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J Gen Virol 65 (1984), 467-475; DOI 10.1099/0022-1317-65-3-467
© 1984 Society for General Microbiology
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Differential Substrate Specificity of DNA Polymerase beta and of a DNA Polymerase Induced by Herpes Simplex Virus Type 2 towards Thymidine Triphosphate Analogues

L. Kowalzick1, K. K. Gauri2, S. Spadari3, G. Pedrali-Noy3 and G. Koch1

1 Abteilung Molekularbiologie, Universität Hamburg, D-2000 Hamburg 13, Federal Republic of Germany
2 Universitätsaugenklinik, D-2000 Hamburg 20, Federal Republic of Germany
and3 Laboratorio di Genetica Biochimica ed Evoluzionistica, CNR, Pavia, Italy

Several triphosphates of 5-substituted deoxyuridine (dU), such as 5-ethyl-, 5-n-propyl-, 5-n-hexyl- and 5-isopropyldeoxyuridine triphosphates and 5-trifluorothymidine triphosphate are substrates for HeLa cell DNA polymerase beta (2'-deoxynucleoside-5'-triphosphate: DNA-deoxynucleotidyltransferase, EC 2.7.7.7 [EC] ) and for a DNA polymerase isolated from HeLa cells infected with herpes simplex virus type 2 (HSV-2) strain 75. At the concentration tested (50 µM), all these analogues were incorporated more readily into DNA by the virus-coded enzyme than by DNA polymerase beta from the host cell. The DNA polymerase coded by HSV-2 showed an affinity for deoxythymidine triphosphate (dTTP) and the analogues studied higher than that of DNA polymerase beta. Analogues are preferential substrates for the viral enzyme, since they readily substitute for dTTP during synthesis in vitro. In contrast, arabinosylthymine-5'-triphosphate was readily incorporated into DNA by the host cell DNA polymerase beta, but inhibited the DNA polymerase specified by HSV-2.

Keywords: HSV-2, DNA polymerase, chemotherapy

Received 9 August 1983; accepted 21 November 1983.




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Copyright © 1984 by the Society for General Microbiology.