author_facet Wengler, Gerd
Wengler, Gisela
Wengler, Gerd
Wengler, Gisela
author Wengler, Gerd
Wengler, Gisela
spellingShingle Wengler, Gerd
Wengler, Gisela
Journal of Virology
Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
Virology
Insect Science
Immunology
Microbiology
author_sort wengler, gerd
spelling Wengler, Gerd Wengler, Gisela 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.17.1.10-19.1976 <jats:p> [ <jats:sup>3</jats:sup> H]leucine-labeled proteins synthesized in BHK-21 cells infected with Semliki Forest virus were fractionated by polyacrylamide gel electrophoresis (PAGE). Cellular and virus-specific proteins were identified by difference analysis of the PAGE profiles. The specific activity of intracellular [ <jats:sup>3</jats:sup> H]leucine was determined. Two alterations of protein synthesis, which develop with different time courses, were discerned. (i) In infected cultures an inhibition of overall protein synthesis to about 25% of the protein synthesis in mock-infected cultures develops between about 1 and 4 h postinfection (p.i.). (ii) The relative amount of virus-specific polypeptides versus cellular polypeptides increases after infection. About 80% of the proteins synthesized at 4 h p.i. are cellular proteins. Since significant amounts of nontranslocating ribosomes in polyribosomes were not detected up to 7 h p.i., the inhibition of protein synthesis is not caused by inactivation of about 75% of all polyribosomes but by a decreased protein synthetic activity of the majority of polyribosomes. Indirect evidence indicates that an inhibition of elongation and/or release of protein synthesis develops in infected cells, which is sufficient to account for the observed inhibition of protein synthesis. Inhibition of over-all protein synthesis developed when virus-specific RNA began to accumulate at the maximal rate. This relationship was observed during virus multiplication at 37, 30, and 25 C. A possible mechanism by which synthesis of virus-specific RNA in the cytoplasm could inhibit cellular protein synthesis is discussed. Indirect evidence and analysis of polyribosomal RNA show that the increased synthesis of virus-specific protein is brought about by a substitution of cellular by viral mRNA in the polyribosomes. </jats:p> Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus Journal of Virology
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source_id 49
title Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_unstemmed Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_full Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_fullStr Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_full_unstemmed Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_short Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_sort protein synthesis in bhk-21 cells infected with semliki forest virus
topic Virology
Insect Science
Immunology
Microbiology
url http://dx.doi.org/10.1128/jvi.17.1.10-19.1976
publishDate 1976
physical 10-19
description <jats:p> [ <jats:sup>3</jats:sup> H]leucine-labeled proteins synthesized in BHK-21 cells infected with Semliki Forest virus were fractionated by polyacrylamide gel electrophoresis (PAGE). Cellular and virus-specific proteins were identified by difference analysis of the PAGE profiles. The specific activity of intracellular [ <jats:sup>3</jats:sup> H]leucine was determined. Two alterations of protein synthesis, which develop with different time courses, were discerned. (i) In infected cultures an inhibition of overall protein synthesis to about 25% of the protein synthesis in mock-infected cultures develops between about 1 and 4 h postinfection (p.i.). (ii) The relative amount of virus-specific polypeptides versus cellular polypeptides increases after infection. About 80% of the proteins synthesized at 4 h p.i. are cellular proteins. Since significant amounts of nontranslocating ribosomes in polyribosomes were not detected up to 7 h p.i., the inhibition of protein synthesis is not caused by inactivation of about 75% of all polyribosomes but by a decreased protein synthetic activity of the majority of polyribosomes. Indirect evidence indicates that an inhibition of elongation and/or release of protein synthesis develops in infected cells, which is sufficient to account for the observed inhibition of protein synthesis. Inhibition of over-all protein synthesis developed when virus-specific RNA began to accumulate at the maximal rate. This relationship was observed during virus multiplication at 37, 30, and 25 C. A possible mechanism by which synthesis of virus-specific RNA in the cytoplasm could inhibit cellular protein synthesis is discussed. Indirect evidence and analysis of polyribosomal RNA show that the increased synthesis of virus-specific protein is brought about by a substitution of cellular by viral mRNA in the polyribosomes. </jats:p>
