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HIV-1 protease or PR is a retroviral aspartyl protease (retropepsin), an enzyme involved with peptide bond hydrolysis in retroviruses, that is essential for the life-cycle of HIV, the retrovirus that causes AIDS.
The HIV-1 protease (HIV-1 PR) is a virus-specific aspartic protease responsible for processing the polyproteins of gag and gag-pol during virion maturation and for the proliferation of the retrovirus (Fig. 2.7).
The function of HIV protease is to cleave the initial polyprotein into its functional constituents (Sussman et al., 2013). This enzyme is made up of a dimer of identical subunits that mimics the two-lobed monomeric structure of pepsin and other aspartate proteases.
HIV protease cuts up large precursor proteins into smaller proteins. These smaller proteins combine with HIV’s genetic material to form a new HIV virus. Protease inhibitors (PIs) prevent HIV from replicating by blocking protease.
HIV protease plays a critical role in viral maturation for producing infectious virus particles. The protease cleaves the precursor Gag and Gag-Pol polyproteins at a minimum of 9 distinct sites.
HIV-1 protease (EC 3.4.23.16; HIV-1 PR) is required for the infectivity of the retrovirus “HIV” (a retrovirus that embodies its genetic information as RNA). HIV causes “AIDS” (acquired immune deficiency syndrome).
HIV protease, the third virally encoded enzyme, is required in this step to cleave a viral polyprotein precursor into individual mature proteins. The viral RNA and viral proteins assemble at the cell surface into new virions, which then bud from the cell and are released to infect another cell.
