Human immunodeficiency virus type 1 glycoprotein 120 constant region 1 (HIV-1 gp120 C1)

The HIV-1 gp120 C1 region is the first of five conserved domains within the gp120 surface glycoprotein of the Human Immunodeficiency Virus type 1. It is located at the N-terminus of the protein and is essential for the non-covalent association between gp120 and the gp41 transmembrane subunit, maintaining the stability of the viral envelope (Env) trimer (Source: UniProt P04578; PubMed: 24089453). During the viral entry process, the binding of gp120 to the host CD4 receptor triggers a conformational shift that exposes the C1 region, making it a target for CD4-induced (CD4i) antibodies (Source: PubMed: 25552715). While many antibodies targeting C1 are non-neutralizing, they are highly effective at mediating antibody-dependent cellular cytotoxicity (ADCC), which helps eliminate infected cells (Source: PubMed: 22933714). Consequently, the C1 region is a significant focus in HIV vaccine research, particularly for strategies aimed at eliciting protective ADCC responses. Therapeutic approaches also include the use of small-molecule CD4 mimetics to open the Env trimer and expose C1 epitopes to the immune system (Source: PubMed: 26085151). This region's relative conservation across various HIV-1 strains makes it an attractive target for broad-spectrum immune interventions. Understanding the structural dynamics of the C1 region is crucial for developing next-generation entry inhibitors and immunogens.

Other names

gp120 C1 domainN-terminal constant region of gp120HIV-1 gp120 C1 regionConstant region 1 of gp120

Mediation of antibody-dependent cellular cytotoxicity (ADCC) and stabilization of the gp120-gp41 interface.