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

Human immunodeficiency virus type 1 envelope glycoprotein gp120 is a surface-exposed viral protein that is essential for the infection of host cells. It functions by binding to the host CD4 receptor and subsequent chemokine co-receptors (CCR5 or CXCR4) on the surface of immune cells, initiating the process of viral entry (UniProt P04578). As a primary target for the immune system, gp120 is the focus of therapeutic development for both vaccines and monoclonal antibodies. The broadly neutralizing antibody 10-1074-LS specifically targets the conserved V3-glycan supersite of gp120, which is a vulnerable region present on many HIV-1 variants (Caskey et al., 2017, Nature Medicine). The LS designation indicates a modification in the antibody's Fc region that extends its half-life in the bloodstream, allowing for less frequent dosing (Gaudinski et al., 2018, PLOS Medicine). However, the high mutation rate of HIV-1 remains a significant challenge, as the virus can develop resistance by altering the structure of gp120 to prevent antibody binding.

Other names

Envgp120Surface protein gp120SUEnvelope surface glycoprotein gp120

Neutralization of viral entry by binding to the V3-glycan supersite of gp120, thereby sterically hindering the virus from interacting with host cell receptors and inhibiting the conformational changes required for membrane fusion (Caskey et al., 2017, Nature Medicine; Schoofs et al., 2016, Science).