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Envelope glycoprotein gp120 with V2 loop deletion is a mutant form of the HIV-1 envelope glycoprotein in which the V2 loop, a highly variable and immunologically important region, has been removed. The gp120 protein is part of the Env trimer complex (along with gp41), mediates the initial binding to the host cell CD4 receptor and subsequently to a chemokine coreceptor (CCR5 or CXCR4), enabling viral entry. The V2 loop in wild-type gp120 plays multiple roles: it contributes to the stabilization of the trimer, masks neutralizing epitopes, participates in receptor and coreceptor binding, and serves as a major site targeted by broadly neutralizing antibodies. Deletion of the V2 loop alters the exposure of other regions (especially the V3 loop and CD4-binding site), dramatically increases sensitivity to neutralizing antibodies, often abrogates the proper folding, surface expression, and function of the envelope glycoprotein, and impairs viral infectivity. However, ΔV2 gp120 is a useful tool in virology and immunogen design to study epitope exposure and neutralization mechanisms.
For neutralizing antibodies and entry inhibitors: Blockade of gp120 binding to CD4 and/or CCR5/CXCR4, preventing viral entry into host cells
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