1887

Abstract

SUMMARY

In cells infected with herpes simplex virus a protein associated with the small subunit of ribosomes became phosphorylated. It was not detectably labelled with C-amino acids added after infection and is therefore probably a cellular protein. The phosphorylated ribosomal proteins from HSV-1- and HSV-2-infected cells were indistinguishable electrophoretically and had an apparent mol. wt. of about 48000.

Phosphorylation of the 48K protein was detected 2 to 3 h after infection and reached a maximum rate at 4 to 5 h. It was prevented by adding cycloheximide at 2 h, or actinomycin at 1.5 h p.i., or azetidine at the beginning of infection. The phosphorylation did not occur on reversal of a cycloheximide block in the presence of actinomycin, confirming that it is not caused by a virus α-polypeptide.

Virus that had been irradiated with u.v. light, although still able to suppress synthesis of cellular protein and DNA, did not induce phosphorylation of the 48K ribosomal protein. Therefore the phosphorylation is not responsible for the suppression of host synthesis.

The α polypeptides ICP 4, 0, 22 and 27 are also phosphorylated but, in contrast to that of the ribosomal protein, their phosphorylation does not depend on the synthesis of β and γ polypeptides. It is probably mediated by a host enzyme.

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1979-11-01
2022-06-29
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References

  1. Courtney R. J., Powell K. L. 1975; Immunological and biochemical characterization of polypeptides induced by herpes simplex virus types 1 and 2. Proceedings of the Symposium on Herpes Viruses and Oncogenesis vol II pp 63–73 Edited by de Thé G., Epstein M. A., Zur Hausen H. Lyon, France: International Agency for Research on Cancer;
    [Google Scholar]
  2. Ejercito P. M., Kieff E. D., Roizman B. 1968; Characterization of herpes simplex virus strains differing in their effect on social behaviour of infected cells. Journal of General Virology 2:357–364
    [Google Scholar]
  3. Fenwick M. L., Walker M. J. 1978; Suppression of the synthesis of cellular macromolecules by herpes simplex virus. Journal of General Virology 41:37–51
    [Google Scholar]
  4. Fenwick M. L., Walker M. J., Petkevich M. 1978; On the association of virus proteins with nuclei of cells infected with herpes simplex virus. Journal of General Virology 39:519–529
    [Google Scholar]
  5. Fenwick M. L., Morse L. S., Roizman B. 1979; Anatomy of herpes simplex virus DNA. XI. Apparent clustering of functions effecting rapid inhibition of host DNA and protein synthesis. Journal of Virology 29:825–827
    [Google Scholar]
  6. Gressner A. M., Wool I. G. 1974; The phosphorylation of liver ribosomal proteins in vivo. Evidence that only a single small subunit protein (S6) is phosphorylated. Journal of Biological Chemistry 249:6917–6925
    [Google Scholar]
  7. Honess R. W., Roizman B. 1974; Regulation of herpes virus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins. Journal of Virology 14:8–19
    [Google Scholar]
  8. Honess R. W., Roizman B. 1975; Regulation of herpes virus macromolecular synthesis: sequential transition of polypeptide synthesis requires functional viral polypeptides. Proceedings of the National Academy of Sciences of the United States of America 72:1276–1280
    [Google Scholar]
  9. Kaerlin M., Horak I. 1976; Phosphorylation of ribosomal proteins in Hela ceils infected with vaccinia virus. Nature, London 259:150–151
    [Google Scholar]
  10. Morse L. S., Pereira L., Roizman B., Schaffer P. A. 1978; Anatomy of herpes simplex virus DNA. X. Mapping of viral genes by analysis of polypeptides and functions specified by HSV–1 X HSV–2 re–combinants. Journal of Virology 26:389–410
    [Google Scholar]
  11. Pereira L., Wolf M. H., Fenwick M. L., Roizman B. 1977; Regulation of herpes virus macromolecular synthesis V. Properties of α polypeptides made in HSV–1 and HSV–2 infected cells. Virology 77:733–749
    [Google Scholar]
  12. Powell K. L., Courtney R. J. 1975; Polypeptides synthesized in HSV–2–infected HEp–2 cells. Virology 66:217–228
    [Google Scholar]
  13. Rose J. K., Trachsel H., Leong K., Baltimore D. 1978; Inhibition of translation by poliovirus: inactivation of a specific initiation factor. Proceedings of the National Academy of Sciences of the United States of America 75:2732–2736
    [Google Scholar]
  14. Rubenstein A. S., Gravell M., Darlington R. 1972; Protein kinase in enveloped herpes simplex virions. Virology 50:287–290
    [Google Scholar]
  15. Russell W. C., Blair G. E. 1977; Polypeptide phosphorylation in adenovirus–infected cells. Journal of General Virology 34:19–35
    [Google Scholar]
  16. Saxton R. E., Stevens J. G. 1972; Restriction of HSV replication by poliovirus: a selective inhibition of viral translation. Virology 48:207–220
    [Google Scholar]
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