HIV-1 Clade C envelope glycoprotein gp140 (gp140)

The HIV-1 Clade C envelope glycoprotein gp140 is a soluble, trimeric version of the viral envelope protein (Env) derived from the Clade C subtype, which is the most prevalent HIV-1 variant globally [18, 19]. It is composed of the gp120 surface subunit and the extracellular portion (ectodomain) of the gp41 transmembrane subunit, mimicking the functional "spike" found on the surface of the virus [5, 13]. The primary biological role of this glycoprotein is to facilitate viral entry into host CD4+ T cells by binding to the CD4 receptor and subsequent co-receptors like CCR5 or CXCR4, which triggers a series of conformational changes leading to membrane fusion [9, 17]. In the context of disease, gp140 is the principal target for the host's humoral immune response and is a central focus for the development of preventative vaccines and therapeutic monoclonal antibodies [7, 14]. Drugs targeting this molecule, such as entry inhibitors and broadly neutralizing antibodies (bNAbs), work by physically blocking receptor binding sites or stabilizing the protein in a non-functional state to prevent infection [9, 12]. Due to its high degree of glycosylation and extreme sequence variability, gp140 presents significant challenges for drug and vaccine design, requiring sophisticated engineering like SOSIP stabilization to maintain its native-like structure [13, 24]. Clinical monitoring of therapies targeting this glycoprotein involves assessing viral load suppression and the induction of specific neutralizing antibody titers [11, 14].

Other names

HIV-1 subtype C gp140Env gp140 (Clade C)HIV-1 envelope glycoprotein gp140gp140 trimer

Inhibition of viral entry by blocking receptor attachment or preventing membrane fusion.