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)

Sindbis and vesicular stomatitis viruses were grown in a line (termed 15B) of Chinese hamster ovary (CHO) cells that is deficient in a specific UDP-N-acetyl-glucosamine:glycoprotein N-acetylglucosaminyltransferase. Both viruses replicated normally in the cell line, but the glycoproteins of the released virus migrated faster on sodium didecyl sulfate-polyacrylamide gels than did glycoproteins of virus grown in parent CHO cells. Digestion of the viral glycoproteins with Pronase followed by gel filtration demonstrated that the glycoproteins with Pronase followed by gel filtration demonstrated that the glycopeptides of Sinbis-15B virus were much smaller than the glycopeptides of Sindbis-CHO virus. In addition, Sindbis-15B viral glycopeptides but not Sindbis-CHO viral glycopeptides contained terminal alpha-mannose residues as shown by their susceptibility to alpha-mannosidase digestion. These findings demonstrate that the oligosaccharide units of the glycoproteins of vesicular stomatitis and Sinbis viruses are altered when the viruses are grown in 15B cells. We conclude that the N-acetylglucosaminyltransferase that is missing in 15B cells normally participates in the biosynthesis of the oligosaccharide units of the viral glycoproteins, and in the absence of this enzyme incomplete oligosaccharide chanis are produced. Viruses released from 15B cells appear to retain full infectivity; Sindbis-15B virus, however, showed a significant decrease in hemagglutination titer compared with that of Sindbis-CHO virus.
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PMID:Growth of enveloped RNA viruses in a line of chinese hamster ovary cells with deficient N-acetylglucosaminyltransferase activity. 17 86

The synthesis of the complex-type oligosaccharide unit of the vesicular stomatitis virus G protein is initiated by the en bloc transfer of a high molecular weight oligosaccharide from a lipid carrier to the nascent polypeptide. Following transfer the oligosaccharide is "processed" by removal of glucose and mannose residues and the sugars that constitute the outer branches of the complex-type oligosaccharide are added. The structure of the oligosaccharide moiety of the lipid-linked precursor has been elucidated in order to further define the steps involved in processing. Since it was not feasible to obtain adequate amounts of material for standard structural studies, most of the structural studies were performed on radiolabeled material, with radioactivity incorporated differentially into glucose, mannose, and N-acetylglucosamine. Based on endo-beta-N-acetylglucosaminidase CII digestion, alpha-mannosidase digestion, acetolysis, Smith periodate degradation, methylation analysis, and periodate oxidation, we propose the following structure for the oligosaccharide moiety of the lipid-linked oligosaccharide.
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PMID:The synthesis of complex-type oligosaccharides. I. Structure of the lipid-linked oligosaccharide precursor of the complex-type oligosaccharides of the vesicular stomatitis virus G protein. 21 34

Lec23 Chinese hamster ovary (CHO) cells have been shown to possess a unique lectin resistance phenotype and genotype compared with previously isolated CHO glycosylation mutants (Stanley, P., Sallustio, S., Krag, S. S., and Dunn, B. (1990) Somatic Cell Mol. Genet. 16, 211-223). In this paper, a biochemical basis for the lec23 mutation is identified. The carbohydrates associated with the G glycoprotein of vesicular stomatitis virus (VSV) grown in Lec23 cells (Lec23/VSV) were found to possess predominantly oligomannosyl carbohydrates that bound strongly to concanavalin A-Sepharose, eluted 3 sugar eq beyond a Man9GlcNAc marker oligosaccharide on ion suppression high pressure liquid chromatography, and were susceptible to digestion with jack bean alpha-mannosidase. Monosaccharide analyses revealed that the oligomannosyl carbohydrates contained glucose, indicating a defect in alpha-glucosidase activity. This was confirmed by further structural characterization of the Lec23/VSV oligomannosyl carbohydrates using purified rat mammary gland alpha-glucosidase I, jack bean alpha-mannosidase, and 1H NMR spectroscopy at 500 MHz. [3H]Glucose-labeled Glc3Man9GlcNAc was prepared from CHO/VSV labeled with [3H]galactose in the presence of the processing inhibitors castanospermine and deoxymannojirimycin. Subsequently, [3H]Glc2Man9GlcNAc was prepared by purified alpha-glucosidase I digestion of [3H]Glc3Man9GlcNAc. When these oligosaccharides were used as alpha-glucosidase substrates it was revealed that Lec23 cells are specifically defective in alpha-glucosidase I, a deficiency not previously identified among mammalian cell glycosylation mutants.
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PMID:A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I. 166 Apr 60

