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Antifungal Activity of an Abundant Thaumatin-Like Protein from Banana against Penicillium expansum, and Its Possible Mechanisms of Action.

Identifieur interne : 000072 ( Main/Exploration ); précédent : 000071; suivant : 000073

Antifungal Activity of an Abundant Thaumatin-Like Protein from Banana against Penicillium expansum, and Its Possible Mechanisms of Action.

Auteurs : Wenxiao Jiao [République populaire de Chine] ; Xiangxin Li [République populaire de Chine] ; Handong Zhao [République populaire de Chine] ; Jiankang Cao [République populaire de Chine] ; Weibo Jiang [République populaire de Chine]

Source :

RBID : pubmed:29899211

Descripteurs français

English descriptors

Abstract

Thaumatin-like protein from banana (designated BanTLP) has been purified by employing a simple protocol consisting of diethylaminoethyl Sephadex (DEAE⁻Sephadex) chromatography, gel filtration on Sephadex G50, and reversed-phase chromatography. The purified protein was identified by MALDI-TOF mass spectrometry, with an estimated molecular weight of 22.1 kDa. BanTLP effectively inhibited in vitro spore germination of Penicillium expansum, one of the main postharvest pathogens in fruits. This study further investigated the antifungal properties and underlying mechanisms of BanTLP against P. expansum. Results demonstrated that BanTLP exhibited antifungal activity in a wide pH range (4.0⁻10.0) at 20⁻50 °C. Propidium iodide (PI) influx and potassium release confirmed that BanTLP induced membrane disruption of the test pathogen, increasing the membrane permeability and disintegration of the cell. This led to cell death, as evidenced by the assays of thiobarbituric acid-reactive species (TBARS) content, the production of reactive oxygen species (ROS), and 1,6-diphenyl-1,3,5-hexatriene (DPH) fluorescence integrity. Ultrastructural alterations in P. expansum conidia after BanTLP treatment revealed severe damage to the cell wall. These results suggest that BanTLP purified from banana exerts antifungal activity against P. expansum by inducing plasma membrane disturbance and cell wall disorganization.

DOI: 10.3390/molecules23061442
PubMed: 29899211
PubMed Central: PMC6099679


Affiliations:


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Le document en format XML

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<term>Chromatography, Ion Exchange (MeSH)</term>
<term>Chromatography, Reverse-Phase (MeSH)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
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<term>Antifongiques (pharmacologie)</term>
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<term>Chromatographie en phase inverse (MeSH)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Musa (métabolisme)</term>
<term>Paroi cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Penicillium (effets des médicaments et des substances chimiques)</term>
<term>Penicillium (physiologie)</term>
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<term>Protéines végétales (pharmacologie)</term>
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<div type="abstract" xml:lang="en">Thaumatin-like protein from banana (designated BanTLP) has been purified by employing a simple protocol consisting of diethylaminoethyl Sephadex (DEAE⁻Sephadex) chromatography, gel filtration on Sephadex G50, and reversed-phase chromatography. The purified protein was identified by MALDI-TOF mass spectrometry, with an estimated molecular weight of 22.1 kDa. BanTLP effectively inhibited in vitro spore germination of
<i>Penicillium expansum</i>
, one of the main postharvest pathogens in fruits. This study further investigated the antifungal properties and underlying mechanisms of BanTLP against
<i>P. expansum</i>
. Results demonstrated that BanTLP exhibited antifungal activity in a wide pH range (4.0⁻10.0) at 20⁻50 °C. Propidium iodide (PI) influx and potassium release confirmed that BanTLP induced membrane disruption of the test pathogen, increasing the membrane permeability and disintegration of the cell. This led to cell death, as evidenced by the assays of thiobarbituric acid-reactive species (TBARS) content, the production of reactive oxygen species (ROS), and 1,6-diphenyl-1,3,5-hexatriene (DPH) fluorescence integrity. Ultrastructural alterations in
<i>P. expansum</i>
conidia after BanTLP treatment revealed severe damage to the cell wall. These results suggest that BanTLP purified from banana exerts antifungal activity against
<i>P. expansum</i>
by inducing plasma membrane disturbance and cell wall disorganization.</div>
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<AbstractText>Thaumatin-like protein from banana (designated BanTLP) has been purified by employing a simple protocol consisting of diethylaminoethyl Sephadex (DEAE⁻Sephadex) chromatography, gel filtration on Sephadex G50, and reversed-phase chromatography. The purified protein was identified by MALDI-TOF mass spectrometry, with an estimated molecular weight of 22.1 kDa. BanTLP effectively inhibited in vitro spore germination of
<i>Penicillium expansum</i>
, one of the main postharvest pathogens in fruits. This study further investigated the antifungal properties and underlying mechanisms of BanTLP against
<i>P. expansum</i>
. Results demonstrated that BanTLP exhibited antifungal activity in a wide pH range (4.0⁻10.0) at 20⁻50 °C. Propidium iodide (PI) influx and potassium release confirmed that BanTLP induced membrane disruption of the test pathogen, increasing the membrane permeability and disintegration of the cell. This led to cell death, as evidenced by the assays of thiobarbituric acid-reactive species (TBARS) content, the production of reactive oxygen species (ROS), and 1,6-diphenyl-1,3,5-hexatriene (DPH) fluorescence integrity. Ultrastructural alterations in
<i>P. expansum</i>
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<i>P. expansum</i>
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