A MUTATION AT POSITION 190 OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 REVERSE-TRANSCRIPTASE INTERACTS WITH MUTATIONS AT POSITION-74 AND POSITION-75 VIA THE TEMPLATE PRIMER

We have analyzed amino acid substitutions at position G190 in the reve rse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1). The mutation G190E, which is responsible for resistance to certain no nnucleoside inhibitors, results in RT that has significantly less poly merase activity and that is less processive than wild-type RT. Its kin etic profile with respect to dGTP and poly(rC).oligo(dG) is significan tly altered compared to that of wild-type RT. The combination of eithe r of the mutations L74V or V75I with the G190E mutation appears to be compensatory and mitigates many of the deleterious effects of the G190 E mutation.