HIV-1 clade C envelope glycoprotein (HIV-1 Clade C Env)

The HIV-1 clade C envelope glycoprotein (Env) is the essential surface protein complex of the Human Immunodeficiency Virus type 1, Subtype C, which is the most widespread clade globally, dominating infections in Southern Africa and India (Source: PubMed, PMID: 30655371). It is synthesized as a gp160 precursor that is proteolytically cleaved into the surface subunit gp120 and the transmembrane subunit gp41, which non-covalently associate as a trimer on the virion surface (Source: UniProt, P04578). The gp120 subunit facilitates viral attachment by binding to the host CD4 receptor and subsequent co-receptors, while gp41 mediates the fusion between the viral and host cell membranes (Source: NIH, NIAID). As the only viral antigen exposed on the surface of the virus and infected cells, it is the primary target for the host's neutralizing antibody response and a central focus for vaccine design (Source: PubMed, PMID: 29133453). Clade C Env is specifically characterized by unique structural features, such as shorter V1-V2 loops, which influence its interaction with the immune system (Source: PubMed, PMID: 24646991). Therapeutic interventions include attachment inhibitors like fostemsavir, which binds gp120, and fusion inhibitors like enfuvirtide, which targets gp41 (Source: FDA). Additionally, broadly neutralizing antibodies (bNAbs) like CAP256-VRC26.25 are being developed to specifically target conserved epitopes on the Clade C Env trimer (Source: ClinicalTrials.gov).

Other names

gp160gp120/gp41 complexHIV-1 subtype C envelope proteinEnvHIV-1 envelope trimer

Inhibition of viral entry by blocking gp120 attachment to host CD4 receptors or preventing gp41-mediated fusion of viral and host cell membranes.