Human immunodeficiency virus type 1 envelope glycoprotein gp120 (gp120) (HIV-1 gp120)

The Human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 is a critical component of the viral entry machinery, functioning as the surface subunit of the Env trimer [UniProt P04578]. It is generated through the proteolytic cleavage of the gp160 precursor, which also produces the transmembrane gp41 subunit. gp120 is responsible for the initial attachment of the virus to host cells by binding to the CD4 receptor, a process that triggers conformational changes allowing for subsequent interaction with co-receptors like CCR5 or CXCR4 [PubMed PMID: 9660879]. These interactions are essential for the subsequent gp41-mediated fusion of the viral and host cell membranes [NIH NIAID HIV/AIDS Research]. Due to its exposed position on the viral surface, gp120 is a primary target for antiretroviral therapy and vaccine design. Drugs such as fostemsavir bind directly to gp120 to inhibit its attachment to CD4+ cells [PubChem CID: 71581154]. However, the protein's high mutation rate and dense glycan shield facilitate immune evasion and the development of drug resistance, presenting significant therapeutic challenges [PubMed PMID: 22678211].

Other names

gp120gp140HIV-1 EnvSurface subunit (SU)gp160 precursor

Attachment inhibition by binding to gp120 and preventing its interaction with the host CD4 receptor, thereby blocking viral entry into the cell.