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A RhoA-derived peptide inhibits human immunodeficiency virus-1 entry in vitro.
|Title||A RhoA-derived peptide inhibits human immunodeficiency virus-1 entry in vitro.|
|Publication Type||Journal Article|
|Year of Publication||2011|
|Authors||Maselko M, Ward C, Pastey M|
|Journal||Current HIV research|
|Date Published||2011 Jan 1|
|Keywords||Cell Line, Cell Proliferation, Cytopathogenic Effect, Viral, HIV Envelope Protein gp41, HIV Fusion Inhibitors, HIV-1, Humans, Microbial Sensitivity Tests, Oligopeptides, Peptide Fragments, Protein Multimerization, rhoA GTP-Binding Protein, Virus Internalization|
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.
|Alternate Journal||Curr. HIV Res.|