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J. Virol., 10 1995, 6563-6566, Vol 69, No. 10
Copyright © 1995, American Society for Microbiology

A screen in Escherichia coli for nucleoside analogs that target human immunodeficiency virus (HIV) reverse transcriptase: coexpression of HIV reverse transcriptase and herpes simplex virus thymidine kinase

B Kim and LA Loeb
Joseph Gottstein Memorial Cancer Research Laboratory, Department of Pathology and Biochemistry, University of Washington, Seattle 98195, USA.

Human immunodeficiency virus (HIV) reverse transcriptase substitutes for temperature-sensitive DNA polymerase I (Pol Its) in Escherichia coli, providing a screen for anti-HIV reverse transcriptase nucleoside analogs in bacteria. Since phosphorylation of nucleosides in E. coli is limited to thymidine and its derivatives, we coexpressed herpes simplex virus thymidine kinase, an enzyme that phosphorylates a wide variety of nucleoside analogs, together with HIV reverse transcriptase. Coexpression of herpes simplex virus thymidine kinase and HIV reverse transcriptase rendered Pol Its cells sensitive to dideoxycytidine. Studies with different nucleoside analogs indicate that this bacterial screening system is able to select and identify nucleoside analogs that specifically target HIV reverse transcriptase.


This article has been cited by other articles:

  • Nissley, D. V., Boyer, P. L., Garfinkel, D. J., Hughes, S. H., Strathern, J. N. (1998). Hybrid Ty1/HIV-1 elements used to detect inhibitors and monitor the activity of HIV-1 reverse transcriptase. Proc. Natl. Acad. Sci. USA 95: 13905-13910 [Abstract] [Full Text]  
  • Kim, B., Hathaway, T. R., Loeb, L. A. (1996). Human Immunodeficiency Virus Reverse Transcriptase. J. Biol. Chem. 271: 4872-4878 [Abstract] [Full Text]  


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