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)

Vesicular stomatitis virus-infected Chinese hamster ovary cells release into the extracellular medium a soluble form of the vesicular stomatitis virus glycoprotein (G protein) termed Gs (Kang and Prevec, Virology 46:678-680, 1971). The properties of this molecule and the cellular site at which it is generated were characterized. By comparing the sizes and the peptide maps of the unglycosylated forms of G and Gs, we found that between 5,000 and 6,000 daltons of the carboxy-terminal end of the G protein is cleaved to generate the Gs molecule. This truncated molecule contains no fatty acid. Gs released from cells grown at 39 degrees C migrated on polyacrylamide gels slightly slower than Gs released at 30 degrees C. The unglycosylated form of Gs also showed this size difference. Furthermore, unglycosylated Gs was resolved into two species upon isoelectric focusing: the relative amounts of the two species depended upon the temperature at which infected cells were incubated. Full-sized unglycosylated virus-associated G also was resolved into two species, but the more basic form predominated at both 30 and 39 degrees C. The appearance of Gs in the extracellular medium depended upon the presence of stable, full-sized G at the cell surface. The amount of Gs released was quantitated in seven different situations in which the migration of G to the cell surface was inhibited. In all cases, the amount of Gs released was also decreased. In addition, incubation of cells surface labeled with 125I resulted in the release of 125I-labeled Gs protein, as well as full-sized G protein. These results suggest that Gs is generated primarily by proteolytic cleavage of plasma membrane-associated G at a site in the molecule just amino terminal to the membrane-spanning region of the molecule.
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PMID:Characterization of the soluble glycoprotein released from vesicular stomatitis virus-infected cells. 629 61

Swainsonine, an inhibitor of glycoprotein processing, inhibits the formation of the normal oligosaccharide chain of the G protein of vesicular stomatitis virus. Thus, when vesicular stomatitis virus was grown in baby hamster kidney cells in the presence of swainsonine (15 to 500 ng/ml) and labeled with [2-(3)H]mannose, the oligosaccharide portion of the G protein was completely susceptible to the action of endoglucosaminidase H. However, the normal viral glycoprotein is not susceptible to this enzyme. Various enzymatic treatments and methylation studies of the mannose-labeled oligosaccharides suggest that swainsonine causes the formation of a hybrid-type oligosaccharide having an oligomannosyl core (Man(5)GlcNAc(2)-Asn) characteristic of neutral oligosaccharides plus the branch structure (NeuNAc-Gal-GlcNAc) characteristic of the complex oligosaccharides. A structure for this hybrid oligosaccharide is proposed. Swainsonine had no effect on the incorporation of [(14)C]leucine into viral proteins, nor did it change the number of PFU produced in these cultures. It did, however, slightly decrease the incorporation of [(3)H]glucosamine and increase the incorporation of [(3)H]mannose. Vesicular stomatitis virus raised in the presence of swainsonine bound much more tightly to columns of concanavalin A-Sepharose than did control virus. Swainsonine had to be added within the first 4 or 5 h of virus infection to be effective. Thus, when 100 ng of the alkaloid per ml was added at any time within the first 3 h of infection, essentially all of the glycoprotein was susceptible to digestion by endoglucosaminidase H. However, when swainsonine was added 4 h after the start of infection, 30% of the glycopeptides became resistant to endoglucosaminidase H; at 5 h, 70% were resistant. The effect of swainsonine was reversible since removal of the alkaloid allowed the cells to form the normal complex glycoproteins. However, the time of removal was critical in terms of oligosaccharide structure.
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PMID:Alterations in the structure of the oligosaccharide of vesicular stomatitis virus G protein by swainsonine. 629 70

