2. Academic Validation
  3. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide

Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide

  • Cell. 2007 Apr 20;129(2):263-75. doi: 10.1016/j.cell.2007.02.042.
Jan Münch 1,  Ludger Ständker,  Knut Adermann,  Axel Schulz,  Michael Schindler,  Raghavan Chinnadurai,  Stefan Pöhlmann,  Chawaree Chaipan,  Thorsten Biet,  Thomas Peters,  Bernd Meyer,  Dennis Wilhelm,  Hong Lu,  Weiguo Jing,  Shibo Jiang,  Wolf-Georg Forssmann,  Frank Kirchhoff
Affiliations

Affiliation

  • 1 Institute of Virology, University of Ulm, 89081 Ulm, Germany.
PMID: 17448989 DOI: 10.1016/j.cell.2007.02.042
Abstract

A variety of molecules in human blood have been implicated in the inhibition of HIV-1. However, it remained elusive which circulating natural compounds are most effective in controlling viral replication in vivo. To identify natural HIV-1 inhibitors we screened a comprehensive peptide library generated from human hemofiltrate. The most potent fraction contained a 20-residue peptide, designated VIRUS-INHIBITORY PEPTIDE (VIRIP), corresponding to the C-proximal region of alpha1-antitrypsin, the most abundant circulating serine protease inhibitor. We found that VIRIP inhibits a wide variety of HIV-1 strains including those resistant to current antiretroviral drugs. Further analysis demonstrated that VIRIP blocks HIV-1 entry by interacting with the gp41 fusion peptide and showed that a few amino acid changes increase its antiretroviral potency by two orders of magnitude. Thus, as a highly specific natural inhibitor of the HIV-1 gp41 fusion peptide, VIRIP may lead to the development of another class of antiretroviral drugs.

Figures
Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-P1753
    抗HIV-1剂
    HIV
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