Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.7.48 (transcriptase)
9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Immunogold labelling and in vitro transcription of influenza virus vRNA have been used to analyse the interaction of anti-influenza polymerase antibodies with influenza-ribonucleoprotein (RNP) complexes. The polymerase proteins (P proteins) were localized exclusively at one end of the RNP segments. In the course of transcription the amount of P protein decreased significantly. The in vitro transcriptase activity y of influenza A virus RNP complexes in the presence of anti-polymerase antibodies to the strain A/PR/8/34 was inhibited by 60%. In contrast, RNP transcriptase activity of influenza B virus was not inhibited by these antibodies.
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PMID:Interaction between anti-influenza viral polymerase antibodies and RNP particles using the in vitro transcription process and an immunogold labelling technique. 290 34

Mono- and bisthiopyrophosphate can inhibit the replication of influenza virus A/X49 in Madin-Darby canine kidney (MDCK) cells at concentrations at which no cytotoxic effect is observed after 3 days. The thiopyrophosphate analogues inhibit the RNA transcriptase activity of this virus possibly by chelating with an essential metal ion in the transcriptase complex. [31P]NMR spectroscopy indicates that bisthiopyrophosphate coordinates to zinc through sulphur and magnesium through oxygen which may influence the inhibitory properties of this compound with metal-containing enzymes.
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PMID:Thio-analogues of inorganic pyrophosphate inhibit the replication of influenza virus A in vitro. 299 Mar 33

Transformed cell lines derived from murine C127 cells were constructed that express the influenza virus RNA-dependent RNA polymerase proteins (PA, PB1, and PB2). Cell lines that express only one or all three of the proteins were tested for their ability to complement temperature-sensitive viral mutants incubated at the nonpermissive temperature. Two cell lines were isolated that express all three polymerase genes and complement the growth of PB2 temperature-sensitive mutants at the nonpermissive temperature. One of these lines also complemented PA temperature-sensitive mutants. The viral titers obtained in these two cell lines were 12-fold to 1000-fold higher than the viral titers obtained upon growth of the corresponding temperature-sensitive mutant in C127 cells at the nonpermissive temperature.
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PMID:Expression of the three influenza virus polymerase proteins in a single cell allows growth complementation of viral mutants. 301 Mar 15

The influenza virus-associated RNA polymerase cleaves capped RNA in an endonucleolytic manner and the transcription is initiated by the addition of GMP, the first substrate to be polymerized under the direction of viral RNA template, onto 3'-termini of resulting capped RNA fragments. In the presence of high concentrations of GTP as a sole substrate, multiple GMP residues were polymerized onto the primers. By the addition of the second substrate CTP, excess GMP residues, other than the 1st residue, were removed prior to elongation. The result may suggest that the RNA-dependent RNA polymerase carries a proofreading function.
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PMID:Proofreading function associated with the RNA-dependent RNA polymerase from influenza virus. 301 29

The complete nucleotide sequence of the PB2 gene of influenza virus A/Chile/1/83 (H1 N1) is presented. Sequence comparison between A/Chile PB2 protein and the known PB2 sequences of the influenza strains A/WSN/33 (H1 N1), A/PR/8/34 (H1 N1), A/NT/60/68 (H3 N2), A/Kiev/59/79 (H1 N1), A/FPV/Rostock/34 (H7 N1), and B/Ann Arbor/1/66 indicates extensive amino acid homology for the influenza A virus PB2 proteins. Small clusters of basic amino acids are conserved in all PB2 proteins including the influenza B PB2 protein which has only 39% sequence homology overall to the PB2 polypeptides of type A influenza viruses. The evolutionary rate of 5.7 x 10(-3) nucleotide substitutions per site per year and 0.25% amino acid changes per year between the A/Chile/1/83 and A/NT/60/68 PB2 appears to be higher than that calculated earlier for A/NT, A/PR/8 and A/WSN. An unusually high degree of sequence change between A/Chile/1/83 and A/Kiev/59/79 PB2 polymerase was revealed and this is discussed in terms of its probable origin.
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PMID:Evolution of influenza polymerase: nucleotide sequence of the PB2 gene of A/Chile/1/83 (H1 N1). 321 73

