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)

The infectivity of herpes simplex virus type 1 (HSV-1) was inactivated after treatment with either concanavalin A (ConA) or periodate. Phytohemagglutinin, wheat germ agglutinin, pokeweed mitogen, and neuraminidase failed to inactivate the virus. The effect of ConA could be specifically inhibited or reversed by the addition of alpha-methyl-d-glucoside or alpha-methyl-d-mannoside. Evidence was obtained that HSV-1 inactivated by ConA could adsorb to host cells. Viral aggregation was not a major mechanism in the inactivation of HSV-1 by ConA. Under the experimental conditions employed, inactivation of HSV-1 was faster by ConA than by antiserum and less temperature dependent. A ConA-resistant fraction was detected which appeared to adsorb less quickly than untreated virus, and penetration of ConA-resistant fraction was strikingly slow. The presence of aggregates in the virus preparation did not appear to account for the ConA-resistant fraction. Inactivation of viral infectivity by ConA was obtained only with enveloped viruses, since HSV-1, HSV-2, pseudorabies, and vesicular stomatitis virus were inactivated and vaccinia and echovirus type 6 were not.
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PMID:Inactivation of herpes simplex virus by concanavalin A. 436 3

Neuraminidase free of proteolytic activity substantially reduced the infectivity of vesicular stomatitis (VS) virus but less effectively than trypsin. The only sugar residue hydrolyzed by neuraminidase was N-acetyl neuraminic acid, approximately 89% of which was liberated from virion glycoprotein and the rest from virion glycolipid. Desialylation of virion glycoprotein but not of glycolipid resulted in progressive loss of infectivity. Sialyl transferase prepared and partially purified from BHK-21 cells catalyzed resialylation by CMP-[(14)C]sialic acid of the glycoprotein of neuraminidase-treated VS virions and supersialylation of unhydrolyzed VS viral glycoprotein. Resialylation of desialylated VS virions resulted in substantial (26-fold) restoration of their infectivity. We conclude that terminal neuraminic acids of VS viral sialoglycoprotein play an important role in initiation of infection with this virus.
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PMID:Sialoglycoprotein of vesicular stomatitis virus: role of the neuraminic acid in infection. 436 3

Influenza virus particles bind rapidly to vesicular stomatitis, Sindbis, or Rauscher murine leukemia virus particles, forming mixed aggregates demonstrable by electron microscopy. The normal hemagglutinating property of influenza virus is inhibited by these viruses, providing a rapid quantitative assay. Prior treatment with neuraminidase blocks the ability of other viruses to inhibit influenza virus hemagglutination.
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PMID:Hemagglutination-inhibition: rapid assay for neuraminic acid-containing viruses. 437

The kinetics of intracellular transport of the vesicular stomatitis virus (VSV) glycoprotein (G) and the Newcastle disease virus (NDV) hemagglutinin-neuraminidase (HN) glycoprotein in chicken embryo cells were compared. To assay for the appearance of pulse-labelled glycoprotein at the cell surface, an antibody-binding assay was developed which allowed the precipitation of only those molecules on the outside surfaces of infected cells. Using this assay, it was found that pulse-labelled VSV G protein appeared at the cell surface with a half-time of approximately 27 min, while pulse-labelled NDV HN glycoprotein reached the cell surface with a half-time of approximately 78 min. To determine the transit time of these glycoproteins to trans-Golgi membranes, the kinetics of the acquisition of endoglycosidase H resistance was analyzed. The half-time of the transit of the G protein to the trans-Golgi membranes was found to be approximately 13 min while that of the HN glycoprotein was found to be approximately 60 min. Since the G protein migrates to the trans-Golgi membranes with a half-time of 13 min, and the cell surface with a half-time of 27 min, the half-time for the transit between the trans-Golgi membrane and the plasma membrane must be approximately 14 min. In a similar analysis, the half-time for the transit of the HN glycoprotein from the trans-Golgi membrane to the plasma membrane must be approximately 18 min, a time not significantly different from that of the G protein. Thus the difference in the kinetics of the intracellular transport of these two glycoproteins resides primarily in the transit from the rough endoplasmic reticulum to the trans-Golgi membranes. These results argue against a non-selective mechanism for the transport of plasma membrane glycoproteins to the cell surface.
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PMID:Intracellular processing of the vesicular stomatitis virus glycoprotein and the Newcastle disease virus hemagglutinin-neuraminidase glycoprotein. 609 58

