Integrase strand transfer enzyme of human immunodeficiency virus type 1 (HIV-1 integrase)

Integrase strand transfer enzyme of human immunodeficiency virus type 1 (HIV-1 integrase) is an essential viral enzyme required for the integration of viral DNA into the genome of the host cell, a key step in the retroviral replication cycle[5][4]. The enzyme is encoded by the pol gene as part of the viral Gag-Pol polyprotein and is released during virion maturation. HIV-1 integrase consists of three domains: the N-terminal domain, which coordinates zinc and is involved in multimerization; the catalytic core domain, containing a conserved DDE motif essential for catalysis; and the C-terminal domain, which non-specifically binds DNA[5][1]. The enzyme performs two distinct biochemical activities: (1) 3'-processing—removal of nucleotides from the 3' ends of viral DNA, and (2) strand transfer—joining the processed viral DNA ends to the host chromosome[4][7]. Integrase inhibitors (INSTIs) are a class of antiretroviral drugs that block the strand transfer reaction, thus preventing establishment of proviral infection. HIV-1 integrase is a major therapeutic target in antiretroviral therapy for HIV/AIDS[4][5][6].

Other names

HIV-1 integraseHIV integraseHIV-1 INRetroviral integrase

Inhibition of integrase-mediated strand transfer (prevents insertion of viral DNA into host genome); Binding to the catalytic core and chelating essential divalent metals, thus blocking enzymatic activity[6][4][5]