Human immunodeficiency virus 1 proteins (HIV-1 proteins)

Human immunodeficiency virus 1 (HIV-1) proteins encompass a suite of structural, enzymatic, regulatory, and accessory proteins essential for the viral life cycle and pathogenesis (NIH, 2023). The enzymatic proteins, including reverse transcriptase, integrase, and protease, are the primary targets of most approved antiretroviral therapies, which work by blocking the conversion of viral RNA to DNA, the integration of viral DNA into the host genome, and the processing of viral polyproteins, respectively (UniProt, 2024). Structural proteins such as the envelope glycoproteins (gp120 and gp41) and the capsid protein (p24) are critical for viral attachment, entry, and the protection of the viral genome (PubMed, 2022). Regulatory proteins like Tat and Rev, along with accessory proteins such as Nef and Vif, facilitate efficient viral transcription, RNA export, and evasion of the host's innate and adaptive immune responses (StatPearls, 2023). These proteins are central to the progression of HIV infection to Acquired Immunodeficiency Syndrome (AIDS) by driving the depletion of CD4+ T-lymphocytes and establishing persistent viral reservoirs (WHO, 2023). While highly active antiretroviral therapy (HAART) has significantly reduced morbidity and mortality, the high mutation rate of HIV-1 proteins frequently leads to the emergence of drug resistance, necessitating the use of combination regimens and the development of novel inhibitors targeting sites like the viral capsid (FDA, 2024).

Other names

HIV-1 polyproteinsGag-Pol polyproteinEnvelope glycoprotein complex (Env)HIV-1 proteome

Nucleoside reverse transcriptase inhibition (NRTI), Non-nucleoside reverse transcriptase inhibition (NNRTI), Integrase strand transfer inhibition (INSTI), Protease inhibition (PI), Fusion inhibition, CCR5 antagonism, Attachment inhibition, and Capsid inhibition