 12

We have developed a stably transfected CHO cell line (CHO24S) that expresses the three structural proteins of rubella virus (RV). RV proteins C (capsid), E2, and E1 are secreted from CHO24S cells in the form of RV-like particles (RLPs) which form by budding into the cisterna of the Golgi complex. RLPs resemble RV virions in their size and morphology and have an identical buoyant density when purified on sucrose gradients. Release of RLPs into the medium was found to be dependent upon the E1 cytoplasmic tail since deletion or substitution of this domain with the same region from vesicular stomatitis virus G protein abrogated release of RV proteins from transfected cells. These results indicate that the RV 40S genomic RNA is not required for efficient particle assembly. Therefore, RLPs may serve as a convenient source of RV antigen for use in diagnostic assays and as an alternative to live attenuated vaccine strains.
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PMID:Assembly of rubella virus structural proteins into virus-like particles in transfected cells. 803 Feb 23

We analyzed the assembly of caveolae in CV1 cells by following the fate of newly synthesized caveolin-1 (CAV1), caveolin-2 and polymerase I and transcript release factor (PTRF)/cavin-1 biochemically and using live-cell imaging. Immediately after synthesis in the endoplasmic reticulum (ER), CAV1 assembled into 8S complexes that concentrated in ER exit sites, due to a DXE sequence in the N-terminal domain. The coat protein II (COPII) machinery allowed rapid transport to the Golgi complex. Accumulating in the medial Golgi, the caveolins lost their diffusional mobility, underwent conformational changes, associated with cholesterol, and eventually assembled into 70S complexes. Together with green fluorescent protein-glycosyl-phosphatidylinositol (GFP-GPI), the newly assembled caveolin scaffolds underwent transport to the plasma membrane in vesicular carriers distinct from those containing vesicular stomatitis virus (VSV) G-protein. After arrival, PTRF/cavin-1 was recruited to the caveolar domains over a period of 25 min or longer. PTRF/cavin-1 itself was present in 60S complexes that also formed in the absence of CAV1. Our study showed the existence of two novel large complexes containing caveolar coat components, and identified a hierarchy of events required for caveolae assembly occurring stepwise in three distinct locations--the ER, the Golgi complex and the plasma membrane.
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PMID:Biogenesis of caveolae: stepwise assembly of large caveolin and cavin complexes. 2007 Jun 7