Abstract
HIV-1 entry is an attractive target for anti-HIV-1 therapy. However, there are no entry inhibitors approved for the clinical treatment of HIV-1 infection. This is likely to be changed in the near future since promising HIV-1 entry inhibitors, such as T20 and some chemokine receptor antagonists, are in the pipeline to join the repertoire of anti-HIV-1 therapeutics. This review will focus on what might be potential targets on the key components of the viral entry machinery, gp120 and gp41. These two molecules are the viral proteins responsible for HIV-1 entry. Binding to CD4 induces a series of structural changes in gp120 and allows it to interact with chemokine receptors. The receptor binding eventually triggers conformational changes in gp41, which result in the formation of a fusion active molecule to attack the cell membrane. The structural and functional motifs that operate this delicate fusion machinery could become the Achilles heel of the virus.
Keywords: hiv-1 envelope glycoproteins, anti-hiv-1 therapy, chemokine receptor antagonists, gp120, gp41
Current Pharmaceutical Design
Title: Potential Drug Targets on the HIV-1 Envelope Glycoproteins, gp120 and gp41
Volume: 9 Issue: 18
Author(s): Li Huang, Linda Zhang and Chin Ho Chen
Affiliation:
Keywords: hiv-1 envelope glycoproteins, anti-hiv-1 therapy, chemokine receptor antagonists, gp120, gp41
Abstract: HIV-1 entry is an attractive target for anti-HIV-1 therapy. However, there are no entry inhibitors approved for the clinical treatment of HIV-1 infection. This is likely to be changed in the near future since promising HIV-1 entry inhibitors, such as T20 and some chemokine receptor antagonists, are in the pipeline to join the repertoire of anti-HIV-1 therapeutics. This review will focus on what might be potential targets on the key components of the viral entry machinery, gp120 and gp41. These two molecules are the viral proteins responsible for HIV-1 entry. Binding to CD4 induces a series of structural changes in gp120 and allows it to interact with chemokine receptors. The receptor binding eventually triggers conformational changes in gp41, which result in the formation of a fusion active molecule to attack the cell membrane. The structural and functional motifs that operate this delicate fusion machinery could become the Achilles heel of the virus.
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Cite this article as:
Huang Li, Zhang Linda and Chen Ho Chin, Potential Drug Targets on the HIV-1 Envelope Glycoproteins, gp120 and gp41, Current Pharmaceutical Design 2003; 9 (18) . https://dx.doi.org/10.2174/1381612033454720
DOI https://dx.doi.org/10.2174/1381612033454720 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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