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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When vesicular stomatitis virus-infected baby hamster kidney cells were treated with rabbit anti-vesicular stomatitis virus serum, there was a loss of the viral glycoprotein G into acid-soluble products. This degradation occurred within minutes at 37 degrees C and required the presence of G protein at the cell surface. The degree of degradation depended on antiserum concentration. The antiserum, also, prevented maturation of extracellular virions and induced partial degradation of the intracellular viral proteins, without affecting host proteins. The degradation could not be prevented by the presence of lysosomotropic agents, protease inhibitors, colchicine, or cytochalasin B. Similar kinetics and specificity of degradation was obtained with cells infected with vesicular stomatitis virus mutants that were less cytopathic. These results characterize a model system for studying the parameters and consequences of antigenic modulation as well as for studying the fate of viral antigens during persistent infections.
Mol Cell Biol 1983 Sep
PMID:Antibody-induced modulation of proteins in vesicular stomatitis virus-infected fibroblasts. 631 22

We constructed a molecular clone encoding the N-terminal 379 amino acids of the polyomavirus middle-size tumor antigen, followed by the C-terminal 60 amino acids of the vesicular stomatitis virus glycoprotein G. This hybrid gene contained the coding region for the C-terminal hydrophobic membrane-spanning domain of the G protein in place of the C-terminal hydrophobic domain of the middle-size tumor antigen. The hybrid gene was expressed in COS-1 cells under the control of the simian virus 40 late promoter. The hybrid protein was located in cell membranes and was associated with a tyrosine-specific protein kinase activity, as was the middle-size tumor antigen. Plasmids encoding the hybrid protein failed to transform mouse NIH 3T3 or rat F2408 cells.
Mol Cell Biol 1984 Feb
PMID:Construction and expression of a recombinant DNA gene encoding a polyomavirus middle-size tumor antigen with the carboxyl terminus of the vesicular stomatitis virus glycoprotein G. 632 57

To screen for cells with different sensitivities to interferon (IFN), NIH 3T3 mouse fibroblasts were subcloned and examined for their response to IFN treatment. Of 30 clones tested, 2 appeared to be relatively resistant to IFN, since the replication of both vesicular stomatitis virus and mengovirus was not inhibited, even in the presence of 1,000 U of IFN per ml. One resistant (A10) and one sensitive (A5) clone were further analyzed. In both clones, murine leukemia virus replication was equally inhibited by IFN, indicating the presence of functional receptors for IFN in the resistant clone. Using the (2'-5')oligoadenylate (2-5A) radiobinding assay, we could demonstrate that both clones contained the RNase L protein. Furthermore, this enzyme appears to be active, since a similar reduction in the rate of protein synthesis was evident after the introduction of exogenous 2-5A to the cells. We also analyzed the activity of another enzyme in the 2-5A pathway, namely, 2-5A synthetase. In the sensitive cells (A5), the induction of enzyme activity was proportional to the IFN concentration used, reaching a maximum of more than a 10-fold increase over the background of untreated cells. However, little if any induction over the basal activity was observed in the resistant cells (A10) when similar doses of IFN were used. It is thus probable that the lack of induction of 2-5A synthetase activity by IFN in A10 cells is at least partly responsible for their relative resistance to IFN treatment.
Mol Cell Biol 1983 Oct
PMID:Isolation and characterization of an interferon-resistant cell line deficient in the induction of (2'-5')oligoadenylate synthetase activity. 664 21

Exposure of intact cells to UV light brings about cross-linking of polyadenylated mRNA to a set of cytoplasmic proteins which are in direct contact with the mRNA in vivo. Substantial amounts of an additional protein of molecular weight 38,000 (38K) become cross-linked to the mRNA when cells are treated with inhibitors of mRNA synthesis (actinomycin D, camptothecin, and 5,6-dichloro-1-beta-D-ribofuranosyl benzimidazole) or after infection with vesicular stomatitis virus. Cordycepin, which inhibits polyadenylation but not mRNA synthesis, has no such effect. Inhibitors of protein synthesis and of rRNA synthesis are also without effect on 38K cross-linking to mRNA. The onset of the effect of inhibitors of mRNA synthesis on the UV cross-linkable interaction between mRNA and 38K is rapid and reaches a maximal level in less than 60 min, and it is completely and rapidly reversible. In cells treated with actinomycin D, the amount of 38K which becomes cross-linked to mRNA is proportional to the extent of inhibition of mRNA synthesis. The association of 38K with mRNA during transcriptional arrest does not require protein synthesis because simultaneous treatment with the protein synthesis inhibitor emetine does not interfere with it. The effectors which promote the interaction of 38K with mRNA do not affect the proteins which are in contact with polyadenylated heterogeneous nuclear RNA and do not markedly affect protein synthesis in the cell. The 38K protein can be isolated with the polyribosomal polyadenylated fraction from which it was purified, and monoclonal antibodies against it were prepared. Immunofluorescence microscopy shows mostly cytoplasmic and some nuclear staining. These observations demonstrate that commonly used inhibitors of transcription affect the physical state of messenger ribonucleoproteins in vivo.
Mol Cell Biol 1984 Mar
PMID:Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription. 671 28