When mouse L-cells are infected with vesicular stomatitis virus, there is a decrease in the rate of protein synthesis ranging from 20 to 85% of that in mock-infected cells. Vesicular stomatitis virus, irradiated with increasing doses of UV light, eventually loses this capacity to inhibit protein synthesis. The UV inactivation curve was biphasic, suggesting that transcription of two regions of the viral genome is necessary for the virus to become inactivated in this capacity. The first transcription product corresponded to about 373 nucleotides, and the second corresponded to about 42 nucleotides. Inhibition of transcription of the larger product by irradiating the virus with low doses of UV light left a residual inhibition of protein synthesis consisting of approximately 60 to 65% of the total inhibition. This residual inhibition could be obviated by irradiating the virus with a UV dose of greater than 20,000 ergs/mm(2) and was thus considered to represent the effect of the smaller transcription product. In the R1 mutant of C. P. Stanners et al. (Cell 11:273-281, 1977), inhibition of transcription of the larger product sufficed to restore protein synthesis to the mock-infected level, suggesting that the smaller transcription product is nonfunctional with respect to protein synthesis inhibition. It thus appears that the inhibition of protein synthesis by wild-type vesicular stomatitis virus involved at least two separate viral transcription products, and the inhibition by the R1 mutant involved only one. Extracts from cells infected with virus irradiated with low doses of UV light showed a protein synthesis capacity quite similar to that of their in vivo counterparts, indicating that these extracts closely reflect the in vivo effects of virus infection.
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PMID:Two transcription products of the vesicular stomatitis virus genome may control L-cell protein synthesis. 630 Apr 25

A technique which detects viral DNA or RNA in situ in the organ systems of whole mice is described. Frozen thin sections from whole mice were transferred directly to nitrocellulose and hybridized to labeled viral DNA, allowing the detection of viral DNA or RNA. By this procedure, polyomavirus infection of newborn mice inoculated intranasally was followed. We found that the initial inoculum could be detected in the nasal cavity, lungs, and stomach lining after a 5-h absorption period. Primary replication of virus was observed in the nasal cavity, submaxillary gland, and lungs, followed by a systemic phase of infection in which the liver, spleen, kidney, and large colon also became infected. Viral RNA as well as DNA could also be detected as shown by infecting mice intracerebrally with vesicular stomatitis virus. Vesicular stomatitis virus-specific RNA was observed only in the brains of these mice. It is most likely that this technique can be applied to general molecular studies of mice. With this method we should be able to detect all viruses, bacteria, plasmids, and organ-specific transcripts to which a cloned probe exists.
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PMID:Detection of DNA and RNA virus genomes in organ systems of whole mice: patterns of mouse organ infection by polyomavirus. 632 7

Vesicular stomatitis virus ribonucleoproteins (RNP) obtained by a detergent treatment of purified virus (vRNP) or from infected HeLa cell cytoplasm (icRNP) were examined by sedimentation in sucrose or Renografin gradients in the presence or absence of EDTA. It was shown that vRNP and icRNP sediment at the same rate in sucrose and Renografin in the absence of EDTA; however, icRNP sedimented more slowly in the presence of EDTA than did vRNP. Polyacrylamide gel electrophoresis of the proteins of vRNA and icRNP recovered from EDTA-containing gradients demonstrated that both RNP structures contained L, N, and NS proteins in the same proportion. Electron microscopy of both RNP structures, in the absence of EDTA, demonstrated that both exist as helical structures approximately 20 by 700 nm. However, in the presence of EDTA the icRNP was completely uncoiled with a mean length of 4,095 nm, whereas vRNP was hardly affected. The addition of excess Mg(2+) or Mn(2+) to uncoiled icRNP preparations partially restored the coiled configuration. These observations suggest that the change in sedimentation of icRNP in the presence of EDTA is due to a change from a coiled to an uncoiled conformation, that icRNP and vRNP are not structurally identical, and that icRNP must undergo a conformational change during maturation of VSV from the 20-by-700-nm intracellular form to the 50-by-175-nm form found in intact virus. The icRNP containing L, N, and NS proteins (icRNP(L,N,NS)) and icRNP containing only N protein (icRNP(N)), prepared by centrifugation of icRNP(L,N,NS) in CsCl to remove L and NS, were compared by cosedimentation in sucrose gradients. There was a decrease in sedimentation rate of icRNP(N) due to loss of L and NS. This sedimentation difference was also apparent in the presence of EDTA; however, both icRNP(L,N,NS) and icRNP(N) sedimented at a much slower rate in the presence of EDTA, and by electron microscopy both were completely uncoiled. These observations suggest that N protein alone is responsible for the 20-by-700-nm coiled structure and that the divalent cation interactions disrupted by EDTA are N-N or N-RNA interactions. These results are discussed with regard to vesicular stomatitis virus maturation.
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PMID:Comparison o;f vesicular stomatitis virus intracellular and virion ribonucleoproteins. 677 8

