Human immunodeficiency virus envelope glycoprotein gp120-gp160 complex (HIV Env (gp120/gp160))

The HIV envelope glycoprotein complex, consisting of gp120 and its precursor gp160, is essential for HIV-1 entry into host cells[1][3][4]. Gp160 is synthesized as a polyprotein that is cleaved by host cell proteases into gp120, a surface-exposed subunit responsible for binding to CD4 and chemokine co-receptors on target lymphocytes, and gp41, a transmembrane subunit involved in fusion of the viral and host membranes[1][3][4][7]. The trimeric spike structure composed of gp120 and gp41 mediates viral attachment and membrane fusion. Gp120 is a primary target for neutralizing antibodies and serves as a critical target for antiretroviral drugs (e.g., entry inhibitors)[3][6]. Its high glycosylation and sequence variability contribute to the virus's ability to evade immune responses and pose significant challenges to vaccine and therapeutic antibody development[4][5][6]. Gp120 and gp160 are both key biomarkers and therapeutic targets in HIV infection and progression[1][3][6].

Other names

HIV envelope glycoproteinHIV Envgp120gp160envelope glycoprotein gp120envelope glycoprotein gp160EnvSU-gp120precursor glycoprotein gp160

- Inhibition of viral attachment to CD4 receptor\n- Blockade of co-receptor (CCR5/CXCR4) binding\n- Inhibition of membrane fusion\n- Neutralization by monoclonal antibodies targeting conformational or linear epitopes on gp120