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Protein Synthesis in BHK-21 Cells Infected with Semliki Forest Virus
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Zeitschriftentitel: | Journal of Virology |
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Personen und Körperschaften: | , |
In: | Journal of Virology, 17, 1976, 1, S. 10-19 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
American Society for Microbiology
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Schlagwörter: |
author_facet |
Wengler, Gerd Wengler, Gisela Wengler, Gerd Wengler, Gisela |
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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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10.1128/jvi.17.1.10-19.1976 |
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1976 |
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American Society for Microbiology |
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Journal of Virology |
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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.
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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 |