Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Apr;74(4):1734–1738. doi: 10.1073/pnas.74.4.1734

Induction of deoxycytidine deaminase activity in mammalian cell lines by infection with herpes simplex virus type 1.

T S Chan
PMCID: PMC430868  PMID: 193115

Abstract

Herpes simplex virus type 1 induces deoxycytidine deaminase (cytidine/deoxycytidine aminohydrolase, EC 3.5.4.5) activity when it lytically infects a number of mammalian cell lines. The deaminase activity is induced in a mouse cell line that is deficient in this enzyme. The induction of the enzyme in this mutant cell line does not occur in the presence of actinomycin D and the induced enzyme is more thermolabile than the enzyme of the wild-type mouse cell line. Furthermore, a new deoxycytidine deaminase species with a characteristic electrophoretic mobility that is different from that of the host cell enzyme is found in cell extracts prepared from a human cell line infected with herpesvirus. These results strongly suggest that the virus-induced deoxycytidine deaminase is coded by the viral genome. Because a deficiency in this enzyme is conditionally lethal for cells growing in a medium containing 5-methyldeoxycytidine as the sole source of thymidylate, this enzyme can be utilized as a selective marker for selecting mutant cells that have regained deoxycytidine deaminase activity as the result of infection by ultraviolet-inactivated herpes simplex virus.

