INTERACTIONS OF THE HIV-1 REVERSE-TRANSCRIPTASE AZT-RESISTANT MUTANT WITH SUBSTRATES AND AZT-TP

To investigate the biochemical basis of the HIV-1 resistance to AZT we obtained the RT mutant containing four amino acid substitutions by an oligonucleotide-directed mutagenesis technique. Enzymatic properties of the wild type and mutant RTs were compared. 'AZT-resistant' mutatio ns in RT were shown to be associated with the reduced capability of AZ T-TP to block the DNA- but not RNA-directed DNA synthesis.