The role of N-acetylneuraminic acid and N-acetyl-D-glucosamine containing molecules in vesicular stomatitis virus-cell interaction was studied using specific lectins (limulin and wheat germ agglutinin) and esoglycosidases (neuraminidase, beta-galactosidase, alpha-mannosidase, alpha-fucosidase, beta-N-acetyl-D-glucosaminidase). Lectin treatment of vesicular stomatitis virus (VSV) indicated that carbohydrates of the VSV G envelope glycoprotein were not required for virus infectivity, whereas sialic acid appeared directly involved in the attachment of virus to erythrocytes. The comparative results obtained after enzymatic digestion of cell membrane carbohydrates or their cross linking by lectins demonstrated that whereas VSV infectivity was strongly reduced by pretreatment of chick embryo cells, virus binding to erythrocytes was unaffected by such treatments. We conclude that sugar residues may participate at the host cell attachment site which differs, at least in part, from the membrane binding site of erythrocytes.
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PMID:Involvement of carbohydrates in vesicular stomatitis virus-cell early interaction. 257 93

The synthesis and oligosaccharide processing of the glycoproteins of SA11 rotavirus in infected Ma104 cells was examined. Rotavirus assembles in the rough endoplasmic reticulum (RER) and encodes two glycoproteins: VP7, a component of the outer viral capsid, and NCVP5, a nonstructural protein. A variety of evidence suggests the molecules are limited to the ER, a location consistent with the high mannose N-linked oligosaccharides modifying these proteins. VP7 and NCVP5 were shown to be integral membrane proteins. In an in vitro translation system supplemented with dog pancreas microsomes, they remained membrane associated after high salt treatment and sodium carbonate-mediated release of microsomal contents. In infected cells, the oligosaccharide processing of these molecules proceeded in a time-dependent manner. For VP7, Man8GlcNAc2 and Man6GlcNAc2 were the predominant intracellular species after a 5-min pulse with [3H]mannose and a 90 min chase, while in contrast, trimming of NCVP5 halted at Man8GlcNAc2. VP7 on mature virus was processed to Man5GlcNAc2. It is suggested that the alpha-mannosidase activities responsible for the formation of these structures reside in the ER. In the presence of the energy inhibitor carbonyl cyanide m-chlorophenylhydrazone (CCCP), processing of VP7 and the vesicular stomatitis virus G protein was blocked at Man8GlcNAc2. After a 20-min chase of [3H]mannose-labeled molecules followed by addition of CCCP, trimming of VP7 could continue while processing of G protein remained blocked. Thus, an energy-sensitive translocation step within the ER may mark the divergence of the processing pathways of these glycoproteins.
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PMID:Processing of the rough endoplasmic reticulum membrane glycoproteins of rotavirus SA11. 299 4

Transport of the vesicular stomatitis virus-encoded glycoprotein (G protein) between the endoplasmic reticulum (ER) and the cis Golgi compartment has been reconstituted in a cell-free system. Transfer is measured by the processing of the high mannose (man GlcNAc2) ER form of G protein to the man5GlcNAc5 form by the cis Golgi enzyme alpha-mannosidase I. G protein is rapidly and efficiently transported to the Golgi complex by a process resembling that observed in vivo. G protein is trimmed from the high mannose form to the man5GlcNAc2 form without the appearance of the intermediate man GlcNAc2 oligosaccharide species, as is observed in vivo. G protein is found in a sealed membrane-bound compartment before and after incubation. Processing in vitro is sensitive to detergent, and the Golgi alpha-mannosidase I inhibitor 1-deoxymannorjirimycin. Transport between the ER and Golgi complex in vitro requires the addition of a high speed supernatant (cytosol) of cell homogenates, and requires energy in the form of ATP. Efficient reconstitution of export of protein from the ER requires the preparation of homogenates from mitotic cell populations in which the nuclear envelope, ER, and Golgi compartments have been physiologically disassembled before cell homogenization. These results suggest that the high efficiency of transport observed here may require reassembly of functional organelles in vitro.
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PMID:Reconstitution of transport of vesicular stomatitis virus G protein from the endoplasmic reticulum to the Golgi complex using a cell-free system. 302 44

