HIV-1 envelope glycoprotein 140 (gp140) trimer (HIV-1 Env gp140)

The HIV-1 envelope glycoprotein (Env) gp140 trimer is a soluble, recombinant form of the viral spike protein responsible for HIV-1 entry into host cells [4, 8]. It consists of three gp120 subunits non-covalently associated with the ectodomains of three gp41 subunits, often stabilized (e.g., SOSIP or NFL designs) to mimic the native, prefusion trimeric structure found on the virion surface [9, 16]. As the sole target for neutralizing antibodies, the Env trimer is a primary focus for HIV-1 vaccine development and therapeutic antibody design [6, 15]. It mediates viral attachment by binding to the host CD4 receptor and subsequent coreceptors (CCR5 or CXCR4), triggering conformational changes that lead to membrane fusion [13, 20]. Drugs and antibodies targeting this molecule, such as broadly neutralizing antibodies (bNAbs) and entry inhibitors like fostemsavir or enfuvirtide, aim to block these entry steps, thereby preventing infection or reducing viral spread [14, 22]. However, the high degree of antigenic diversity and the presence of a dense glycan shield present significant challenges for effective drug and vaccine design [2, 18].

Other names

gp140HIV-1 Env trimerSoluble gp140SOSIP gp140NFL gp140Env spikeHIV-1 envelope glycoprotein complex

Inhibition of viral entry by blocking the interaction between the viral envelope and host cell receptors (CD4, CCR5, or CXCR4) or by preventing the conformational changes required for membrane fusion [13, 14, 22].