Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev.
Antifungal effects of nuclear entry inhibitory signal peptide of HIV-1 Rev protein (Rev-NIS) were investigated. Rev-NIS contained potent antifungal activities without hemolytic effects. To understand the antifungal mechanism(s), in vivo and in vitro fluorescent studies were conducted. Flow cytometric analysis with bis-(1,3-dibutylbarbituric acid) trimethine oxonol [DiBAC(4)(3)] and calcein-leakage measurement from large unilamellar vesicles (LUVs) indicated that Rev-NIS depolarized and disrupted the fungal membranes. These results were further confirmed by using giant unilamellar vesicles (GUVs). The current study suggests that Rev-NIS exerts its antifungal activity with membrane-active mechanism(s).
School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, 1370 Sankyuk-dong, Puk-ku, Daegu 702-701, Republic of Korea.
Juneyoung
J
Lee
Dong Gun
DG
Lee
D000935:Antifungal Agents / Q000494:pharmacology*; D002175:Candida / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D008290:Malassezia / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D021382:Protein Sorting Signals; D014250:Trichosporon / Q000187:drug effects; D054321:rev Gene Products, Human Immunodeficiency Virus / Q000737:chemistry*
D000935:Antifungal Agents; D021382:Protein Sorting Signals; D054321:rev Gene Products, Human Immunodeficiency Virus; C514860:rev protein, Human Immunodeficiency Virus-1