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Human immunodeficiency virus type 1 Gag protein p24, also known as the capsid protein (CA), is the primary structural component of the HIV-1 core [1, 13]. It is generated through the proteolytic cleavage of the Gag polyprotein (Pr55Gag) by the viral protease during the maturation phase of the viral life cycle [8, 12]. Approximately 1,500 to 3,000 p24 subunits assemble into a characteristic cone-shaped shell that encapsulates and protects the viral RNA genome and essential enzymes [5, 6]. Beyond its structural role, p24 is critical for multiple stages of infection, including viral uncoating, reverse transcription, and the nuclear import of the pre-integration complex [2, 8]. As a therapeutic target, p24 is inhibited by a novel class of antiretrovirals known as capsid inhibitors, such as lenacapavir, which disrupt the stability of the capsid to block both early and late stages of replication [1, 6]. These drugs interfere with the precise assembly and disassembly processes required for the virus to infect new cells and produce infectious progeny [3, 9]. Additionally, p24 serves as a vital diagnostic biomarker, as its presence in the blood allows for the early detection of HIV-1 infection during the window period before antibodies are detectable [4, 17].
Capsid inhibition (disruption of viral assembly and disassembly), interference with host factor interactions (e.g., CPSF6, NUP153)
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