Exterior membrane glycoprotein (gp120) (gp120)

Exterior membrane glycoprotein, commonly referred to as gp120, is a critical component of the human immunodeficiency virus (HIV) envelope complex. It is a surface glycoprotein that forms a trimeric spike with the transmembrane protein gp41, facilitating the virus's ability to infect host cells. The primary biological function of gp120 is to mediate attachment to host immune cells by binding to the CD4 receptor and subsequently to chemokine co-receptors like CCR5 or CXCR4. This series of interactions triggers a conformational change that enables the viral and cellular membranes to fuse, allowing the viral genome to enter the cell. Because of its essential role in the HIV life cycle, gp120 is a major target for therapeutic intervention. Drugs such as fostemsavir (and its active form temsavir) act as attachment inhibitors by binding directly to gp120 and preventing its interaction with the CD4 receptor. Additionally, gp120 is a central focus for the development of broadly neutralizing antibodies and vaccines aimed at preventing HIV infection.

Other names

Surface glycoprotein gp120Envelope glycoprotein gp120EnvHIV-1 gp120SU

Attachment inhibition; CD4-binding site competition; Stabilization of the pre-fusion trimer conformation