We have examined the effects of deoxynojirimycin and castanospermine, compounds known to inhibit the removal of glucose from high mannose asparagine-linked oligosaccharides, on the formation of Sindbis virus. These drugs inhibited virion formation in baby hamster kidney (BHK) cells, 15B - the CHO cell line that lacks GlcNAc transferase activity, and chicken embryo fibroblasts, although our results with the latter cells were variable. We analyzed the [3H]mannose-labeled oligosaccharides from Sindbis virus infected 15B cells. Those from control cells were predominantly GlcNAc2Man5. Oligosaccharides from the treated cells were larger than the Man5 species and as expected, were partially resistant to alpha-mannosidase. The growth of Sindbis virus was inhibited to a much greater extent at 37 degrees C than at 30 degrees C in BHK cells treated with either deoxynojirimycin or castanospermine. Both of these compounds also inhibited the proteolytic cleavage of the viral glycoprotein precursor, PE2, to the virion glycoprotein, E2, but did not prevent the migration of the glycoprotein to the cell surface. These results, taken together with our earlier studies with vesicular stomatitis virus (Schlesinger et al., 1984) provide strong evidence that the removal of glucose residues during the processing of asparagine-linked oligosaccharides is critical for some proteins to achieve a functional conformation.
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PMID:The effects of inhibitors of glucosidase I on the formation of Sindbis virus. 315 36

The glycosylation of the G-protein was analyzed in vesicular stomatitis virus-infected baby hamster kidney cells incubated in the absence of glucose. The results indicate that the G-protein in glucose-starved cells is initially glycosylated from a lipid donor with a glucosylated oligosaccharide which is resistant to endo-beta-N-acetylglucosaminidase H and partially susceptible to alpha-mannosidase. With longer times, the protein-bound carbohydrate chain becomes much more sensitive to alpha-mannosidase while remaining endo-beta-N-acetylglucosaminidase H-resistant. Purified virions from glucose-starved baby hamster kidney cells, labeled with [35S]methionine and isolated on a sucrose gradient, contain altered forms of the G-protein, whereas the other viral proteins remain unchanged. These altered forms could also be radiolabeled with [3H]mannose, and upon analysis of labeled glycopeptides by chromatography on concanavalin A-Sepharose and Bio-Gel P-6, it was apparent that modification of the oligosaccharide portion of the G-protein occurs in baby hamster kidney cells, leading to aberrant mature carbohydrate chains.
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PMID:Altered G-protein glycosylation in vesicular stomatitis virus-infected glucose-deprived baby hamster kidney cells. 628 41

An earlier report suggested that SS33410, structurally related to folimycin and bafilomycin A(1), blocked secretion of the glycoprotein (G protein) of vesicular stomatitis virus (VSV) into the medium and, instead, G protein was accumulated intracellulary. To identify the inhibition site of SS33410 in intracellular protein transport, I have analyzed the oligosaccharide chain structure of the intracellularly accumulated G protein. In SS33410-treated VSV-infected cells, G protein oligosaccharide was suggested to have a composition of GlcNAc-Man(5)-GlcNAc(2) as analyzed by Bio-Gel P-4 column chromatography following digestion with alpha-mannosidase, beta-N-acetylhexosaminidase, and then with alpha-mannosidase. SS33410 specifically inhibited vacuolar-type ATPase (V-ATPase). These studies thus suggest that SS33410 blocks the intracellular protein transport before the step of trimming by mannosidase II, which is confined to the medial Golgi compartment.
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PMID:SS33410, an inhibitor of V-ATPase, blocks intracellular protein transport of the VSV-G protein in the Golgi compartment. 1473 Jan 37