Human immunodeficiency virus type 1 envelope glycoprotein gp140 (HIV-1 gp140) (HIV-1 gp140)

The HIV-1 gp140 envelope protein is a soluble, trimeric version of the viral envelope glycoprotein (Env) that includes the gp120 subunit and the ectodomain of the gp41 subunit (Sanders & Moore, 2017). It serves as a key structural representation of the functional spike used by HIV-1 to infect host cells, specifically by binding to the CD4 receptor and coreceptors like CCR5 or CXCR4 (UniProt Consortium, 2024). Because gp140 displays many of the same epitopes as the native viral spike, it is a central focus in vaccine research for eliciting broadly neutralizing antibodies (bNAbs) (Kwong & Mascola, 2018). In clinical practice, components of this protein are targeted by entry inhibitors such as Fostemsavir, which binds gp120, and Enfuvirtide, which targets the gp41 fusion machinery (FDA, 2020; PubMed, 2003). The protein's high degree of glycosylation and rapid mutational escape pose significant hurdles for drug and vaccine development (NIH, 2021). Despite these challenges, gp140 remains one of the most important targets for preventing and treating HIV-1 infection.

Other names

HIV-1 Envgp140Soluble gp140Env trimer ectodomaingp120-gp41 ectodomainEnvelope glycoprotein gp140

Inhibition of viral entry by blocking the attachment of gp120 to the host CD4 receptor, preventing subsequent interaction with coreceptors (CCR5 or CXCR4), or interfering with the gp41-mediated fusion of the viral and host cell membranes (FDA, 2020; PubMed, 2003).