Human immunodeficiency virus envelope glycoprotein gp140 (HIV Env gp140)

Human immunodeficiency virus envelope glycoprotein gp140 is a recombinant, soluble form of the HIV-1 envelope glycoprotein ectodomain, consisting of the extracellular portions of both gp120 (surface subunit) and the N-terminal part of gp41 (transmembrane subunit), but lacking the transmembrane and cytoplasmic domains[1][3][4][5]. Gp140 forms stable trimers that mimic the native structure of the HIV-1 envelope spike and mediate virus entry by binding to the host CD4 receptor and then to CCR5 or CXCR4 co-receptors, resulting in conformational changes that drive membrane fusion[2][4][5][9]. It is a critical target for HIV vaccine design due to its role as the main antigenic structure for neutralizing antibodies; however, extensive glycosylation, conformational flexibility, and sequence diversity present significant barriers to effective immunogen design[4][8]. Soluble stabilized forms (such as SOSIP gp140) are extensively studied as vaccine candidates and immunogens in research, but have yet to reliably induce broadly neutralizing antibody responses in humans[4][8]. Drugs and therapeutic antibodies that interact with the envelope glycoprotein can prevent HIV infection by blocking its binding or conformational activation, making it a validated antiviral target[10][9].

Other names

HIV-1 envelope glycoprotein gp140HIV Env gp140gp140HIV envelope glycoprotein ectodomainStable gp140 trimer (when referring to stabilized constructs such as SOSIP)

Inhibition of attachment to CD4 (attachment inhibitors) Blocking conformational changes required for fusion (fusion inhibitors) Neutralization of virus by antibody binding to key epitopes (neutralizing antibodies)