1. A RhoA-derived peptide inhibits human immunodeficiency virus-1 entry in vitro.
- Author
-
Maselko M, Ward C, and Pastey M
- Subjects
- Cell Line, Cell Proliferation drug effects, Cytopathogenic Effect, Viral drug effects, Enfuvirtide, HIV Envelope Protein gp41 pharmacology, HIV Fusion Inhibitors toxicity, Humans, Microbial Sensitivity Tests methods, Oligopeptides genetics, Oligopeptides toxicity, Peptide Fragments pharmacology, Protein Multimerization, rhoA GTP-Binding Protein genetics, rhoA GTP-Binding Protein toxicity, HIV Fusion Inhibitors pharmacology, HIV-1 drug effects, HIV-1 physiology, Oligopeptides pharmacology, Virus Internalization drug effects, rhoA GTP-Binding Protein pharmacology
- Abstract
RhoA-derived peptides have been shown to have antiviral activity against both human respiratory syncytial virus and human parainfluenza virus-3. The present study investigates the toxicity, anti-HIV-1 activity and mechanism of action of a RhoA-derived peptide (RhoA 77-95). The efficacy of this peptide was compared to a scrambled peptide of the same amino acid composition and Enfuvirtide, a HIV entry inhibitor. Our data show that this RhoA-derived peptide is a non-toxic and effective inhibitor of a CXCR4 tropic strain of HIV-1. We also demonstrate that the mechanism of entry inhibition is likely mediated by polyanionic properties and is dependent on the dimerization of peptides.
- Published
- 2011
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