Envelope glycoprotein gp160 (Env) (Env)

The HIV-1 Envelope glycoprotein gp120/gp160 is a viral surface protein complex essential for the entry of Human Immunodeficiency Virus type 1 (HIV-1) into host cells (UniProt Q9IZE4). It is synthesized as a 160 kDa precursor (gp160) that is subsequently cleaved by host furin-like proteases into two non-covalently associated subunits: the surface glycoprotein gp120 and the transmembrane glycoprotein gp41 (NIH, 2023). gp120 mediates the initial attachment of the virus to the host CD4 receptor, which induces conformational changes that allow for secondary binding to chemokine co-receptors, typically CCR5 or CXCR4 (Wikipedia). This sequential binding process is a prerequisite for gp41-mediated fusion of the viral and cellular membranes, enabling the release of the viral genome into the host cytoplasm (MDPI, 2023). Beyond its structural role, gp120 is involved in immune evasion through extensive N-linked glycosylation and can trigger apoptosis in uninfected bystander T cells, contributing to the depletion of the immune system (UniProt). In clinical practice, gp120 is the target of attachment inhibitors like fostemsavir, which prevent the virus from binding to CD4+ cells (NIH, 2024). However, the high mutation rate of the env gene leads to significant antigenic diversity, posing a major challenge for the development of long-lasting therapeutics and effective vaccines (PubMed).

Other names

gp120gp160Envelope surface glycoprotein gp120Envelope polyprotein gp160SUEnv

Attachment inhibition; the drug binds directly to the gp120 subunit of the viral envelope, preventing its interaction with the host CD4 receptor and inhibiting the conformational changes necessary for viral entry into the host cell (NIH, 2024; Wikipedia).