Human immunodeficiency virus 1 envelope glycoprotein with V2 loop deletion (HIV-1 DeltaV2 Env) (HIV-1 DeltaV2 Env)

Human immunodeficiency virus 1 envelope glycoprotein with V2 loop deletion (HIV-1 DeltaV2 Env) is an engineered variant of the HIV-1 Env protein, which is the primary mediator of viral entry into host cells (Wang et al., 2017, Journal of Virology). The native Env protein is a trimeric complex of gp120 and gp41 subunits that facilitates attachment to CD4 receptors and coreceptors (Prentoe et al., 2013, Journal of Virology). In the wild-type virus, the V1 and V2 variable loops of gp120 form a protective shield over highly conserved epitopes, such as the CD4 binding site, to evade the host immune system (Sanders & Moore, 2017, Immunological Reviews). By deleting the V2 loop, the protein adopts a more "open" conformation, significantly increasing the exposure of these conserved regions to B-cell receptors (NIH, 2023, HIV Vaccine Development). This modification is a key strategy in vaccine design, aimed at eliciting broadly neutralizing antibodies (bNAbs) that can recognize and neutralize a wide range of HIV-1 clinical isolates. DeltaV2Env is frequently used in DNA, viral vector, and protein subunit vaccine platforms to improve the quality and breadth of the immune response. While it enhances the visibility of critical neutralization targets, a major challenge remains the potential for the immune system to focus on non-neutralizing or strain-specific epitopes.

Other names

HIV-1 gp120 DeltaV2V2-deleted HIV-1 envelope glycoproteinHIV-1 Env DeltaV2gp120 dV2HIV-1 DeltaV2 gp120

Monoclonal antibodies like VRC01 bind to the exposed CD4 binding site on the DeltaV2Env protein, preventing the virus from attaching to and infecting host CD4+ T-cells (Wang et al., 2017, Journal of Virology). As a vaccine immunogen, it functions by presenting conserved epitopes to B-cells to stimulate the production of endogenous neutralizing antibodies (Prentoe et al., 2013, Journal of Virology).