HIV-1 reverse transcriptase or HIV-2 reverse transcriptase (RT)

HIV-1 reverse transcriptase (RT) is an essential viral enzyme that catalyzes the conversion of the single-stranded RNA genome of human immunodeficiency virus (HIV) into double-stranded DNA, a critical step for integration of the viral genome into host DNA[1][3][4][5]. The enzyme is a heterodimer, composed of two subunits, p66 and p51, both derived from the viral Gag-Pol polyprotein[1][2][3][7]. RT possesses two distinct enzymatic functions: an RNA-dependent DNA polymerase activity that synthesizes DNA from the RNA template, and an RNase H activity that degrades the RNA strand of RNA/DNA hybrids formed during reverse transcription[1][2][3][6]. This dual activity is required for the production of a proviral DNA that can integrate into the host cell genome and is indispensable for productive infection. Drugs targeting RT form the backbone of antiretroviral therapy, but resistance mutations frequently arise due to the enzyme’s inherent error-prone replication[5]. Both HIV-1 and HIV-2 have structurally and functionally similar reverse transcriptases, with some differences in drug susceptibility profiles[6].

Other names

HIV reverse transcriptaseHIV-1 RTHIV-2 RTRT (with appropriate context)Human immunodeficiency virus reverse transcriptase

Nucleoside/Nucleotide RT inhibitors (NRTIs/NtRTIs): - Act as chain terminators by incorporating into viral DNA, preventing further DNA synthesis by RT - Non-nucleoside RT inhibitors (NNRTIs): - Bind allosterically to RT at a distinct site, inducing conformational changes that inhibit polymerase activity - RNase H inhibitors: - Inhibit the RNase H active site, preventing degradation of RNA in RNA/DNA hybrids