Abstract

The gp160 complex of the envelope of the HIV virus and its component gp120 are essential for viral entry into the host cell. Gp120 binding to its receptor CD4 and co-receptor, CXCR4 or CCR5 is required for fusion of viral and cellular membranes. The presence of gp120 facilitates immune escape of the virus through its profound effect on the immune cells. It is a polyclonal activator of B cells, causing them to differentiate into immunoglobulin producing cells while activating the complement cascade. This results in the formation of immune complexes that are unable to kill the virus but instead shield it from the attack of other immune cells. Such HIV-1 virus that is trapped within immune complexes and is bound to the B cells via CD21 is more infectious than the free virion. In addition, HIV virions are trapped on the membrane of follicular dendritic cells (FDC) processes in immune complexes or through complement receptors. Thus, FDC can serve as a ‘Trojan horse’ and transmit the trapped virus to CD4+ T lymphocytes as they migrate through the germinal centre to the follicular mantle and paracortical areas. It was demonstrated that CXCR4-binding HIV-1 X4 gp120 causes the movement of T cells, including HIV-specific CTL, away from high concentrations of the viral protein and its expression by target cells reduces CTL efficacy in vitro. Therefore, apart from the essential role in viral attachment and infection of cells, gp120 possesses several properties that affect the behavior of immune cells and skew the immune response to the virus facilitating viral escape.

Keywords: HIV, gp120, T cells, B cells, structure, escape