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Reverse transcriptase enzyme of HIV-1 (HIV-1 RT) is a heterodimeric viral enzyme essential for the replication of the human immunodeficiency virus type 1. It consists of two subunits (p66 and p51), both derived from the Gag-Pol polyprotein, and has two main enzymatic activities: (1) DNA polymerase activity (which copies viral RNA or DNA templates into DNA) and (2) RNase H activity (which degrades RNA in RNA/DNA hybrids)[1][2][4][6]. This enzyme enables the conversion of single-stranded viral RNA into double-stranded DNA, which is integrated into the host genome for productive infection. RT is the primary target of nucleoside and non-nucleoside reverse transcriptase inhibitors, a core component of antiretroviral therapy for HIV/AIDS[3]. Resistance can arise through mutations in the RT gene, which are routinely monitored to guide therapy. RT is considered an archetype of viral enzymes used as therapeutic targets, and its inhibition is fundamental to modern HIV treatment regimens[1][2].
Inhibition of DNA polymerase activity (NRTIs); Allosteric inhibition of reverse transcriptase (NNRTIs); RNase H inhibition (investigational agents)
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