The oligosaccharide processing and secretion of hepatitis B surface antigen (HBsAg) was studied in Chinese hamster ovary cells stably transfected with the gene coding HBsAg. HBsAg was secreted from cells with a relatively long half time (ca. 5 h). This appeared to be a characteristic of HBsAg itself, since HBsAg-producing cells infected with vesicular stomatitis virus transported the viral envelope glycoprotein to the cell surface with normal kinetics (half time of ca. 30 min). The secreted HBsAg was comprised of both the unglycosylated (P20) and the glycosylated (G25) polypeptides, characteristic of HBsAg isolated from human serum or secreted from other cell lines (C. W. Crowley, C.-C. Liu, and A. D. Levinson, Mol. Cell. Biol. 3:44-55, 1983; M. F. Dubois, C. Pourcel, S. Rousset, C. Chang, and P. Tiollais, Proc. Natl. Acad. Sci. U.S.A. 77:4549-4553, 1980; C.-C. Liu, D. Yansura, and A. D. Levinson, DNA, 1:213-221, 1982; G. M. Macnab, J. J. Alexander, G. Lecatsas, E. M. Bey, and J. M. Urbanocvicz, Br. J. Cancer, 24:509-515, 1976; A. M. Moriarity, B. H. Hoyer, J. W.-K. Shih, J. L. Gerin, and D. H. Hamer, Proc. Natl. Acad. Sci. U.S.A. 78:2606-2610, 1981; D. L. Peterson, J. Biol. Chem., 256:6975-6983, 1981). The glycosylated polypeptide (GP25) contained complex oligosaccharide chains. Cell-associated HBsAg also was comprised of both an unglycosylated and a glycosylated polypeptide; however, the glycosylated form (GP23) contained only high-mannose oligosaccharide chains. No oligosaccharide processing of the high-mannose chains could be detected within the cells. Thus, most of the time before secretion of HBsAg from cells must have been spent in a pre-Golgi or early Golgi compartment. Glycosylation was inhibited completely by tunicamycin, although unglycosylated particles were still secreted from cells and were antigenic. The secretion and oligosaccharide processing of HBsAg were inhibited with high concentrations of monensin, but at lower concentrations of monensin HBsAg was still secreted, although only half of the oligosaccharide chains were processed to the complex form.
 ...
PMID:Intracellular transport and secretion of hepatitis B surface antigen in mammalian cells. 674 60

Using Mitomycin C mutagenesis and negative and positive selection with monoclonal antibodies specific for H-2Kb and H-2Kbm10, respectively, a mutant cell line clone, Mitc-182, was isolated. Direct sequencing of uncloned cDNA as well as PCR based cloning and sequencing of the H-2Kb182 transcript from this mutant revealed a single G-->T transversion resulting in the substitution of Trp167 by cysteine. Serologically, the mutant Kb182 and Kbm10 are almost identical as each has lost at least five Kb specific mAb epitopes and gained several new epitopes. Interestingly, the mutant cell line, Mitc-182, is efficiently recognized by alloreactive CTLs raised in reciprocal combinations, e.g. CB6 anti Cbm10 and Cbm10 anti CB6, indicating that Kb182 contains both Kb and Kbm10 specific epitopes. The mutation has not affected the ability of Kb182 to present Kb restricted antigenic peptides of Sendai and vesicular stomatitis viruses. In addition to underscoring the importance of amino acid residue 167 in alloreactivity, these results indicate a positive correlation between the gain of both an mAb epitope and a defined alloreactive CTL epitope.
Mol Immunol 1993 Dec
PMID:A single amino acid substitution in the H-2Kb molecule generates a defined allogeneic epitope. 750 82

A brief overview is presented of progress in the development of specific inhibitors of protein kinases CKI and CKII. Two promising classes of inhibitors, which have the ability to traverse cell membranes, are now known. One of these is based on halogenated benzimidazoles and 2-aza-benzimidazoles (benzotriazoles) and some of their nucleosides. The second embraces modified isoquinoline sulfonamides, several of which are known as inhibitors of other protein kinases. Both classes include analogs that permit discrimination between CKI and CKII. Ongoing research with halogenated benzotriazoles leads to inhibitors with Ki values below 1 microM. Also considered are nucleoside triphosphate analog inhibitors and their potential properties as donors, with illustrative examples from the field of nucleoside kinases, including the apparent existence of a dual-specific viral protein/nucleoside kinase. The role of cellular CKII and viral-encoded CKII-like activities in viral replication underlines the potential of CKII inhibitors as antiviral agents, exemplified by the case of vesicular stomatitis virus.
Cell Mol Biol Res 1994
PMID:Development of inhibitors of protein kinases CKI and CKII and some related aspects, including donor and acceptor specificities and viral protein kinases. 773 15