An altered baby hamster kidney cell culture which resists the c.p.e. of HVJ (haemagglutinating virus of Japan - the Sendai strain of parainfluenza I virus) has been obtained and characterized. These cells, designated BHK-R, were originally obtained by prolonged cultivation of cells surviving HVJ infection; they have been subcultured in the presence of HVJ. No infectious virus was recovered from BHK-R cells and no evidence for the presence of HVJ antigens in the cells was demonstrated by immunofluorescent staining. When BHK-R cells were inoculated with HVJ the growth of challenge virus was suppressed and no obvious cytopathic changes were detected, while these cells normally supported the replication of mumps, influenza, Newcastle disease, vesicular stomatitis or Sindbis viruses. BHK-R cells became susceptible to HVJ infection after serial subculture in growth medium free of HVJ. It was suggested that sialic acid residues present in the surface of BHK-R cell membranes and responsible for adsorption of HVJ were split off by the action of neuraminidase of virus particles, resulting in inhibition of the attachment of challenge virus of HVJ.
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PMID:Characterization of altered BHK cells resistant to HVJ (Sendai virus) infection. 615 23

The glycoprotein (G) of vesicular stomatitis virus (VSV) was radiolabelled, extracted and purified so that its potential interaction with host cell surfaces could be studied. When BHK-21 cells were incubated with the radiolabelled virus glycoprotein, the virus component rapidly attached to the cell surface. The attachment was shown to be temperature-dependent adn saturated at approx. 3 X 10(5) molecules/cell. The omission of Mg2+ or Ca2+ from the incubation medium had little effect on the glycoprotein binding. Treating the isolated G protein and intact virions with neuraminidase did not significantly decrease their binding to BHK-21 cells. Pre-incubating cells with trypsin did not decrease the attachment of VSV virions nor the binding of purified G protein. Treating cells with phospholipase A or phospholipase C suggested that the binding of the glycoprotein and the intact virion might have been dissimilar. Unlabelled glycoprotein competitively inhibited binding of the labelled molecules although the presence of intact virions did not inhibit attachment of the G protein. Likewise, saturating amounts of the glycoprotein did not decrease binding of VSV to BHK-21 cells. These observations suggested that either the isolated glycoprotein bound to cell surface components that were distinct from the virion receptor or that the manner of the purified glycoprotein attachment differed from the G protein still associated with the intact virion. Chemical crosslinking and diagonal two-dimensional gel electrophoresis were used to identify and to compare the cell surface components responsible for glycoprotein and virion attachment.
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PMID:Isolation of the glycoprotein of vesicular stomatitis virus and its binding to cell surfaces. 625 23

The major surface glycoprotein (G) of vesicular stomatitis virus (VSV) was purified and incorporated into lipid vesicles containing the purified hemagglutinin-neuraminidase (HN) and fusion (F) glycoproteins of Sendai Virus. These lipid vesicles were then used to modify the render target cells susceptible to lysis by anti-VSV cytotoxic T lymphocytes. The results obtained provide direct evidence that the G protein is a target antigen for specific and cross-reactive anti-VSV cytotoxic T lymphocytes. The significance of this work is discussed.
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PMID:Cross-reactive anti-vesicular stomatitis virus (VSV) cytotoxic T lymphocytes recognize the major surface glycoprotein. 626 37

