Resistance to nucleoside analogs of selective mutants of human immunodeficiency virus type 2 reverse transcriptase

Michal Perach, Tami Rubinek, Amnon Hizi

Research output: Contribution to journalComment/debate

Abstract

We have studied selected mutants of human immunodeficiency virus type 2 (HIV-2) reverse transcriptase (RT) in a cell-free system in order to assess whether the mutant proteins exhibit a reduction in the sensitivity to nucleoside analog inhibitors similar to that of HIV-1 RT. We have modified, by site-directed mutagenesis, several of those amino acid residues so that their equivalent substitutions in HIV-1 RT have led to the formation of HIV- 1 RT variants with the highest degree of resistance to dideoxynucleoside triphosphates (i.e., Glu-89→Gly, Leu-74→Val, and Ser-215→Tyr [which is comparable to the Thr-215→Tyr mutation of HIV-1 RT] and the double mutations Glu-89→Gly/Ser-215→Tyr and Leu-74→Val/Ser-215→Tyr). The similarity found between resistance of the newly generated HIV-2 RT mutants to nucleoside analogs and that of the comparable mutants of HIV-1 RT can support the notion that the overall protein folding around the DNA polymerase active site in HIV-2 RT is quite similar to that of HIV-1 RT.

Original languageEnglish
Pages (from-to)509-512
Number of pages4
JournalJournal of Virology
Volume69
Issue number1
DOIs
StatePublished - Jan 1995

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