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HIV-1 envelope glycoprotein gp150 is an engineered, truncated variant of the full-length HIV-1 envelope precursor protein, gp160 [1, 7]. It is typically generated by truncating the C-terminal cytoplasmic tail of the gp41 subunit, often at residue 730, to improve protein expression and facilitate its incorporation into virus-like particles (VLPs) for vaccine development [10, 12]. As a type I transmembrane glycoprotein, gp150 forms trimeric spikes on the viral surface that are essential for the initial stages of the HIV-1 life cycle, including attachment to host CD4 receptors and subsequent interaction with CCR5 or CXCR4 co-receptors [3, 4]. These interactions trigger conformational changes that lead to the fusion of viral and cellular membranes, allowing the viral core to enter the host cell [6, 16]. In clinical research, gp150 serves as a primary target for the induction of broadly neutralizing antibodies (bNAbs) and is the focus of various vaccine strategies [7, 11]. Drugs such as fostemsavir and enfuvirtide target the gp120 and gp41 components of the envelope complex, respectively, to inhibit viral entry [15, 17]. However, the high degree of glycosylation and rapid mutational escape of the envelope protein remain significant challenges for both therapeutic and preventative interventions [5, 17].
CD4 receptor binding, Co-receptor binding, Membrane fusion, Immunogen for neutralizing antibodies
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