Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The main structural nucleocapsid protein, NP, of parental influenza virus (WSN, HON1) was modified in the infected cells early after inoculation. The modification took place within ribonucleoprotein particles in the cytoplasm but was not observed within ribonucleoprotein particles in the nuclei. It occurred when the cells were incubated at 37 degrees C and not at 4 degrees C. The modified protein migrated slightly faster in SDS-containing polyacrylamide gels. Peptide mapping of NP protein labelled with 125I- of 14C-amino acids showed the modified form of NP not to contain at least two peptides but to contain one additional peptide as compared with the unmodified precursor. This suggested that the modification could be due both to proteolytic cleavage and to covalent modification of an amino acid residue. According to the latter suggestion, the intense phosphorylation of parental NP was observed in the cytoplasma of the infected cells when 32P was added for 30 min one hour postinfection. The nuclei of the infected cells early after infection contained more than half of parental ribonucleoprotein particles in which, however, unmodified NP was present. The possible significance of the observed modification of parental NP in the infectious cycle of influenza virus is discussed.
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PMID:[Modification of the parent influenza virus nucleocapsid protein in infected cells]. 729 60

The electrophoretic migration rates of structural and non-structural polypeptides of 38 influenza B viruses isolated in epidemics in 1978-1980 and antigenically closely related to B/Singapore/222/79 virus were compared using high resolution SDS polyacrylamide gels. Thirty of the viruses could be distinguished from the prototype B/Singapore/222/79 virus by electrophoretic migration rate differences in HA, 17 by differences in NP and 27 by differences in mobility of the NS 1 polypeptide. Mobility differences of NP, NS 1 and HA polypeptides was noted in influenza B viruses isolated in the UK in the same year. In addition, electrophoretic mobility of 32P labeled virus RNAs varied for certain UK isolates and indicated heterogeneity in genes 2, 3, 4 and 8 coding for polymerase proteins 2 and 1, nucleoprotein (NP) and non-structural protein (NS 1) respectively.
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PMID:Differences in the electrophoretic migration rates of polypeptides and RNAs of recent isolates of influenza B viruses. 729 41

Intratypic electrophoretic mobility differences in high resolution SDS-polyacrylamide gels were detected between corresponding matrix (M) proteins, nucleoproteins (NP), haemagglutinin (HA) and the non-structural polypeptides NS1 and NS2 induced in Vero cells by human influenza A viruses of the antigenic subtypes H1N1 and H3N2. Such phenotypic differences were distinguishable in both H1N1 and H3N2 viruses isolated in single school and city outbreaks. Additional intratypic variation was detected in the biological property of virus plaquing in MDCK cells. Although the biochemical basis is not established, phenotypic variation could represent an additional factor influencing the epidemiology of influenza A viruses.
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PMID:Intratypic electrophoretic variation of structural and non-structural polypeptides of human influenza A viruses. 731 Mar 81

RNA and protein interaction in the structure of influenza virus ribonucleoprotein (RNP) was studied by ultraviolet (UV) irradiation. After UV-irradiation of virion RNP for 1 hour only 6% of 3H-uridine-labeled RNA was found to go into the aqueous phase upon phenol-detergent extraction. Pretreatment of RNP with small doses of pancreatic RNase before RNA extraction slightly increased (up to 18%) the amount of RNA going into the aqueous phase. About 90% RNA was found after extraction in the aqueous phase in the nonirradiated material. As a result of UV-irradiation of RNP, RNA in RNP became more resistant to RNase: the residual acid-insoluble radioactivity was 21% whereas with nonirradiated RNP it was 3.2%. The results of the analysis of RNP labeled for protein in polyacrylamide gel and SDS-sucrose gradient after UV-irradiation and ribonuclease treatment indicate the formation of UV-induced linkages between RNA and NP protein.
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PMID:[RNA-protein interactions in influenza virus A ribonucleoprotein detected by UV radiation]. 733 92

