Human immunodeficiency virus type 1 surface glycoprotein gp120 (gp120) (gp120)

The HIV-1 gp120 envelope protein is a heavily glycosylated protein that forms the outer layer of the Human Immunodeficiency Virus type 1 (HIV-1) virion [1, 2]. It is derived from the proteolytic cleavage of the gp160 precursor and exists as a non-covalent trimer on the viral surface, associated with the transmembrane protein gp41 [1, 3]. The primary biological function of gp120 is to facilitate viral entry into host cells by binding to the CD4 receptor and subsequently to a coreceptor, typically CCR5 or CXCR4 [2, 3]. This binding triggers a series of conformational changes that allow gp41 to mediate the fusion of the viral and host cell membranes [1, 3]. Because of its essential role in the viral life cycle, gp120 is a critical target for antiretroviral therapy and vaccine development [5, 6]. Drugs like fostemsavir specifically bind to gp120 to prevent its initial attachment to CD4+ cells, thereby inhibiting infection [5, 6]. However, the protein's high mutation rate and "glycan shield" present significant challenges for long-term efficacy and broad-spectrum vaccine design [7, 8]. Therapeutic strategies also include broadly neutralizing antibodies that target conserved epitopes on gp120 to prevent viral entry across diverse strains [8].

Other names

Surface glycoprotein gp120SUEnvgp160 (precursor)

Attachment inhibition; blocking the interaction between the viral gp120 protein and the host CD4 receptor [5, 6].