Based on subcellular fractionation data, the following maturation pathways were proposed for the Newcastle disease virus glycoproteins. During or shortly after synthesis in rough endoplasmic reticulum, hemagglutinin-neuraminidase (HN) and fusion (F0) glycoproteins underwent dolichol pyrophosphate-mediated glycosylation, and HN assumed a partially trypsin-resistant conformation. HN began to associate into disulfide-linked dimers in rough endoplasmic reticulum, and at least one of its oligosaccharide side chains was processed to a complex form en route to the cell surface. During migration in intracellular membranes, F0 was proteolytically cleaved to F1.2. Neither HN nor F1,2 required oligosaccharide side chains for migration to plasma membranes, and cleavage of F0 also occurred without glycosylation. Virion- and plasma membrane-associated HN contained both complex and high-mannose oligosaccharide chains on the same molecule, and F1,2 contained at least high-mannose forms. Several of the properties of HN were notable for a viral glycoprotein. The oligosaccharide side chains of HN were modified very slowly in chick cells, whereas those of the G glycoprotein of vesicular stomatitis virus were rapidly processed to a complex form. Therefore, their different rates of migration and carbohydrate processing were intrinsic properties of these glycoproteins. Consistent with its slow maturation, the HN glycopolypeptide accumulated to high levels in intracellular membranes as well as in plasma membranes. Intracellular HN contained immature oligosaccharide side chains, suggesting that it accumulated in the pre-Golgi/Golgi segment of the maturation pathway. The major site of accumulation of mature HN with neuraminidase activity was the plasma membrane.
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PMID:Maturation of the envelope glycoproteins of Newcastle disease virus on cellular membranes. 628 83

Recently we described a saturable, high-affinity binding site for vesicular stomatitis virus (VSV) on the surface of Vero cells that appears to mediate viral infectivity. To isolate this binding site, we have extracted Vero cells with the detergent, octyl-beta-D-glucopyranoside. The dialyzed detergent extract specifically inhibits the saturable, high-affinity binding of 35S-methionine-labeled VSV to Vero cells. The inhibitory activity is resistant to protease, neuraminidase and heating to 100 degrees C. It is soluble in chloroform-methanol and inactivated by phospholipase C, suggesting that it is a phospholipid. Of various purified lipids tested, only phosphatidylserine was capable of totally inhibiting the high-affinity binding of VSV. The half-maximal inhibitory concentration for phosphatidylserine was 1 microM. Phosphatidylserine also inhibited VSV plaque formation by 80%-90%; Herpes simplex virus plaque formation was unaffected. Centrifugation and electron microscopy studies have shown that phosphatidylserine-containing liposomes bind to VSV. The finding that phosphatidylserine directly binds to VSV and inhibits VSV attachment and infectivity suggests that plasma membrane phosphatidylserine could function as a binding site or portion of a binding site for VSV.
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PMID:Inhibition of VSV binding and infectivity by phosphatidylserine: is phosphatidylserine a VSV-binding site? 629 4

A specific, saturable receptor for rabies virus was analyzed on cultured cells of neural or non-neural origin. Viral attachment kinetics were enhanced by DEAE-dextran, an effect which in turn enhanced the apparent infectivity of the virus inoculum. Under optimized conditions, the attachment of metabolically labeled ERA strain rabies virus obeyed the laws of mass action, whereby the amount of virus bound to cells varied proportionally with the concentration of cells or virus. Attachment was sensitive to changes of temperature and pH, did not require divalent cations such as Mg2+ or Ca2+, and occurred despite prior treatment of cells with proteolytic or sialic acid-specific enzymes. Saturation of the cell surface with rabies virus could be accomplished with 3 X 10(3) to 15 X 10(3) attached virions per cell. Competition for the rabies receptor occurred with rabies nonpathogenic variant virus, RV194 -2, and vesicular stomatitis virus. Reovirus type 3, another neurotropic virus, failed to inhibit rabies virus binding, and West Nile virus only slightly inhibited rabies virus binding, suggesting independent cellular receptors were recognized by these viruses. Isolated rabies virus glycoprotein failed to compete in an equivalent manner. However, solubilization of BHK-21 cells with octylglucoside yielded a chloroform-methanol-soluble extract which blocked rabies virus attachment. The binding inhibition activity of this extract was resistant to proteases but could be destroyed by phospholipases and neuraminidase, suggesting a phospholipid or glycolipid component at the receptor site. These data provide evidence for a rhabdovirus-common mechanism for cellular attachment to cells in culture.
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PMID:Characterization of saturable binding sites for rabies virus. 672 88


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