The biologically active form of the fusion glycoprotein F from Newcastle disease virus (NDV) comprises two polypeptides, F1 and F2 (derived from a precursor polypeptide F0 by a post translational cleavage event), which are covalently linked together (F1,2) by disulphide bonds. This feature was exploited in a two-dimensional SDS-polyacrylamide gel electrophoretic analysis to orientate the position of the cleavage event within F0. Separation of proteins from NDV-infected CEF in the first dimension in the absence of reducing agent resolved F1,2 protein from all NDV-induced proteins other than F0. Reduction of the first dimension gel with 2-mercaptoethanol, followed by electrophoresis in the second dimension, resolved F1 (55K), F2 (12.5K) and F0 (64K) proteins. The only polypeptides other than F1 and F2 which fell below the diagonal, indicating the positions of the polypeptides from infected cells, were two minor glycoproteins designated HN1 (51.5K) and HN2 (27.5K) which took up positions vertically beneath the major haemagglutinin-neuraminidase glycoprotein HN (75K). Dual isotope labelling experiments with NDV-infected chick embryo fibroblasts, which had previously received a salt shock to effect synchronization of polypeptide initiation upon release of salt shock, revealed the following orientations within the parent molecules: NH2-F2-F1-COOH and NH2-HN1-HN2-COOH. The existence of intermolecular disulphide bonds, orientation and relative lengths of the two NDV HN fragments is analogous to the HA1 and HA2 proteins of influenza virus haemagglutinin.
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PMID:Location of post-translational cleavage events within F and HN glycoproteins of Newcastle disease virus. 736 63

Electrophoretic migration rate differences were detected in high resolution SDS polyacrylamide gels for nucleoprotein (NP), matrix protein (M), non structural protein (NS1), haemagglutinin (HA) annd, less regularly, for the polymerase polypeptides P1, P2 and P3 induced by different influenza A viruses. The technique allowed parental assignation of the corresponding genes in certain recombinant viruses including A/PR/8/34 (H0N1)--A/HK/117/77 (H1N1), A/Okuda/57 (H2N2)--A/HK/119/77 (H1N1) and A/Leningrad/76 (H3N2)--A/Leningrad/46 (H0N1) recombinants, thus considerably extending the technique which had been applied previously to A/PR/8/34--A/HK/68 (H3N2) only. Agreement in gene assignment between three recombinants of the former group and 11 of 17 recombinants in the A/Okuda/57--A/HK/119/77 group was noted when the data obtained using the polypeptide method was correlated with a direct genetic analysis by others using RNA:RNA hybridisation techniques. The polypeptide method appears to have wide application for the initial rapid analysis of influenza A virus recombinants obtained using parents of different influenza subtypes although complete analysis of the total genome requires the use of RNA hybridisation techniques. Two additional virus induced proteins are described, a phosphorylated form of NS 1 and a non structual polypeptide with a molecular weight of 16K daltons.
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PMID:Electrophoretic migration rate differences of polypeptides of human influenza A viruses: partial analysis of the genome of influenza vaccine recombinant viruses. 741 71

To analyze cotranslational folding of influenza hemagglutinin in the endoplasmic reticulum of live cells, we used short pulses of radiolabeling followed by immunoprecipitation and analysis with a two-dimensional SDS/polyacrylamide gel system which was nonreducing in the first dimension and reducing in the second. It separated nascent glycopolypeptides of different length and oxidation state. Evidence was obtained for cotranslational disulfide formation, generation of conformational epitopes, N-linked glycosylation, and oligosaccharide-dependent binding of calnexin, a membrane-bound chaperone that binds to incompletely folded glycoproteins via partially glucose-trimmed oligosaccharides. When glycosylation or oligosaccharide trimming was inhibited, the folding pathway was perturbed, suggesting a role for N-linked oligosaccharides and calnexin during translation of hemagglutinin.
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PMID:Cotranslational folding and calnexin binding during glycoprotein synthesis. 754 32