Rubella virus (RV) envelope glycoproteins, E2 and E1, form a heterodimeric complex that is targeted to medial/trans-Golgi cisternae. To identify the Golgi targeting signal(s) for the E2/E1 spike complex, we constructed chimeric proteins consisting of domains from RV glycoproteins and vesicular stomatitis virus (VSV) G protein. The location of the chimeric proteins in stably transfected Chinese hamster ovary cells was determined by immunofluorescence, immunoelectron microscopy, and by the extent of processing of their N-linked glycans. A trans-dominant Golgi retention signal was identified within the C-terminal region of E2. When the transmembrane (TM) and cytoplasmic (CT) domains of VSV G were replaced with those of RV E2, the hybrid protein (G-E2TMCT+) was retained in the Golgi. Transport of G-E2TMCT+ to the Golgi was rapid (t1/2 = 10-20 min). The G-E2TMCT+ protein was determined to be distal to or within the medial Golgi based on acquisition of endo H resistance but proximal to the trans-Golgi network since it lacked sialic acid. Deletion analysis revealed that only the TM domain of E2 was required for Golgi targeting. Although the cytoplasmic domain of E2 was not necessary for Golgi retention, it was required for efficient transport of VSV G-RV chimeras out of the endoplasmic reticulum. When assayed in sucrose velocity sedimentations gradients, the Golgi-retained G-E2TMCT+ protein behaved as a dimer. Unlike virtually all other Golgi targeting signals, the E2 TM domain does not contain any polar amino acids. The TM and CT domains of E1 were not required for targeting of E2 and E1 to the Golgi indicating that a heterodimer of two integral membrane proteins can be retained in the Golgi by a single retention signal.
Mol Biol Cell 1995 Jan
PMID:Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal. 774 96

Substitution in the alpha 3 domain of class I molecules can ablate the recognition of target cells by CD8 dependent cytotoxic T lymphocytes. This effect has been attributed to a destruction of the CD8 alpha binding site on the class I molecule, a hypothesis which is consistent with results obtained in conjugate binding assays. To assess the relative contribution to CTL activation of CD8 functioning as either a coreceptor or an accessory molecule, we have compared the ability of H-2Kb ovalbumin reactive CTL to lyse M12.C3 or T2 cells transfected with an H-2Kb gene encoding a wild type or mutant (CD8 nonbinding) alpha 3 domain. To establish that the substitution in the alpha 3 domain does not alter the ability of the H-2Kb molecule to bind the antigenic peptide, we have compared the binding of the ovalbumin derived H-2Kb restricted peptide (SIINFEKL) to T2 cells expressing either the CD8 binding or the CD8 nonbinding form of H-2Kb. This peptide conjugated with FITC bound equally well to T2 cells expressing either form of H-2Kb. Upon binding of this peptide, both forms of the H-2Kb molecule underwent the same conformational change as revealed by increases in the expression of particular serological epitopes. Furthermore, inhibition of the binding of the SIINFEKL peptide to both the wild type and mutant H-2Kb was observed following pretreatment of the cells with similar amounts of other H-2Kb restricted peptides derived from Sendai and Vesicular Stomatitis viruses. When the transfected M12 cells were tested for their ability to serve as targets for an anti-H-2Kb ovalbumin CTL clone, cells expressing the mutant H-2Kb molecule required the addition of 100-fold more exogenous peptide than did cells expressing the wild type molecule in order to obtain significant lysis. These data strengthen the previous hypothesis that CD8 functions much more efficiently as a coreceptor than as an accessory molecule for T cell effector function.
Mol Immunol 1994 Aug
PMID:Analysis of coreceptor versus accessory molecule function of CD8 as a correlate of exogenous peptide concentration. 806 71

The homologous and heterologous interactions between the nucleocapsid protein N and the phosphoprotein P of New Jersey and Indiana serotypes of vesicular stomatitis virus were studied. SP6 derived N and P mRNAs were cotranslated in rabbit reticulocyte lysate and the complexes formed thereof were analyzed by 7.5% nondenaturing polyacrylamide gel electrophoresis. P protein of VSV(NJ) has two binding sites for homologous N protein: One located within the C-terminal 11 amino acids (within domain III) is responsible for the formation of five specific complexes while the other site, which spans the acidic domain I, is necessary for the formation of the sixth complex only. In contrast, P(IND) does not form the sixth complex when interacted with homologous N protein. Interestingly, P(NJ) forms only complexes 1 to 5 when it interacts with N(IND). The above results suggest that the complex 6 formation or domain I interacting site is NJ-serotype specific. Two chimeric P proteins were made using heterologous domains I and II/III of the P proteins of both serotypes. The soluble interaction of the chimeric proteins with the N protein supported the observed serotype specific interactions. The chimeric P proteins bound with equal efficiency with N-RNA template of both serotypes. These results strongly suggest that the acidic domain I of the P protein differentially interacts with homologous and heterologous N proteins. The biological significance of these findings is discussed.
Cell Mol Biol Res 1993
PMID:Acidic domain of the phosphoprotein (P) of vesicular stomatitis virus differentially interacts with homologous and heterologous nucleocapsid protein (N). 822 May 88


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