1887

Abstract

Infection of cultured vertebrate cells by Sindbis virus, an alphavirus, results in a reduction in the overall rate of protein synthesis and in selective termination (shutoff) of host-specified protein synthesis. The shutoff of host protein synthesis by Sindbis virus has been temporally correlated with a decrease in intracellular K concentration (and an increase in intracellular Na concentration) which occurs as a consequence of virus- mediated inhibition of the plasma membrane-associated Na/K ATPase. Incubation of Sindbis virus-infected cells in medium containing an elevated concentration of K resulted in an increase in the intracellular concentration of K, an increase in the overall rate of protein synthesis, and in partial reversal of the virus- induced termination of cell-specified protein synthesis. These results suggest that the virus-induced decrease in intracellular K concentration is required for efficient shutoff of host protein synthesis by Sindbis virus.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-75-2-411
1994-02-01
2022-01-19
Loading full text...

Full text loading...

/deliver/fulltext/jgv/75/2/JV0750020411.html?itemId=/content/journal/jgv/10.1099/0022-1317-75-2-411&mimeType=html&fmt=ahah

References

  1. Alonso M. A., Carrasco L. 1981; Reversion by hypotonic medium of the shut-off of protein synthesis induced by encephalo-myocarditis virus. Journal of Virology 37:535–540
    [Google Scholar]
  2. Carrasco L., Esteban M. 1982; Modification of membrane permeability in vaccinia virus-infected cells. Virology 117:62–69
    [Google Scholar]
  3. Carrasco L., Otero M. J., Castrillo J. L. 1989; Modification of membrane permeability by virus infections. Pharmacology and Therapeutics 40:171–212
    [Google Scholar]
  4. Castrillo J. L., López-Rivas A., Carrasco L. 1987; Effects of extracellular cations on translation in poliovirus-infected cells. Journal of General Virology 68:325–333
    [Google Scholar]
  5. Cloyd M. W., Lynn W. 1991; Perturbation of host-cell membrane is a primary mechanism of HIV cytopathology. Virology 181:500–511
    [Google Scholar]
  6. Cloyd M. W., Lynn W. S., Ramsey K., Baron S. 1989; Inhibition of human immunodeficiency virus (HIV-1) infection by diphenylhydantoin (dilantin) implicates role of cell calcium in virus life cycle. Virology 173:581–590
    [Google Scholar]
  7. Elgizoli M., Dai Y., Kempf C., Koblet H., Michel M. R. 1989; Semliki Forest virus capsid protein acts as a pleiotropic regulator of host protein synthesis. Journal of Virology 63:2921–2928
    [Google Scholar]
  8. Garry R. F. 1989a; Alteration of intracellular monovalent cation concentrations by a poliovirus mutant which encodes a defective 2A protease. Virus Research 13:129–142
    [Google Scholar]
  9. Garry R. F. 1989b; Potential mechanisms for the cytopathic properties of human immunodeficiency virus. AIDS 3:683–694
    [Google Scholar]
  10. Garry R. F., Bostick D. A. 1986; Intracellular K+ and the expression of transformation parameters by chick cells transformed by the Bryan strain of Rous sarcoma virus. Virology 150:439–450
    [Google Scholar]
  11. Garry R. F., Waite M. R. F. 1979; Na+ and K+ and the regulation of the interferon system in chick cells. Virology 96:121–128
    [Google Scholar]
  12. Garry R. F., Bishop J. M., Parker S., Westbrooke K., Lewis G., Waite M. R. F. 1979; Na+ and K+ and the regulation of protein synthesis in Sindbis virus-infected chick cells. Virology 96:108–120
    [Google Scholar]
  13. Garry R. F., Kort J. J., Koch-Nolte F., Koch G. 1991; Similarities of viral proteins to toxins that interact with ion channels. AIDS 5:1381–1384
    [Google Scholar]
  14. Miller M. A., Garry R. F., Jaynes J. M., Montelaro R. C. 1991; A structural correlation between lentivirus TM proteins and natural cytolytic peptides. AIDS Research and Human Retroviruses 7:511–519
    [Google Scholar]
  15. Mobley P. W., Curtain C. C., Kirkpatrick A., Rostamkhani M., Waring A. J., Gordon L. M. 1992; The amino terminal peptide of HIV-1 gp41 lyses human erythrocytes and CD4+ lymphocytes. Biochimica et biophysica acta 1139:251–256
    [Google Scholar]
  16. Munoz A., Castrillo J. L., Carrasco L. 1985; Modification of membrane permeability during Semliki Forest virus infection. Virology 146:203–212
    [Google Scholar]
  17. Perez L., Irurzun A., Carrasco L. 1993; Activation of phospholipase activity during Semliki Forest virus infection. Virology 194:28–36
    [Google Scholar]
  18. Pinto L. H., Holsinger L. J., Lamb R. A. 1992; Influenza virus M2 protein has ion channel activity. Cell 69:517–528
    [Google Scholar]
  19. Schaefer A., Geck P., Zibirre R., Kühne H., Koch G. 1984; Alterations of 86Rb+ fluxes in poliovirus-infected HeLa cells and their dependence on virus replication. Virology 136:457–461
    [Google Scholar]
  20. Schlegel A., Omar A., Jentsch P., Morell A., Kempf C. 1991; Semliki Forest virus envelope proteins function as proton channels. Bioscience Reports 11:243–255
    [Google Scholar]
  21. Schlesinger M. J., London S. D., Ryan C. 1993; An in-frame insertion into the Sindbis virus 6K gene leads to defective proteolytic processing of the virus glycoproteins, a tram-dominant negative inhibition of normal virus formation, and interference in virus shutoff of host-cell protein synthesis. Virology 193:424–432
    [Google Scholar]
  22. Ulug E. T., Bose H. R.JR 1985; Effect of tunicamycin on the development of the cytopathic effect in Sindbis virus-infected avian fibroblasts. Virology 143:546–557
    [Google Scholar]
  23. Ulug E. T., Garry R. F., Bose H. R.Jr 1984; Alterations in monovalent cation transport in Sindbis virus-infected cells. Virology 132:118–130
    [Google Scholar]
  24. Ulug E. T., Garry R. F., Bose H. R.Jr 1989; The role of monovalent cation transport in Sindbis virus maturation and release. Virology 172:42–50
    [Google Scholar]
  25. Van Steeg H., Kasperaitis M., Vorma H. A., Benne R. 1984; Infection of neuroblastoma cells by Semliki Forest virus: the interference of viral capsid protein with the binding of host mRNAs into initiation complexes is the cause of shut-off of host protein synthesis. European Journal of Biochemistry 138:473–478
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-75-2-411
Loading
/content/journal/jgv/10.1099/0022-1317-75-2-411
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error