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

The HIV-1 Env gp140 trimer is a soluble, engineered version of the native envelope glycoprotein spike found on the surface of Human Immunodeficiency Virus type 1. It typically consists of the entire gp120 subunit and the extracellular domain (ectodomain) of the gp41 subunit, stabilized to maintain a trimeric configuration that mimics the functional viral spike (PubMed: 24179289). This molecule is a primary target for HIV-1 vaccine research, as it contains the vulnerable epitopes recognized by broadly neutralizing antibodies (bNAbs) which can prevent viral infection (NIH: NIAID). In its biological role, the native Env trimer mediates viral attachment to host CD4 receptors and subsequent membrane fusion via coreceptors like CCR5 or CXCR4 (UniProt: P04578). Because the native spike is highly unstable and heavily glycosylated, gp140 trimers (such as the SOSIP design) are used as structural templates to guide the development of immunogens and therapeutic antibodies (Nature: 10.1038/nature12653). Targeting this protein is essential for neutralizing the virus and preventing the progression of HIV infection to AIDS.

Other names

HIV-1 Env gp140gp140 trimerSoluble HIV-1 envelope trimergp120-gp41 ectodomain trimerSOSIP gp140

The gp140 trimer serves primarily as an immunogen in vaccine development to elicit broadly neutralizing antibodies (bNAbs) that block viral entry by binding to conserved epitopes on the native Env spike. In the context of therapeutic antibodies, these drugs bind to the trimer to prevent its interaction with host CD4 receptors and coreceptors (CCR5/CXCR4), thereby neutralizing the virus.