Envelope glycoprotein gp120 (HIV-1) (gp120)

Envelope glycoprotein gp120 is a heavily glycosylated surface protein found on the HIV-1 viral envelope[1][3][7]. It is derived from proteolytic cleavage of precursor gp160 into two non-covalently linked subunits: the surface subunit gp120 and the transmembrane subunit gp41[1][3]. Gp120 mediates viral attachment by binding first to the host CD4 receptor, predominantly on helper T-cells, then to a co-receptor (CCR5 or CXCR4), inducing conformational changes that facilitate membrane fusion and viral entry[1][5][9]. The structure of gp120 features conserved inner and outer domains, variable loops (notably V1/V2 and V3), and extensive glycan shielding, enabling both receptor recognition and immune evasion[2][3][5][6][9]. Gp120 is a major target for broadly neutralizing antibodies, entry inhibitors, and vaccine efforts, but therapeutic design is challenged by its exceptional sequence diversity, glycan shield, and conformational flexibility[3][5][6][9]. No apparent spelling or naming errors were found; "Envelope glycoprotein gp120" accurately and specifically describes the canonical HIV-1 envelope target for drugs and antibodies[1][2][3].

Other names

HIV-1 gp120HIV envelope glycoprotein gp120SU (surface unit)Human immunodeficiency virus type 1 gp120

Inhibition of gp120-CD4 binding (blocks viral attachment); Inhibition of gp120-co-receptor binding (prevents fusion/entry); Neutralization via antibodies binding conformational epitopes; Allosteric stabilization of non-functional conformations