Structural attributes and binding role of HIV-1 exterior envelope gp120

HIV/AIDS is a global deadly disease. Since its discovery in 1983, the Human Immunodeficiency Virus has sustained one of the major pandemics in the history of mankind [1]. Human immunodeficiency virus type 1 (HIV-1) is characterized by extensive genetic variability, as a consequence of high replication and mutation rates and frequent recombination [2,3]. The most up-to-date estimates that more than 30 million people are now living with HIV-1 infection, most of them in sub-Saharan Africa [4]. The virus depends on the physiological state of its target cells for efficient replication, and, in turn, viral infection perturbs the cellular state significantly. A cure for HIV is still urgently needed and has become a global research priority. A unique cohort of HIV-infected individuals who spontaneously control HIV exists, and these are known as ‚elite controllers‘ [5]. These subjects represent a model with long term control of viral replication and HIV remission, based on natural CD4+ T cells depletion. CD4+ T cells play important role particularly in the adaptive immune system by releasing T cell cytokines, thus helping to suppress or regulate immune responses [6]. CD4+ T cells are a primary target of HIV viral entry, because of interaction between HIV exterior envelope glycoprotein 120 (gp120) and CD4 receptor found on the surface of CD4+ T cells [7,8]. Thereof, perfect understanding of interaction between gp120 and CD4 receptors could lead to development of novel chemical substances with ability to block this interaction and inhibit the viral entry into the host cells. The present paper focuses on description of role of gp120 in entry into the host cells through interaction with their CD4 receptors and further summarizes recent knowledge in development of HIV vaccines based on interaction with gp120.

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