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.
MeSH terms
-
Cell Line
-
Cell Proliferation / drug effects
-
Cytopathogenic Effect, Viral / drug effects
-
Enfuvirtide
-
HIV Envelope Protein gp41 / pharmacology
-
HIV Fusion Inhibitors / pharmacology*
-
HIV Fusion Inhibitors / toxicity
-
HIV-1 / drug effects*
-
HIV-1 / physiology*
-
Humans
-
Microbial Sensitivity Tests / methods
-
Oligopeptides / genetics
-
Oligopeptides / pharmacology*
-
Oligopeptides / toxicity
-
Peptide Fragments / pharmacology
-
Protein Multimerization
-
Virus Internalization / drug effects*
-
rhoA GTP-Binding Protein / genetics
-
rhoA GTP-Binding Protein / pharmacology*
-
rhoA GTP-Binding Protein / toxicity
Substances
-
HIV Envelope Protein gp41
-
HIV Fusion Inhibitors
-
Oligopeptides
-
Peptide Fragments
-
RHOA protein, human
-
Enfuvirtide
-
rhoA GTP-Binding Protein