Reversion by Hypotonic Medium of the Shutoff of Protein Synthesis Induced by Encephalomyocarditis Virus

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1981 Feb 1

PMID 6261005

Citations 10

Authors

M A Alonso

L Carrasco

Affiliations

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Abstract

Infection of human HeLa cells by picornaviruses produces a drastic inhibition of host protein synthesis. Treatment of encephalomyocarditis virus-infected HeLa cells with hypotonic medium reversed this inhibition; no viral protein synthesis was detected. The blockade of viral translation by hypotonic conditions was observed for a wide range of multiplicities of infection. However, only with low virus-to-cell ratios did cellular protein synthesis resume. The ratio of cellular to viral mRNA translation was strongly influenced by the concentration of monovalent ions present in the culture medium: a high concentration of NaCl or KCl favored the translation of viral mRNA and strongly inhibited cellular protein synthesis, whereas the opposite was true when NaCl was omitted from the culture medium. Once viral protein synthesis had been blocked by hypotonic medium treatment, it resumed when the infected cells were placed in a normal or hypertonic medium, indicating that the viral components synthesized in the infected cells were not destroyed by this treatment. These observations reinforced the idea that ions play a role in discriminating between viral and cellular mRNA translation in virus-infected animal cells.

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References

Helentjaris T, EHRENFELD E, Hershey J . Alterations in initiation factor activity from poliovirus-infected HeLa cells. J Biol Chem. 1979; 254(21):10973-8. View

Trachsel H, Sonenberg N, Shatkin A, Rose J, Leong K, Bergmann J . Purification of a factor that restores translation of vesicular stomatitis virus mRNA in extracts from poliovirus-infected HeLa cells. Proc Natl Acad Sci U S A. 1980; 77(2):770-4. PMC: 348362. DOI: 10.1073/pnas.77.2.770. View

Lodish H . Model for the regulation of mRNA translation applied to haemoglobin synthesis. Nature. 1974; 251(5474):385-8. DOI: 10.1038/251385a0. View

EHRENFELD E, Hunt T . Double-stranded poliovirus RNA inhibits initiation of protein synthesis by reticulocyte lysates. Proc Natl Acad Sci U S A. 1971; 68(5):1075-8. PMC: 389116. DOI: 10.1073/pnas.68.5.1075. View

Carrasco L . Membrane leakiness after viral infection and a new approach to the development of antiviral agents. Nature. 1978; 272(5655):694-9. DOI: 10.1038/272694a0. View

Nuss D, Oppermann H, Koch G . Selective blockage of initiation of host protein synthesis in RNA-virus-infected cells. Proc Natl Acad Sci U S A. 1975; 72(4):1258-62. PMC: 432511. DOI: 10.1073/pnas.72.4.1258. View

Leibowitz R, Penman S . Regulation of protein synthesis in HeLa cells. 3. Inhibition during poliovirus infection. J Virol. 1971; 8(5):661-8. PMC: 376244. DOI: 10.1128/JVI.8.5.661-668.1971. View

Carrasco L, Smith A . Molecular biology of animal virus infection. Pharmacol Ther. 1980; 9(3):311-55. DOI: 10.1016/0163-7258(80)90022-4. View

Koch G, Oppermann H, Bilello P, Koch F, Nuss D . Control of peptide chain initiation in uninfected and virus infected cells by membrane mediated events. Hamatol Bluttransfus. 1976; 19:541-55. DOI: 10.1007/978-3-642-87524-3_51. View

10.

Carrasco L, Smith A . Sodium ions and the shut-off of host cell protein synthesis by picornaviruses. Nature. 1976; 264(5588):807-9. DOI: 10.1038/264807a0. View

11.

Oppermann H, Koch G . On the regulation of protein synthesis in vaccinia virus infected cells. J Gen Virol. 1976; 32(2):261-73. DOI: 10.1099/0022-1317-32-2-261. View

12.

Sonenberg N, Trachsel H, Hecht S, Shatkin A . Differential stimulation of capped mRNA translation in vitro by cap binding protein. Nature. 1980; 285(5763):331-3. DOI: 10.1038/285331a0. View

13.

Kaufmann Y, Goldstein E, Penman S . Poliovirus-induced inhibition of polypeptide initiation in vitro on native polyribosomes. Proc Natl Acad Sci U S A. 1976; 73(6):1834-8. PMC: 430401. DOI: 10.1073/pnas.73.6.1834. View

14.

Rubin A, Terasaki M, Sanui H . Major intracellular cations and growth control: correspondence among magnesium content, protein synthesis, and the onset of DNA synthesis in BALB/c3T3 cells. Proc Natl Acad Sci U S A. 1979; 76(8):3917-21. PMC: 383947. DOI: 10.1073/pnas.76.8.3917. View

15.

Garry R, Bishop J, Parker S, Westbrook K, Lewis G, Waite M . Na+ and K+ concentrations and the regulation of protein synthesis in Sindbis virus-infected chick cells. Virology. 1979; 96(1):108-20. DOI: 10.1016/0042-6822(79)90177-6. View

16.

Nair C, STOWERS J, Singfield B . Guanidine-sensitive Na+ accumulation by poliovirus-infected HeLa cells. J Virol. 1979; 31(1):184-9. PMC: 353434. DOI: 10.1128/JVI.31.1.184-189.1979. View

17.

Rubin H . Central role for magnesium in coordinate control of metabolism and growth in animal cells. Proc Natl Acad Sci U S A. 1975; 72(9):3551-5. PMC: 433033. DOI: 10.1073/pnas.72.9.3551. View

18.

Carrasco L . The inhibition of cell functions after viral infection. A proposed general mechanism. FEBS Lett. 1977; 76(1):11-5. DOI: 10.1016/0014-5793(77)80110-5. View

19.

Helentjaris T, EHRENFELD E . Control of protein synthesis in extracts from poliovirus-infected cells. I. mRNA discrimination by crude initiation factors. J Virol. 1978; 26(2):510-21. PMC: 354088. DOI: 10.1128/JVI.26.2.510-521.1978. View

20.

Rose J, Trachsel H, Leong K, Baltimore D . Inhibition of translation by poliovirus: inactivation of a specific initiation factor. Proc Natl Acad Sci U S A. 1978; 75(6):2732-6. PMC: 392637. DOI: 10.1073/pnas.75.6.2732. View