A polyphenolic complex (PC) with antiviral properties has been isolated from the Bulgarian medicinal plant Geranium sanguineum L. A study was undertaken to investigate the effect of PC on virus-specific protein synthesis in influenza virus-infected cells. The expression of viral glycoproteins on the surface of chick embryo fibroblasts infected with virus A/FPV, strain Rostock (H7N1) was suppressed. Virus protein synthesis was selectively inhibited as shown by SDS polyacrylamide gel electrophoresis of 35S-methionine-labelled proteins and proteins immunoprecipitated with monoclonal antibodies. The inhibitory effect was dose-dependent and better pronounced when PC was applied after virus infection. Two variants of influenza virus FPV/Rostock with reduced drug susceptibility were selected. PC affected to a lesser extent the synthesis of viral proteins in cells infected with the variants as compared to the sensitive parental virus.
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PMID:Inhibition of influenza virus protein synthesis by a plant preparation from Geranium sanguineum L. 757 69

The influenza A virus non-structural protein NS1 was produced using a copper-inducible expression system in the yeast Saccharomyces cerevisiae. The protein produced had a molecular weight of 26 kDa by SDS-PAGE and was reactive with anti-NS1 antisera. The recombinant NS1 protein was targetted to the nucleolus/nuclear envelope fraction of the yeast cell nucleus, showing that its localisation signals remain functional in yeast. In addition, immune-electron microscopy detected cytoplasmic inclusions reminiscent of those seen in cells infected with some influenza strains. The NS1 protein was shown to be capable of in vivo self-interaction which probably forms the basis of its propensity to form inclusions. Expression of the protein was found to be toxic to yeast cells expressing it, supporting a role for the protein in the shutdown of influenza virus-infected cells. Deletion mapping of NS1 pointed to 2 regions of the molecule being important for this toxicity: a basic C-terminal stretch which has been shown to act as a nuclear localisation signal, and an N-terminal region implicated in RNA binding.
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PMID:Expression and characterisation of the influenza A virus non-structural protein NS1 in yeast. 799 36

Here we describe the molecular cloning of 7.1-kilobase cDNA encoding chick cardiac muscle tensin. It contains an open reading frame of 1,744 amino acid (aa) residues. Sequence analysis reveals that, in addition to the previously noted SH2 domain (Davis, S., Lu, M. L., Lo, S. H., Lin, S., Butler, J. A., Druker, B. J., Roberts, T. M., An, Q., and Chen, L. B. (1991) Science 252, 712-715), tensin contains virtually all of the known sequence (362 aa) of insertin, an actin-capping protein that allows actin monomer to be "inserted" (Schroer, E., and Wegner, A. (1985) Eur. J. Biochem. 153, 515-520). Moreover, tensin shares partial homology with actin (46.7% identity in 30 aa), beta-spectrin's actin-binding consensus (40% identity in 26 aa), BCR (40% identity in 25 aa), catenin alpha (35% identity in 45 aa), synapsin Ia (25.6% identity in 156 aa), IL-3 receptor (20.2% identity in 384 aa), and IL-2/EPO receptors (14% identity in 20 aa). Recombinant full-length tensin, tagged with an influenza-derived epitope, was over-expressed by a baculovirus system and purified to apparent homogeneity. It migrates as a 200-kDa protein in SDS-polyacrylamide gel electrophoresis, similar to the native tensin. The structure of the tensin molecule has been characterized by light scattering, electron microscopy, and gel filtration. Nine monoclonal antibodies recognizing different regions of tensin have been prepared and characterized. The epitope-tagged recombinant tensin gene was subcloned into a pRcCMV vector and transfected into NIH 3T3 cells. Immunofluorescence stainings with monoclonal antibodies specific for chick tensin (not cross-reactive with mouse tensin) showed that the expressed protein is indeed localized at focal contacts, as that of native tensin.
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PMID:Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence, expression, and characterization. 807 58


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