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We have found a close correlation between viral stavudine (d4T) resistance and resistance to d4T-triphosphate at the human immunodeficiency virus type 1 reverse transcriptase (RT) level. RT from site-directed mutants with 69S-XX codon insertions and/or conventional zidovudine resistance mutations seems to be involved in an ATP-dependent resistance mechanism analogous to pyrophosphorolysis, whereas the mechanism for RT with the Q151M or V75T mutation appears to be independent of added ATP for reducing binding to d4T-triphosphate.

Original publication




Journal article


Antimicrob Agents Chemother

Publication Date





2144 - 2146


Adenosine Triphosphate, Amino Acid Substitution, Binding Sites, Drug Resistance, Microbial, HIV Reverse Transcriptase, HIV-1, Reverse Transcriptase Inhibitors, Stavudine