Human immunodeficiency virus type 1 surface glycoprotein gp120 (gp120)

The HIV-1 surface glycoprotein gp120 is a critical component of the viral envelope spike, serving as the primary mediator for viral attachment and entry into host cells. It is derived from the proteolytic cleavage of the gp160 precursor protein into the gp120 surface subunit and the gp41 transmembrane subunit. The biological function of gp120 involves high-affinity binding to the host CD4 receptor on T-lymphocytes and macrophages, which induces conformational changes that allow the virus to engage coreceptors such as CCR5 or CXCR4. This sequential binding process is essential for initiating the fusion of the viral and host cell membranes, thereby facilitating infection. In clinical practice, gp120 is a significant therapeutic target; for example, the drug fostemsavir (and its active form temsavir) acts as an attachment inhibitor by binding to gp120 and preventing its interaction with CD4. However, the high genetic diversity and rapid mutation rate of the HIV-1 envelope present substantial challenges for drug development, often leading to the selection of resistant viral variants.

Other names

Surface glycoproteinSUgp120 subunitEnvelope surface glycoprotein gp120Env gp120

Attachment inhibition by binding directly to the gp120 subunit, preventing the conformational change required for CD4 receptor interaction and subsequent viral entry.