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

The HIV-1 envelope glycoprotein gp140 is a recombinant, soluble trimeric ectodomain mimicking the surface envelope spike (Env) of HIV-1. It comprises the surface subunit gp120 and the external portion of the transmembrane subunit gp41, minus the transmembrane and cytoplasmic domains. gp140 presents critical conformational and linear epitopes—such as the CD4-binding site, V1/V2 and V3 loops, and the membrane-proximal external region—required for viral entry. These epitopes are the main targets of neutralizing antibodies and are a focus of HIV vaccine research. B cell responses to gp140 are central to controlling infection and informing vaccine design. Despite structural challenges including glycan shields and epitope masking, engineered gp140 trimers are used to better present conserved neutralization epitopes to the immune system.

Other names

HIV-1 Env gp140HIV-1 envelope trimer (soluble or cleaved/uncleaved)HIV-1 envelope glycoprotein ectodomainHIV-1 gp160 (precursor, cleaved to gp120 + gp41; gp140 is an engineered ectodomain)

For neutralizing antibodies: Block viral entry by binding to conserved epitopes (e.g., CD4 binding site, V3 loop, MPER) on gp140/gp120/gp41, preventing attachment or membrane fusion. For fusion inhibitors: Stabilize non-fusogenic conformations or block conformational transitions required for membrane fusion (often targeting gp41). For vaccine immunogens: Present conserved epitopes to elicit broadly neutralizing or ADCC-mediating antibodies.