Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1971 Apr;7(4):438–447. doi: 10.1128/jvi.7.4.438-447.1971

Virus Protein Synthesis in Animal Cell-Free Systems: Nature of the Products Synthesized in Response to Ribonucleic Acid of Encephalomyocarditis Virus

Ian M Kerr 1, E M Martin 1
PMCID: PMC356142  PMID: 4329561

Abstract

Ribonucleic acid (RNA) from encephalomyocarditis (EMC) virus stimulates the incorporation of amino acids into protein in cell-free protein-synthetic systems derived from Krebs mouse ascites tumor cells and chick embryo fibroblasts; the mouse system is the more responsive to the viral RNA. The greater part of this difference in activity can be ascribed to the cell sap, but the origin of the ribosomes also has a marked effect. The nature of the polypeptides formed in these cell-free systems was investigated by electrophoresis on polyacrylamide gels and by fingerprint analysis of tryptic digests. The same product in part appears to be synthesized in response to the EMC RNA in both systems. It was not detected if the EMC RNA was partly degraded (≤4S) or replaced by other species of RNA, including that from influenza virus. The results suggest that EMC RNA is partially translated in these systems to yield virus-specific polypeptides.

Full text

PDF
438

Images in this article

443Image
on p.443
444Image
on p.444
445Image
on p.445

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burness A. T., Clothier F. W. Particle weight and other biophysical properties of encephalomyocarditis virus. J Gen Virol. 1970 Mar;6(3):381–393. doi: 10.1099/0022-1317-6-3-381. [DOI] [PubMed] [Google Scholar]
  2. Burness A. T. Purification of Encephalomyocarditis virus. J Gen Virol. 1969 Sep;5(2):291–303. doi: 10.1099/0022-1317-5-2-291. [DOI] [PubMed] [Google Scholar]
  3. Burness A. T. Ribonucleic acid content of encephalomyocarditis virus. J Gen Virol. 1970 Mar;6(3):373–380. doi: 10.1099/0022-1317-6-3-373. [DOI] [PubMed] [Google Scholar]
  4. Duesberg P. H. The RNA of influenza virus. Proc Natl Acad Sci U S A. 1968 Mar;59(3):930–937. doi: 10.1073/pnas.59.3.930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gerin J. L., Anderson N. G. Purification of influenza virus in the K-II zonal centrifuge. Nature. 1969 Mar 29;221(5187):1255–1256. doi: 10.1038/2211255a0. [DOI] [PubMed] [Google Scholar]
  6. Girard M., Baltimore D. The effect of HeLa cell cytoplasm on the rate of sedimentation of RNA. Proc Natl Acad Sci U S A. 1966 Sep;56(3):999–1002. doi: 10.1073/pnas.56.3.999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KERR I. M., MARTIN E. M., HAMILTON M. G., WORK T. S. The initiation of virus protein synthesis in Krebs ascites tumor cells infected with EMC virus. Cold Spring Harb Symp Quant Biol. 1962;27:259–269. doi: 10.1101/sqb.1962.027.001.025. [DOI] [PubMed] [Google Scholar]
  8. Kerr I. M., Cohen N., Work T. S. Factors controlling amino acid incorporation by ribosomes from krebs II mouse ascites-tumour cells. Biochem J. 1966 Mar;98(3):826–835. doi: 10.1042/bj0980826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kerr I. M. Protein synthesis in cell-free systems: an effect of interferon. J Virol. 1971 Apr;7(4):448–459. doi: 10.1128/jvi.7.4.448-459.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kerr I. M., Sonnabendja, Martin E. M. Proein-synthetic activity of ribosomes from interferon-treated cells. J Virol. 1970 Feb;5(2):132–144. doi: 10.1128/jvi.5.2.132-144.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. MARTIN E. M., MALEC J., SVED S., WORK T. S. Studies on protein and nucleic acid metabolism in virus-infected mammalian cells. 1. Encephalomyocarditis virus in Krebs II mouse-ascites-tumour cells. Biochem J. 1961 Sep;80:585–597. doi: 10.1042/bj0800585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Mathews M., Korner A. Mammalian cell-free protein synthesis directed by viral ribonucleic acid. Eur J Biochem. 1970 Dec;17(2):328–338. doi: 10.1111/j.1432-1033.1970.tb01170.x. [DOI] [PubMed] [Google Scholar]
  14. SANGER F., BRETSCHER M. S., HOCQUARD E. J. A STUDY OF THE PRODUCTS FROM A POLYNUCLEOTIDE-DIRECTED CELL-FREE PROTEIN SYNTHESIZING SYSTEM. J Mol Biol. 1964 Jan;8:38–45. doi: 10.1016/s0022-2836(64)80146-7. [DOI] [PubMed] [Google Scholar]
  15. Smith A. E., Marcker K. A., Mathews M. B. Translation of RNA from encephalomyocarditis virus in a mammalian cell-free system. Nature. 1970 Jan 10;225(5228):184–187. doi: 10.1038/225184a0. [DOI] [PubMed] [Google Scholar]
  16. Zwartouw H. T., Algar D. J. Growth of high-titre Semliki forest virus in concentrated suspensions of chick embryo cells. J Gen Virol. 1968 Mar;2(2):243–250. doi: 10.1099/0022-1317-2-2-243. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES