Abstract
During 30 years of research on human immunodeficiency virus (HIV), our knowledge of its cellular receptors - CD4, CCR5 and CXCR4 - has illuminated aspects of the pathogenesis of the acquired immune deficiency syndrome (AIDS). Studying how the HIV envelope glycoproteins interact with the receptors led to anti-retroviral drugs based on blocking the docking or fusion of virus to the host cell. Genetic polymorphisms of CCR5 determine resistance to HIV infection and the rate of progression to AIDS. Eliciting neutralizing antibodies to the sites of receptor interaction on HIV glycoproteins is a promising approach to HIV vaccine development.
Highlights
During 30 years of research on human immunodeficiency virus (HIV), our knowledge of its cellular receptors – CD4, CCR5 and CXCR4 – has illuminated aspects of the pathogenesis of the acquired immune deficiency syndrome (AIDS)
As we celebrate the 30th anniversary of the discovery of HIV-1 by Françoise Barré-Sinoussi and colleagues [1], it is a sobering thought that during the two years between the first notification of AIDS [2] and the discovery of its cause, epidemiologists established all the modes of transmission and risk factors associated with HIV-1 infection without knowing the identity of the virus
It became apparent from the first full clinical description of AIDS in 1981 [3] that the salient feature underlying the disease is a specific depletion of CD4 T‐helper lymphocytes
Summary
During 30 years of research on human immunodeficiency virus (HIV), our knowledge of its cellular receptors – CD4, CCR5 and CXCR4 – has illuminated aspects of the pathogenesis of the acquired immune deficiency syndrome (AIDS). The viral envelope is studded with viral glycoprotein ‘spikes’ that recognize the cell receptors to which HIV binds as the first step in virus entry. Gp120 bears the binding sites for the CD4 viral receptor and chemokine co-receptors, while gp41 contains the hydrophobic domains that effect fusion between viral envelope and host membranes.
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