Human immunodeficiency virus type 1 structural and enzymatic proteins (HIV-1 proteins)

HIV-1 structural and enzymatic proteins are the essential components of the Human Immunodeficiency Virus type 1 responsible for its life cycle and pathogenicity [9, 10, 12, 13]. The structural proteins, derived from the Gag and Env polyproteins, include the matrix (MA), capsid (CA), nucleocapsid (NC), and the envelope glycoproteins (gp120 and gp41), which facilitate viral assembly and entry into host cells [10, 12, 13, 16]. The enzymatic proteins, encoded by the Pol gene, include reverse transcriptase (RT), integrase (IN), and protease (PR), which are critical for converting viral RNA into DNA, integrating it into the host genome, and processing polyproteins into functional units [10, 13, 22]. These proteins are the primary targets for antiretroviral therapy (ART), which aims to suppress viral replication and prevent the progression to AIDS [2, 5, 6, 15, 20]. Inhibition of these targets has transformed HIV infection into a manageable chronic condition, though the emergence of drug resistance remains a significant challenge [2, 6, 15, 17, 23].

Other names

HIV-1 polyproteinsHIV-1 Gag-Pol-EnvHIV-1 proteome (partial)HIV-1 structural and enzymatic proteins

Inhibition of reverse transcription (nucleoside and non-nucleoside), inhibition of viral protease-mediated polyprotein cleavage, inhibition of integrase-mediated strand transfer, inhibition of viral entry (attachment, co-receptor binding, and fusion), and inhibition of capsid assembly/disassembly [2, 3, 4, 5, 6, 15, 19].