Full text

PDF
1734

Selected References

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

  1. CREASEY W. A. Studies on the metabolism of 5-iodo-2'-deoxycytidine in vitro. Purification of nucleoside deaminase from mouse kidney. J Biol Chem. 1963 May;238:1772–1776. [PubMed] [Google Scholar]
  2. Chan T. S., Long C., Green H. A human-mouse somatic hybrid line selected for human deoxycytidine deaminase. Somatic Cell Genet. 1975 Jan;1(1):81–90. doi: 10.1007/BF01538733. [DOI] [PubMed] [Google Scholar]
  3. Chan T. S., Meuth M., Green H. Pyrimidine excretion by cultured fibroblasts: effect of mutational deficiency in pyrimidine salvage enzymes. J Cell Physiol. 1974 Apr;83(2):263–266. doi: 10.1002/jcp.1040830213. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. Cooper G. M. Phosphorylation of 5-bromodeoxycytidine in cells infected with herpes simplex virus. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3788–3792. doi: 10.1073/pnas.70.12.3788. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. DUBBS D. R., KIT S. MUTANT STRAINS OF HERPES SIMPLEX DEFICIENT IN THYMIDINE KINASE-INDUCING ACTIVITY. Virology. 1964 Apr;22:493–502. doi: 10.1016/0042-6822(64)90070-4. [DOI] [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. Davis D. B., Kingsbury D. T. Quantitation of the viral DNA present in cells transformed by UV-irradiated herpes simplex virus. J Virol. 1976 Mar;17(3):788–793. doi: 10.1128/jvi.17.3.788-793.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Durham J. P., Ives D. H. Deoxycytidine kinase. II. Purification and general properties of the calf thymus enzyme. J Biol Chem. 1970 May 10;245(9):2276–2284. [PubMed] [Google Scholar]
  10. Garfinkle B., McAuslan B. R. Transformation of cultured mammalian cells by viable herpes simplex virus subtypes 1 and 2. Proc Natl Acad Sci U S A. 1974 Jan;71(1):220–224. doi: 10.1073/pnas.71.1.220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hatanaka M., Del Giudice R., Long C. Adenine formation from adenosine by mycoplasmas: adenosine phosphorylase activity. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1401–1405. doi: 10.1073/pnas.72.4.1401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Jamieson A. T., Bjursell G. Deoxyribonucleoside triphosphate pools in herpes simplex type 1 infected cells. J Gen Virol. 1976 Apr;31(1):101–113. doi: 10.1099/0022-1317-31-1-101. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. KIT S., DUBBS D. R. Acquisition of thymidine kinase activity by herpes simplex-infected mouse fibroblast cells. Biochem Biophys Res Commun. 1963 Apr 2;11:55–59. doi: 10.1016/0006-291x(63)90027-5. [DOI] [PubMed] [Google Scholar]
  15. KIT S., DUBBS D. R., PIEKARSKI L. J., HSU T. C. DELETION OF THYMIDINE KINASE ACTIVITY FROM L CELLS RESISTANT TO BROMODEOXYURIDINE. Exp Cell Res. 1963 Aug;31:297–312. doi: 10.1016/0014-4827(63)90007-7. [DOI] [PubMed] [Google Scholar]
  16. Kit S., Dubbs D. R., Anken M. Altered properties of thymidine kinase after infection of mouse fibroblast cells with herpes simplex virus. J Virol. 1967 Feb;1(1):238–240. doi: 10.1128/jvi.1.1.238-240.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. Kraiselburd E., Gage L. P., Weissbach A. Presence of a herpes simplex virus DNA fragment in an L cell clone obtained after infection with irradiated herpes simplex virus I. J Mol Biol. 1975 Oct 5;97(4):533–542. doi: 10.1016/s0022-2836(75)80057-x. [DOI] [PubMed] [Google Scholar]
  19. LITTLEFIELD J. W. SELECTION OF HYBRIDS FROM MATINGS OF FIBROBLASTS IN VITRO AND THEIR PRESUMED RECOMBINANTS. Science. 1964 Aug 14;145(3633):709–710. doi: 10.1126/science.145.3633.709. [DOI] [PubMed] [Google Scholar]
  20. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  21. Leung W. C., Dubbs D. R., Trkula D., Kit S. Mitochondrial and herpesvirus-specific deoxypyrimidine kinases. J Virol. 1975 Sep;16(3):486–497. doi: 10.1128/jvi.16.3.486-497.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Long C., Chan T., Levytska V., Kusano T., Green H. Absence of demonstrable linkage of human genes for enzymes of the purine and pyrimidine salvage pathways in human-mouse somatic cell hybrids. Biochem Genet. 1973 Jul;9(3):283–297. doi: 10.1007/BF00485741. [DOI] [PubMed] [Google Scholar]
  23. McFerran N. V., Smyth M., Orsi B. A. Regulation of cytidine aminohydrolase. Biochem J. 1969 Aug;114(1):8P–9P. doi: 10.1042/bj1140008pb. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Meyers R., Malathi V. G., Cox R. P., Silber R. Studies on nucleoside deaminase. Increase in activity in HeLa cell cultures caused by cytosine arabinoside. J Biol Chem. 1973 Sep 10;248(17):5909–5913. [PubMed] [Google Scholar]
  25. Munyon W., Buchsbaum R., Paoletti E., Mann J., Kraiselburd E., Davis D. Electrophoresis of thymidine kinase activity synthesized by cells transformed by herpes simplex virus. Virology. 1972 Sep;49(3):683–689. doi: 10.1016/0042-6822(72)90525-9. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. Neil G. L., Moxley T. E., Manak R. C. Enhancement by tetrahydrouridine of 1-beta-D-arabinofuranosylcytosine (cytarabine) oral activity in L1210 leukemic mice. Cancer Res. 1970 Aug;30(8):2166–2172. [PubMed] [Google Scholar]
  28. Roller B., Cohen G. H. Deoxyribonucleoside triphosphate pools in synchronized human cells infected with herpes simplex virus types 1 and 2. J Virol. 1976 Apr;18(1):58–64. doi: 10.1128/jvi.18.1.58-64.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Schneider E. L., Stanbridge E. J., Epstein C. J. Incorporation of 3H-uridine and 3H-uracil into RNA: a simple technique for the detection of mycoplasma contamination of cultured cells. Exp Cell Res. 1974 Mar 15;84(1):311–318. doi: 10.1016/0014-4827(74)90411-x. [DOI] [PubMed] [Google Scholar]
  30. 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]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES