Human immunodeficiency virus type 1 reverse transcriptase; Hepatitis B virus reverse transcriptase (HIV-1 RT; HBV RT)

The reverse transcriptase enzyme in HIV-1 and HBV is a multifunctional viral protein critical for replication. In HIV-1, reverse transcriptase is a heterodimer of p66 and p51 subunits, possessing DNA polymerase activity capable of copying either RNA or DNA templates, and an RNase H domain that degrades the RNA strand in RNA/DNA hybrids[1][3][5]. HBV reverse transcriptase is part of the viral polymerase and uniquely initiates viral DNA synthesis via a protein priming mechanism, with activities including RNA-dependent DNA polymerization and RNase H cleavage[6]. Both serve as main targets for antiviral drugs (nucleoside analogues) that block viral genome replication, making them essential for the management of HIV/AIDS and hepatitis B infection[4][6][8]. Drug resistance can rapidly emerge due to mutations in RT, complicating long-term therapy[7]. Note: The target as presented ("HIV-1/HBV Reverse Transcriptase") is not a canonical entity—these are distinct enzymes encoded by separate viruses with overlapping drug susceptibility but unique structural and functional features[2][6]. Each should be referenced and structured separately for clarity and scientific accuracy.

Other names

HIV-1 RTHBV RTHIV reverse transcriptaseHepatitis B reverse transcriptaseHIV-1 polymeraseHepatitis B polymerase

Nucleoside/nucleotide analogue inhibition (competitive incorporation of analogues into viral DNA, leading to chain termination and/or enzyme inhibition). Non-nucleoside inhibition (binding to allosteric sites in HIV-1 RT, distorting enzyme conformation; less relevant for HBV RT, which is only targeted by nucleoside analogues in clinics so far). Protein priming inhibition (unique to HBV RT, entecavir can inhibit this step).