Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev

Juneyoung Lee; Dong Gun Lee

doi:10.1016/j.febslet.2009.03.063

Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev

Juneyoung Lee
, Dong Gun Lee

Kyungpook National University

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

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 [DiBAC₄(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).

Original language	English
Pages (from-to)	1544-1547
Number of pages	4
Journal	FEBS Letters
Volume	583
Issue number	9
DOIs	https://doi.org/10.1016/j.febslet.2009.03.063
State	Published - 6 May 2009

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Antifungal peptide
Membrane-active mechanism
Nuclear entry inhibitory signal peptide of Rev protein (Rev-NIS)

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10.1016/j.febslet.2009.03.063

Cite this

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title = "Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev",

abstract = "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 [DiBAC4(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).",

keywords = "Antifungal peptide, Membrane-active mechanism, Nuclear entry inhibitory signal peptide of Rev protein (Rev-NIS)",

author = "Juneyoung Lee and Lee, \{Dong Gun\}",

year = "2009",

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language = "English",

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journal = "FEBS Letters",

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T1 - Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev

AU - Lee, Juneyoung

AU - Lee, Dong Gun

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N2 - 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 [DiBAC4(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).

AB - 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 [DiBAC4(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).

KW - Antifungal peptide

KW - Membrane-active mechanism

KW - Nuclear entry inhibitory signal peptide of Rev protein (Rev-NIS)

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DO - 10.1016/j.febslet.2009.03.063

M3 - Article

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AN - SCOPUS:67349286175

SN - 0014-5793

VL - 583

SP - 1544

EP - 1547

JO - FEBS Letters

JF - FEBS Letters

IS - 9

ER -

Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev

Abstract

UN SDGs

Keywords

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