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. 1978 Jun;26(3):547–553. doi: 10.1128/jvi.26.3.547-553.1978

Aanlysis of dCMP deaminase and CDP reductase levels in hamster cells infected by herpes simplex virus.

Y Langelier, M Déchamps, G Buttin
PMCID: PMC525880  PMID: 209209

Abstract

Several enzymatic activities involved in the biosynthetic pathways of nucleotides, including thymidine kinase, which has been used as a biochemical marker in studies of gene transfer, are induced by herpes simplex virus (HSV). The utility of additional markers prompted us to reanalyze the effects of HSV infection on the activities of two other enzymes for which direct selective methods can be devised: dCMP deaminase and CDP reductase. For this purpose, mutant Chinese hamster (lA1) cells devoid of dCMP deaminase activity or Syrian hamster (BHK-21/C13) cells were infected by HSV type 1 or 2, and the activities of thymidine kinase, dCMP deaminase, and CDP reductase were measured in the cell extracts. The reported induction of thymidine kinase and CDP reductase by HSV was confirmed, whereas the stimulation of dCMP deaminase activity could not be observed. For both cell lines, the HSV-induced CDP reductase differed from the host enzyme by sensitivity to inhibition by both dTTP and dATP. This property should be helpful in developing a selection system for this activity.

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Selected References

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

  1. Caboche M. Comparison of the frequencies of spontaneous and chemically-induced 5-bromodeoxyuridine-resistance mutations in wild-type and revertant BHK-21-13 cells. Genetics. 1974 Jun;77(2):309–322. doi: 10.1093/genetics/77.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chan T. S. Induction of deoxycytidine deaminase activity in mammalian cell lines by infection with herpes simplex virus type 1. Proc Natl Acad Sci U S A. 1977 Apr;74(4):1734–1738. doi: 10.1073/pnas.74.4.1734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cheng Y. C., Goz B., Prusoff W. H. Deoxyribonucleotide metabolism in Herpes simplex virus infected HeLa cells. Biochim Biophys Acta. 1975 May 16;390(3):253–263. doi: 10.1016/0005-2787(75)90346-9. [DOI] [PubMed] [Google Scholar]
  4. Cheng Y. C., Ostrander M. Deoxythymidine kinase induced in HeLa TK- cells by herpes simplex virus type I and type II. II. Purification and characterization. J Biol Chem. 1976 May 10;251(9):2605–2610. [PubMed] [Google Scholar]
  5. Cohen G. H., Factor M. N., Ponce de Leon M. Inhibition of herpes simplex virus type 2 replication by thymidine. J Virol. 1974 Jul;14(1):20–25. doi: 10.1128/jvi.14.1.20-25.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cohen G. H. Ribonucleotide reductase activity of synchronized KB cells infected with herpes simplex virus. J Virol. 1972 Mar;9(3):408–418. doi: 10.1128/jvi.9.3.408-418.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Davidson R. L., Adelstein S. J., Oxman M. N. Herpes simplex virus as a source of thymidine kinase for thymidine kinase-deficient mouse cells: suppression and reactivation of the viral enzyme. Proc Natl Acad Sci U S A. 1973 Jul;70(7):1912–1916. doi: 10.1073/pnas.70.7.1912. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dechamps M., de Saint-Vincent B. R., Evrard C., Sassi M., Buttin G. Studies on 1-beta-D-arabinofuranosyl-cytosine (Ara-C) resistant mutants of Chinese hamster fibroblasts. II. High resistance to Ara-C as a genetic marker for cellular hybridization. Exp Cell Res. 1974 Jun;86(2):269–279. doi: 10.1016/0014-4827(74)90713-7. [DOI] [PubMed] [Google Scholar]
  9. Jamieson A. T., Gentry G. A., Subak-Sharpe J. H. Induction of both thymidine and deoxycytidine kinase activity by herpes viruses. J Gen Virol. 1974 Sep;24(3):465–480. doi: 10.1099/0022-1317-24-3-465. [DOI] [PubMed] [Google Scholar]
  10. Jamieson A. T., Subak-Sharpe J. H. Biochemical studies on the herpes simplex virus-specified deoxypyrimidine kinase activity. J Gen Virol. 1974 Sep;24(3):481–492. doi: 10.1099/0022-1317-24-3-481. [DOI] [PubMed] [Google Scholar]
  11. Jofre J. T., Schaffer P. A., Parris D. S. Genetics of resistance to phosphonoacetic acid in strain KOS of herpes simplex virus type 1. J Virol. 1977 Sep;23(3):833–836. doi: 10.1128/jvi.23.3.833-836.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kit S., Dubbs D. R. Regulation of herpesvirus thymidine kinase activity in LM(TK) cells transformed by ultraviolet light-irradiated herpes simplex virus. Virology. 1977 Jan;76(1):331–340. doi: 10.1016/0042-6822(77)90306-3. [DOI] [PubMed] [Google Scholar]