Vesicular stomatitis and rabies viruses enter cells through receptor-mediated endocytosis, followed by fusion of the viral with the endosomal membrane. The latter step is catalyzed by the viral envelope glycoprotein, which, in the low pH environment of the endosome, undergoes a conformational transition to a fusion-competent state. To investigate whether fusion competence involves the low pH exposure of a hydrophobic fusion region(s), we have applied hydrophobic photolabeling using the recently developed phospholipid analogue 1-O-hexadecanoyl-2-O-[9-[[[2-[125I]iodo-4-(trifluoromethyl-3H- diazirin-3-yl)benzyl]oxy]carbonyl] nonanoyl]-sn-glycero-3-phosphocholine ([125I]TID-PC/16) (Weber, T., and Brunner, J. (1995) J. Am. Chem. Soc. 117, 3084-3095). Rosettes of rabies virus glycoprotein, whole rabies virus, or vesicular stomatitis virus were incubated with large unilamellar vesicles containing [125I]TID-PC/16. Following reagent activation, the labeled glycoprotein was isolated and analyzed. In all cases, labeling of the glycoprotein strongly increased as the pH was lowered from 7.0 to 6.0, suggesting the exposure at acidic pH of a domain capable of interacting with membranes. To identify the labeled region(s), CNBr fragments were generated and analyzed by SDS-polyacrylamide followed by autoradiography. In rabies glycoprotein, the labeled segment was found to be contained within fragment RCr5 (residues 103-179). Glycoprotein from vesicular stomatitis virus was labeled within fragment VCr1 (residues 59-221). These results demonstrate that rhabdovirus glycoprotein contains a domain that at low pH is capable of interacting with a target membrane in a hydrophobic manner. This domain may play a role similar to that of the fusion peptide found in many other viral fusion proteins.
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PMID:Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses. 761 63

The biology, veterinary importance and control of certain Nematocera are described and discussed. Culicoides spp. (family Ceratopogonidae) transmit the arboviruses of bluetongue (BT), African horse sickness (AHS), bovine ephemeral fever (BEF) and Akabane. Some other arboviruses have been isolated from these species, while fowl pox has been transmitted experimentally by Culicoides. These insects are vectors of the parasitic protozoans Leucocytozoon caulleryi and Haemoproteus nettionis, and the parasitic nematodes Onchocerca gutturosa, O. gibsoni and O. cervicalis. They also cause recurrent summer hypersensitivity in horses, ponies, donkeys, cattle and sheep. Farm animals can die as a result of mass attack by Simulium spp., which are also vectors of Leucocytozoon simondi, L. smithi and the filariae O. gutturosa, O. linealis and O. ochengi. Venezuelan equine encephalomyelitis (VEE) and Rift Valley fever (RVF) have been isolated from simuliids, and vesicular stomatitis virus New Jersey strain has been replicated in Simulium vittatum. Simuliids are well known as vectors of O. volvulus, the cause of human onchocercosis (river blindness). The family Psychodidae includes the genera Phlebotomus and Lutzomyia (subfamily Phlebotominae), vectors of Leishmania spp. in humans, dogs and other mammals. Vesicular stomatitis virus Indiana strain has been regularly isolated from phlebotomine sandflies. Mass attack by mosquitoes can also prove fatal to farm animals. Mosquitoes are vectors of the viruses of Akabane, BEF, RVF, Japanese encephalitis, VEE, western equine encephalomyelitis, eastern equine encephalomyelitis and west Nile meningoencephalitis, secondary vectors of AHS and suspected vectors of Israel turkey meningoencephalitis. The viruses of hog cholera, fowl pox and reticuloendotheliosis, the rickettsiae Eperythrozoon ovis and E. suis, and the bacterium Borrelia anserina are mechanically transmitted by mosquitoes. These insects also induce allergic dermatitis in horses. They transmit several filarial worms of both animals and humans, and are of great medical importance as vectors of major human diseases, including malaria, yellow fever, dengue fever and many more diseases caused by arboviruses.
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PMID:Nematocera (Ceratopogonidae, Psychodidae, Simuliidae and Culicidae) and control methods. 771 9

