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Background The viral reverse transcriptase (RT) is a major target in the therapeutic strategy against the human immunodeficiency virus (HIV). This multifunctional enzyme performs the viral genome replication by two associated functions: DNA polymerase and ribonuclease H (RNase H). Both activities are essential for viral replication and validated targets. Currently, none of the approved antiviral drugs acts on both activities, although few classes of compounds have been reported to inhibit both RT functions in vitro [1]. In a previous virtual screening [2] we identified a new isatine-based scaffold for dual functions RT inhibitors that was further derivatized.

retrovirology

Site directed mutagenesis studies on HIV-1 reverse transcriptase (RT) shed light on the mechanism of action of a new Ribonuclease H/ DNA polymerase RT dual inhibitor