  13. Kit S., Jorgensen G. N., Dubbs D. R., Chan S. K., Leung W. C. Biochemical and serological properties of the thymidine-phosphorylating enzymes induced by herpes simplex virus mutants temperature-dependent for enzyme formation. Virology. 1976 Jan;69(1):179–190. doi: 10.1016/0042-6822(76)90205-1. [DOI] [PubMed] [Google Scholar]
  14. Kit S., Leung W. C., Jorgensen G. N., Dubbs D. R. Distinctive properties of thymidine kinase isozymes induced by human and avian hepresviruses. Int J Cancer. 1974 Nov 15;14(5):598–610. doi: 10.1002/ijc.2910140506. [DOI] [PubMed] [Google Scholar]
  15. Klemperer H. G., Haynes G. R., Shedden W. I., Watson D. H. A virus-specific thymidine kinase in BHK-21 cells infected with herpes simplex virus. Virology. 1967 Jan;31(1):120–128. doi: 10.1016/0042-6822(67)90015-3. [DOI] [PubMed] [Google Scholar]
  16. Krakoff I. H., Brown N. C., Reichard P. Inhibition of ribonucleoside diphosphate reductase by hydroxyurea. Cancer Res. 1968 Aug;28(8):1559–1565. [PubMed] [Google Scholar]
  17. Leiden J. M., Buttyan R., Spear P. G. Herpes simplex virus gene expression in transformed cells. I. Regulation of the viral thymidine kinase gene in transformed L cells by products of superinfecting virus. J Virol. 1976 Nov;20(2):413–424. doi: 10.1128/jvi.20.2.413-424.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lin S. S., Munyon W. Expression of the viral thymidine kinase gene in herpes simplex virus-transformed L cells. J Virol. 1974 Nov;14(5):1199–1208. doi: 10.1128/jvi.14.5.1199-1208.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Munyon W., Kraiselburd E., Davis D., Mann J. Transfer of thymidine kinase to thymidine kinaseless L cells by infection with ultraviolet-irradiated herpes simplex virus. J Virol. 1971 Jun;7(6):813–820. doi: 10.1128/jvi.7.6.813-820.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Nii S., Rosenkranz H. S., Morgan C., Rose H. M. Electron microscopy of herpes simplex virus. 3. Effect of hydroxyurea. J Virol. 1968 Oct;2(10):1163–1171. doi: 10.1128/jvi.2.10.1163-1171.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Perera P. A., Morrison J. M. Evidence for the induction of a new deoxycytidine kinase in cells infected with herpes virus. Biochem J. 1970 Apr;117(2):21P–22P. doi: 10.1042/bj1170021pb. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Peterson D. M., Moore E. C. Independent fluctuations of cytidine and adenosine diphosphate reductase activities in cultured Chinese hamster fibroblasts. Biochim Biophys Acta. 1976 Apr 15;432(1):80–91. doi: 10.1016/0005-2787(76)90043-5. [DOI] [PubMed] [Google Scholar]
  23. Purifoy D. J., Lewis R. B., Powell K. L. Identification of the herpes simplex virus DNA polymerase gene. Nature. 1977 Oct 13;269(5629):621–623. doi: 10.1038/269621a0. [DOI] [PubMed] [Google Scholar]
  24. RAPP F., HSU T. C. VIRUSES AND MAMMALIAN CHROMOSOMES. IV. REPLICATION OF HERPES SIMPLEX VIRUS IN DIPLOID CHINESE HAMSTER CELLS. Virology. 1965 Mar;25:401–411. doi: 10.1016/0042-6822(65)90061-9. [DOI] [PubMed] [Google Scholar]
  25. Rolton H. A., Keir H. M. Deoxycytidylate deaminase evidence for a new enzyme in cells infected by the virus of herpes simplex. Biochem J. 1974 Nov;143(2):403–409. doi: 10.1042/bj1430403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Summers W. P., Wagner M., Summers W. C. Possible peptide chain termination mutants in thymide kinase gene of a mammalian virus, herpes simplex virus. Proc Natl Acad Sci U S A. 1975 Oct;72(10):4081–4084. doi: 10.1073/pnas.72.10.4081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Thouless M. E., Wildy P. Deoxypyrimidine kinases of herpes simplex viruses types 1 and 2: comparison of serological and structural properties. J Gen Virol. 1975 Feb;26(2):159–170. doi: 10.1099/0022-1317-26-2-159. [DOI] [PubMed] [Google Scholar]
  28. Weissbach A., Hong S. C., Aucker J., Muller R. Characterization of herpes simplex virus-induced deoxyribonucleic acid polymerase. J Biol Chem. 1973 Sep 25;248(18):6270–6277. [PubMed] [Google Scholar]
  29. Wentworth B. B., French L. Plaque assay of Herpesvirus hominis on human embryonic fibroblasts. Proc Soc Exp Biol Med. 1969 Jun;131(2):588–592. doi: 10.3181/00379727-131-33932. [DOI] [PubMed] [Google Scholar]

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