The combined effect of sodium selenite and remantadine on influenza A virus reproduction in vitro and in vivo is described. The effect of sodium selenite on influenza virus transcriptase was studied. Inoculation of remantadine in combination with nontoxic concentrations of sodium selenite was found to be a promising combination for inhibition of experimental influenza infection.
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PMID:[Antiviral action of sodium selenite and its combination with remantadine]. 344 84

Polynucleotide inhibitors of the influenza virion transcriptase, which is activated in vitro by detergent, can be divided into two categories. Polyribonucleotides comprised of adenine and guanine bases or adenine and uracil bases inhibit initiation but not elongation events of transcription. In contrast, polyribonucleotides containing cytidine and uracil or inosine and uracil block both initiation and elongation. Effects on elongation are apparent on addition of polynucleotides at either 5 or 10 min post-initiation. Dose-response studies with these and other polynucleotides have shown that the concentrations causing 50% inhibition of transcription vary considerably with the most potent inhibitor being the modified polymer, poly(C,S4U10).
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PMID:Effects of polynucleotide inhibitors on transcriptional events of influenza virions. 350 18

Activity of RNA polymerase was studied in original non-pathogenic for mice viruses of influenza A and B (A/seal/Massachusetts 1/80, A/USSR 05/81, A/Philippines 2/82 and B/Singapore 227/79) and of their pathogenic derivatives. All the non-pathogenic viruses studied exhibited the low rate of transcriptase activity. Pathogenic derivatives of these strains exhibited higher activity of RNA polymerase, which was 1.5-3-fold higher as compared with the original strain. During passage of influenza viruses A and B in mice organism selection of the population appears to occur, which had the highest transcriptase activity.
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PMID:[Comparative study of the RNA-polymerase activity of non-pathogenic and pathogenic influenza viruses A and B]. 366 Jul 48

Oligodeoxynucleotides covalently linked to an acridine derivative were targeted to part of the 3'-terminal sequence which is common to the eight RNAs of type A influenza viruses. The cytopathic effect of the virus on MDCK cells in culture was strongly decreased by a heptanucleotide covalently attached to the acridine ring. Control experiments using other oligonucleotide sequences showed that the effect was specific for the complementary sequence of the 3'-terminal region of the viral RNAs. The RNA transcriptase reaction of a type A virus was also selectively inhibited in vitro by the heptanucleotide-acridine conjugate. A type B influenza virus was used as a control. The common sequence at the 3' end of its eight viral RNAs is different from that of type A viruses. Three mismatches were expected with the heptanucleotide which was fully complementary to type A viral RNAs. This heptanucleotide had no effect on the cytopathic effect of a type B influenza virus. These results demonstrate that viral RNAs are specific targets for the oligonucleotide-acridine conjugate that inhibits the cytopathic effect of type A influenza viruses.
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PMID:Selective inhibition of the cytopathic effect of type A influenza viruses by oligodeoxynucleotides covalently linked to an intercalating agent. 369 85

The complete nucleotide sequence of a cloned cDNA copy of the genome RNA segment encoding the influenza B/Lee/40 virus PB1 polymerase protein has been determined. The genome RNA segment is 2368 nucleotides in length and is capable of encoding a polymerase (PB1) protein of 752 amino acids with a calculated mol mass of 84,407 Da. As expected, the protein is highly basic with a net charge of +20 at pH 7.0. Sequence comparison between the influenza A and B virus PB1 proteins reveals that they share 61% amino acid homology. An internal hydrophobic domain and 90% of the proline residues found within the influenza A virus PB1 protein are conserved in the influenza B virus molecule. The influenza A and B virus PB1 proteins share the highest homology yet seen between proteins encoded by these disparate viruses. This remarkable conservation of primary structure argues for severe functional constraint on the evolution of this influenza virus polymerase protein.
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PMID:Influenza B virus PB1 protein; nucleotide sequence of the genome RNA segment predicts a high degree of structural homology with the corresponding influenza A virus polymerase protein. 375 92


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