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description <jats:p> [ <jats:sup>3</jats:sup> H]leucine-labeled proteins synthesized in BHK-21 cells infected with Semliki Forest virus were fractionated by polyacrylamide gel electrophoresis (PAGE). Cellular and virus-specific proteins were identified by difference analysis of the PAGE profiles. The specific activity of intracellular [ <jats:sup>3</jats:sup> H]leucine was determined. Two alterations of protein synthesis, which develop with different time courses, were discerned. (i) In infected cultures an inhibition of overall protein synthesis to about 25% of the protein synthesis in mock-infected cultures develops between about 1 and 4 h postinfection (p.i.). (ii) The relative amount of virus-specific polypeptides versus cellular polypeptides increases after infection. About 80% of the proteins synthesized at 4 h p.i. are cellular proteins. Since significant amounts of nontranslocating ribosomes in polyribosomes were not detected up to 7 h p.i., the inhibition of protein synthesis is not caused by inactivation of about 75% of all polyribosomes but by a decreased protein synthetic activity of the majority of polyribosomes. Indirect evidence indicates that an inhibition of elongation and/or release of protein synthesis develops in infected cells, which is sufficient to account for the observed inhibition of protein synthesis. Inhibition of over-all protein synthesis developed when virus-specific RNA began to accumulate at the maximal rate. This relationship was observed during virus multiplication at 37, 30, and 25 C. A possible mechanism by which synthesis of virus-specific RNA in the cytoplasm could inhibit cellular protein synthesis is discussed. Indirect evidence and analysis of polyribosomal RNA show that the increased synthesis of virus-specific protein is brought about by a substitution of cellular by viral mRNA in the polyribosomes. </jats:p>
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spelling Wengler, Gerd Wengler, Gisela 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.17.1.10-19.1976 <jats:p> [ <jats:sup>3</jats:sup> H]leucine-labeled proteins synthesized in BHK-21 cells infected with Semliki Forest virus were fractionated by polyacrylamide gel electrophoresis (PAGE). Cellular and virus-specific proteins were identified by difference analysis of the PAGE profiles. The specific activity of intracellular [ <jats:sup>3</jats:sup> H]leucine was determined. Two alterations of protein synthesis, which develop with different time courses, were discerned. (i) In infected cultures an inhibition of overall protein synthesis to about 25% of the protein synthesis in mock-infected cultures develops between about 1 and 4 h postinfection (p.i.). (ii) The relative amount of virus-specific polypeptides versus cellular polypeptides increases after infection. About 80% of the proteins synthesized at 4 h p.i. are cellular proteins. Since significant amounts of nontranslocating ribosomes in polyribosomes were not detected up to 7 h p.i., the inhibition of protein synthesis is not caused by inactivation of about 75% of all polyribosomes but by a decreased protein synthetic activity of the majority of polyribosomes. Indirect evidence indicates that an inhibition of elongation and/or release of protein synthesis develops in infected cells, which is sufficient to account for the observed inhibition of protein synthesis. Inhibition of over-all protein synthesis developed when virus-specific RNA began to accumulate at the maximal rate. This relationship was observed during virus multiplication at 37, 30, and 25 C. A possible mechanism by which synthesis of virus-specific RNA in the cytoplasm could inhibit cellular protein synthesis is discussed. Indirect evidence and analysis of polyribosomal RNA show that the increased synthesis of virus-specific protein is brought about by a substitution of cellular by viral mRNA in the polyribosomes. </jats:p> Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus Journal of Virology
spellingShingle Wengler, Gerd, Wengler, Gisela, Journal of Virology, Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus, Virology, Insect Science, Immunology, Microbiology
title Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_full Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_fullStr Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_full_unstemmed Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_short Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
title_sort protein synthesis in bhk-21 cells infected with semliki forest virus
title_unstemmed Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
topic Virology, Insect Science, Immunology, Microbiology
url http://dx.doi.org/10.1128/jvi.17.1.10-19.1976