Human immunodeficiency virus type 1 viral proteins (HIV-1 proteins)

Human immunodeficiency virus type 1 (HIV-1) viral proteins encompass the full suite of proteins encoded by the HIV-1 genome, which are critical for the virus's ability to infect host cells, replicate, and evade the immune system (UniProt, 2024). These proteins are synthesized as polyprotein precursors (Gag, Gag-Pol, and Env) that are subsequently cleaved by viral or host proteases into functional units, alongside several regulatory (Tat, Rev) and accessory (Vif, Vpr, Vpu, Nef) proteins (NIH, 2023). The enzymes—reverse transcriptase, integrase, and protease—are the most well-established therapeutic targets, forming the backbone of highly active antiretroviral therapy (HAART) (StatPearls, 2023). Additionally, the envelope glycoproteins (gp120 and gp41) and the capsid protein (CA) serve as targets for entry and capsid inhibitors, respectively (PubMed, 2022). By targeting these proteins, pharmacological interventions aim to suppress viral replication to undetectable levels, thereby preventing the progression to Acquired Immunodeficiency Syndrome (AIDS) and reducing transmission (WHO, 2023).

Other names

HIV-1 gene productsHIV-1 polyproteinsHIV-1 proteomeHIV-1 structural and regulatory proteins

Drugs targeting HIV-1 viral proteins act by inhibiting essential steps in the viral life cycle: reverse transcriptase inhibitors (NRTIs and NNRTIs) block the conversion of viral RNA to DNA; protease inhibitors (PIs) prevent the cleavage of polyproteins into mature, infectious virions; integrase strand transfer inhibitors (INSTIs) prevent the integration of viral DNA into the host genome; and entry/capsid inhibitors block viral attachment, fusion, or assembly (NIH, 2023; PubMed, 2022).