Human immunodeficiency virus type 2 envelope glycoprotein gp125 (HIV-2 gp125)

Human immunodeficiency virus type 2 envelope glycoprotein gp125 is the surface subunit (SU) of the viral envelope protein complex, essential for the virus's ability to infect host cells. It is produced by the proteolytic cleavage of the gp140 precursor protein by host cell furin-like proteases during viral maturation (UniProt P04577). The primary function of gp125 is to mediate viral entry by binding to the host CD4 receptor and subsequently to a co-receptor, typically CCR5 or CXCR4, which triggers the fusion process (PubMed: 25142596). While HIV-2 is generally less pathogenic than HIV-1, gp125 remains a critical factor in the progression to Acquired Immunodeficiency Syndrome (AIDS) by facilitating the depletion of CD4+ T-cells. From a therapeutic perspective, gp125 is a challenging target due to its high degree of glycosylation and genetic variability, which allow the virus to evade the host immune response. Furthermore, HIV-2 is intrinsically resistant to several classes of antiretroviral drugs used for HIV-1, including non-nucleoside reverse transcriptase inhibitors and the fusion inhibitor enfuvirtide, making the development of specific gp125-targeted therapies a high priority for managing multi-drug resistant infections (NIH: HIV-2 Treatment Guidelines).

Other names

HIV-2 surface glycoproteingp125HIV-2 SUEnvelope surface glycoprotein gp125HIV-2 Env protein

Entry inhibition