Human immunodeficiency virus type 1 envelope glycoprotein gp160 (gp160) (gp160)

The HIV-1 Envelope glycoprotein gp160 is the essential precursor protein responsible for the entry of the Human Immunodeficiency Virus type 1 into host cells [1]. Synthesized in the endoplasmic reticulum, gp160 undergoes extensive glycosylation and is subsequently cleaved by host cell proteases, such as furin, into two functional subunits: the surface glycoprotein gp120 and the transmembrane glycoprotein gp41 [4]. These subunits form a non-covalent trimeric complex on the viral envelope, where gp120 facilitates initial attachment to the CD4 receptor and subsequent binding to co-receptors like CCR5 or CXCR4 [2]. This binding triggers a conformational change in gp41, leading to the fusion of the viral and host cell membranes, allowing the viral capsid to enter the cytoplasm [2]. As the sole viral protein exposed on the virion surface, gp160 is the primary target for the host's neutralizing antibody response and a critical focus for vaccine development and antiretroviral therapy [1]. Drugs such as fostemsavir target the gp120 subunit to prevent attachment, while enfuvirtide targets gp41 to inhibit membrane fusion [3].

Other names

EnvEnvelope polyproteingp160 precursorHIV-1 gp160Envelope glycoprotein

Inhibition of viral entry by blocking gp120 attachment to CD4 receptors or preventing gp41-mediated membrane fusion.