Summary
The pattern of Interferon (IFN) production in virus-infected cells has been compared with the rate of bulk cellular protein synthesis, on one hand, and with the synthesis of representative cell and virus proteins such as actin, the γ and the NP proteins of encephalomyocarditis (EMC) and Newcastle Disease (NDV) viruses, on the other hand. This was investigated under conditions of impaired protein synthesis such as i) high osmolarity media, ii) a virus-induced shut-off, and iii) in cells exposed to relatively low doses of cycloheximide (CXM), which slow elongation of protein chain and thus favour the translation of low-affinity messenger RNAs (mRNAs). In each instance IFN production was compared with35S-methionine incorporation into TCA-precipitable materials and into SDS-polyacrylamide gel-analysed proteins.
Data obtained from each of the experimental approachesall indicate that IFN production and cellular protein synthesis are modified in a closely related fashion suggesting that their mRNAs share a similar degree of affinity for ribosomes. Conversely, two mRNAs coding for representative EMC and NDV virus proteins exhibit, respectively, the highest and the lowest affinity for ribosomes as compared to actin mRNA.
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Abbreviations
- VSV:
-
Vesicular stomatitis virus
- IFN:
-
Interferon
- EMC:
-
Encephalomyocarditis virus
- NDV:
-
Newcastle disease virus
- MOI:
-
multiplicity of infection
- PFU:
-
plaque-forming units
- FCS:
-
fetal calf serum
- PBS:
-
phosphate-buffered saline
- HCI:
-
hydrochloric acid
- TCA:
-
trichloroacetic acid
- CXM:
-
cycloheximide
- SDS:
-
sodium dodecyl sulphate
- NP:
-
nucleocapsid protein
References
Alonso, M. A., Carrasco, L.: Reversion by hypotonic medium of the shut-off of protein synthesis induced by encephalomyocarditis virus. J. Virol.37, 535–540 (1981).
Bishop, J. M., Maldonado, R. L., Garry, R. F., Allen, P. T., Bose, H. R., Waite, M. R. F.: Effect of medium of lowered NaCl on virus release and protein synthesis in cells infected with reticuloendotheliosis virus. J. Virol.17, 446–452 (1976).
Garry, R. F., Waite, M. R. F.: Na+ and K+ Concentrations and the regulation of the Interferon system in chick cells. Virology96, 121–128 (1979).
Garry, R. F., Bishop, J. M., Parker, S., Westbrook, K., Lewis, G., Waite, M. R. F.: Na+ and K+ concentrations and the regulation of protein synthesis in sindbis virus-infected chick cells. Virology76, 108–120 (1979).
Ito, Y., Montagnier, L.: Heterogeneity of the sensitivity of vesicular stomatitis virus (VSV) to Interferons. Infect. Immun.18, 23–27 (1977).
Jen, G., Birge, C. H., Thach, R. E.: Comparison of initiation rates of encephalomyocarditis virus and host protein synthesis in infected cells. J. Virol.27, 640–647 (1978).
Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature227, 680–685 (1970).
Lodish, H. F.: Alpha and beta globin messenger ribonucleic acid different amounts and rates of initiation of translation. J. Biol. Chem.246, 7131–7138 (1971).
Lodish, H. F.: Translational control of protein synthesis. Ann. Rev. Biochem.45, 39–72 (1976).
Lodish, H. F., Desalu, O.: Regulation of synthesis of non-globin proteins in cell-free extracts of rabbit reticulocytes. J. Biol. Chem.248, 3520–3527 (1973).
Madore, H. P., England, J. M.: Selective suppression of cellular protein synthesis in BHK21 cells infected with rabies virus. J. Virol.10, 1351–1354 (1975).
Meager, A., Shuttleworth, J., Just, M. D., Boseley, P., Morser, J.: The effect of hypertonic salt on Interferon and Interferon mRNA synthesis in human MG63 cells. J. gen. Virol.59, 177–181 (1982).
Oppermann, H., Koch, G.: On the regulation of protein synthesis in vaccinia virus infected cells. J. gen. Virol.32, 261–273 (1976).
Perlman, S., Hirsh, M., Penman, S.: Utilization of messenger in adenovirus-2-infected cells at normal and elevated temperatures. Nature New Biol.238, 143–144 (1972).
Revel, M., Groher, Y.: Post-transcriptional controls of gene expression in eukaryotes. Ann. Rev. Biochem.47, 1079–1126 (1978).
Rossi, G. B.: Interferon and cell differentiation. In:Gresser, I. (ed.), Interferon 1985, Vol. 6, 31–68. London-New York: Academic Press.
Sonnenshein, G. E., Brawerman, G.: Regulation of immunoglobulin synthesis in mouse myeloma cells. Biochemistry15, 5497–5501 (1976).
Sorrentino, V., di Francesco, P., Soria, M., Rossi, G. B.: A Human Amniotic cell line yielding high titres of human fibroblast Interferon. J. gen. Virol.63, 509–511 (1982).
Stewart, W. E.: The Interferon System. Wien-New York: Springer 1979.
Strome, S., Young, E. T.: Translational discriminations against bacteriophage T7 gene 0.3 messenger RNA. J. Mol. Biol.136, 433–450 (1980).
Tan, Y. H., Armstrong, J. A., Ke, Y. H., Ho, M.: Regulation of cellular interferon production: enhancement by antimetabolites. Proc. Natl. Acad. Sci. U.S.A.67, 464–471 (1970).
Ussery, M. A., Ramirez-Mitchell, R., Hardesty, B. A.: Inhibition of Friend murine leukemia virus production by low-ionic-strength medium. J. Virol.17, 453–461 (1976).
Vilček, J., Rossman, T. G., Varacalli, F.: Differential effects of actinomycin D and puromycin on the release of Interferon induced by double stranded RNA. Nature222, 682–683 (1969).
Vilček, J., Havell, A., Kohasen, M.: Superinduction of Interferon with metabolic inhibitors: possible mechanisms and practical applications. J. Infect. Dis.133, A22-A29 (1976).
Walden, W. E., Godefroy-Colburn, T., Thach, R. E.: The role of mRNA competition in regulating translation 1. Demonstration of competitionin vivo. J. Biol. Chem.256, 11739–11746 (1981).
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Sorrentino, V., Battistini, A., di Francesco, P. et al. Interferon production in L929 cells under impaired translational conditions: Comparison of rates of interferon, actin, Newcastle disease and encephalomyocarditis viruses mRNAs initiation of protein synthesis. Archives of Virology 88, 175–187 (1986). https://doi.org/10.1007/BF01310873
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DOI: https://doi.org/10.1007/BF01310873