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The **Gag–Pol polyprotein of HIV-1** is a large, multifunctional viral precursor protein generated by a ribosomal frameshift event during HIV-1 translation[4][7][8][9]. It contains at its N-terminus the *Gag* region (which mediates viral structural assembly and budding) and at its C-terminus the *Pol* region, which encodes the viral enzymes **protease (PR)**, **reverse transcriptase (RT)**, and **integrase (IN)**[2][5][6][8][9]. During viral maturation, the *Gag–Pol polyprotein* is cleaved by the encoded protease to yield mature structural proteins and functional enzymes critical for HIV-1 infectivity. Inhibition of this processing step leads to noninfectious, immature viral particles, forming the basis of current antiretroviral therapies targeting the protease, reverse transcriptase, and integrase activities[7][8][9]. The polyprotein is essential for HIV Assembly, maturation, and integration, making it a principal target in anti-HIV drug development[7][8].
Inhibition of viral protease prevents cleavage of Gag and Gag-Pol, arresting viral maturation - Inhibition of reverse transcriptase blocks conversion of viral RNA to DNA - Inhibition of integrase prevents integration of viral DNA into the host genome
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