Interferon-gamma (IFN-gamma) and a type I IFN (spI IFN) are transiently coexpressed by trophoblastic cells of pig conceptuses at implantation between day 12 and day 20 of gestation. The local effects of these trophoblastic IFNs were examined on endometrial cells and on trophoblast by measuring antiviral activity and the induction of (2',5')-oligoadenylate synthetase activity. Trophoblastic vesicles were shown to be susceptible to infection by vesicular stomatitis virus and transmissible gastroenteritis virus. Vesicular stomatitis virus multiplied by about 1000 times in trophoblastic vesicles, and endogenous trophoblastic IFNs or exogenous recombinant IFN-gamma or spI IFN had no effect on virus production. No (2',5')-oligoadenylate synthetase activity could be measured on the trophoblast, even after treatment with IFN-gamma or spI IFN. These results clearly show that trophoblastic IFNs cannot induce antiviral resistance or (2',5')-oligoadenylate synthetase activity in the trophoblast, suggesting that these IFNs have no autocrine function. Endometrial epithelial and stromal cells in primary cultures displayed distinct sensitivity to the antiviral effect of IFN-gamma and spI IFN. Stromal fibroblasts were highly sensitive to spI IFN but weakly sensitive to IFN-gamma; epithelial cells were sensitive to both IFNs. The same sensitivity pattern was obtained when measuring the (2',5')-oligoadenylate synthetase activity. Flushing fluid, containing IFN-gamma and type I IFN, was a potent inducer of antiviral effect and (2',5')-oligoadenylate synthetase activity. It is therefore postulated that the endometrial epithelium is the most likely target of trophoblastic IFNs. It is possible that these IFNs play a role in the viral protection of conceptuses.
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PMID:Paracrine activities of porcine trophoblastic interferons. 779 12

Vesicular stomatitis virus infection causes a rapid and potent inhibition of both host transcription and translation. Recently, the viral matrix (M) protein was shown to inhibit host-directed transcription in vivo in the absence of any other viral component (B. L. Black and D. S. Lyles, J. Virol. 66:4058-4064, 1992). The goal of this study was to determine the effect of M protein on host-directed translation. In vitro-transcribed mRNAs encoding M protein and chloramphenicol acetyltransferase (CAT) were cotransfected into BHK cells to determine the effect of M protein expression on translation of CAT mRNA. The results presented here show that M protein did not inhibit host-directed translation of CAT mRNA. On the contrary, this study gave the unexpected result that M protein actually stimulated host-directed translation under the same conditions in which it potently inhibited host-directed transcription. Under these conditions, the combined effect on host gene expression was a greater-than-20-fold inhibition. Furthermore, the enhancement of host translation mediated by M protein was genetically correlated with M protein's ability to inhibit host transcription. Thus, the results of this study establish that M protein does not inhibit host protein synthesis under the same conditions in which it potently inhibits host transcription and suggest that the inhibition of transcription and that of translation by vesicular stomatitis virus require separate viral gene products.
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PMID:Effect of vesicular stomatitis virus matrix protein on host-directed translation in vivo. 825 71

Vesicular stomatitis is a viral disease of cattle, pigs, and horses. The disease is characterized by vesicular lesions on the epithelium of the mouth, feet, and teats. The pathological lesions are virtually indistinguishable from that of foot-and-mouth disease. We have developed a recombinant baculovirus that expresses the nucleocapsid (N) protein of the New Jersey serotype of vesicular stomatitis virus (VSVNJ) in insect cells (Sf9) and larvae (Spodoptera exigua). The gene was expressed under control of the polyhedrin promoter as a fusion or nonfusion protein. The recombinant N protein expressed in insect cells could not be distinguished from N protein produced in VSVNJ-infected CHO cells by immunological and biochemical analyses. The level of expression of N as a percentage of the total protein in Sf9 cells was 41% for the fusion and 60% for the nonfusion protein. Higher level (68%) of expression of the nonfusion N protein was obtained in larvae. Recombinant N protein was used in an ELISA to distinguish animals vaccinated with a recombinant VSV glycoprotein from those exposed to the whole virus by infection or classical vaccine. Lysate of a single infected larva (0.2-0.3 g) was adequate for coating ELISA plates to perform 10,000 serum assays in duplicate.
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PMID:Immunological characterization of the VSV nucleocapsid (N) protein expressed by recombinant baculovirus in Spodoptera exigua larva: use in differential diagnosis between vaccinated and infected animals. 839 Jul 53


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