HIV-1 envelope glycoprotein (ectodomain gp140) (HIV-1 Env gp140)

The HIV-1 envelope glycoprotein gp140 is a recombinant soluble ectodomain form of the native Env spike on the HIV-1 virion, typically constructed as a trimer derived from the viral gp160 precursor, encompassing the entire gp120 and the external region of gp41[3][5][8]. In HIV-1, the full Env spike is composed of three gp120–gp41 heterodimers and is essential for mediating viral entry by binding the cellular CD4 receptor and a chemokine co-receptor (CCR5 or CXCR4), which triggers conformational changes resulting in fusion of viral and host cell membranes[1][7]. Recombinant gp140 mimics the native Env trimer's architecture, preserving key conformational states and antigenic properties, and is a focus for vaccine design due to its central role in HIV infection and its exposure on the viral surface[3][5][6][8]. However, the Env exhibits considerable antigenic heterogeneity and extensive glycosylation, presenting major challenges for developing effective vaccines and therapeutics[1][8]. gp140 is used as an immunogen for eliciting neutralizing antibodies and as a target for entry inhibitors such as enfuvirtide (T-20)[2]. Stabilized forms (e.g., SOSIP gp140) are designed to retain critical epitopes for broad antibody recognition while aiming to present Env conformations relevant for neutralization[3][6][8].

Other names

Env (envelope glycoprotein)gp140 (soluble/truncated/modified ectodomain form)HIV-1 Env trimergp120–gp41 ectodomain

Block receptor binding (CD4, coreceptors) Inhibit conformational changes required for fusion Prevent formation of fusion intermediate (pre-hairpin or six-helix bundle)