Multitargeted Flavonoid Inhibition of the Pathogenic Bacterium Staphylococcus aureus: A Proteomic Characterization

Wael Elmasri; Rui Zhu; Wenjing Peng; Moustafa Al-Hariri; Firas Kobeissy; Phat Tran; Abdul N. Hamood; Mohamed F. Hegazy; Paul W. Paré; Yehia Mechref

Multitargeted Flavonoid Inhibition of the Pathogenic Bacterium Staphylococcus aureus: A Proteomic Characterization

Wael Elmasri, Rui Zhu, Wenjing Peng, Moustafa Al-Hariri, Firas Kobeissy, Phat Tran, Abdul N. Hamood, Mohamed F. Hegazy, Paul W. Paré, Yehia Mechref

Chemistry and Biochemistry

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

Abstract

© 2017 American Chemical Society. Growth inhibition of the pathogen Staphylococcus aureus with currently available antibiotics is problematic in part due to bacterial biofilm protection. Although recently characterized natural products, including 3′,4′,5-trihydroxy-6,7-dimethoxy-flavone [1], 3′,4′,5,6,7-pentahydroxy-flavone [2] , and 5-hydroxy-4′,7-dimethoxy-flavone [3], exhibit both antibiotic and biofilm inhibitory activities, the mode of action of such hydroxylated flavonoids with respect to S. aureus inhibition is yet to be characterized. Enzymatic digestion and high-resolution MS analysis of differentially expressed proteins from S. aureus with and without exposure to antibiotic flavonoids (1-3) allowed for the characterization of global protein alterations induced by metabolite treatment. A total of 56, 92, and 110 proteins were differentially expressed with bacterial exposure to 1, 2, or 3, respectively. The connectivity of the identified proteins was characterized using a sear

Original language	English
Pages (from-to)	2579-2586
Journal	Journal of Proteome Research
State	Published - Jul 7 2017

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@article{6013456a473e4deca82dce3ae43af792,

title = "Multitargeted Flavonoid Inhibition of the Pathogenic Bacterium Staphylococcus aureus: A Proteomic Characterization",

abstract = "{\textcopyright} 2017 American Chemical Society. Growth inhibition of the pathogen Staphylococcus aureus with currently available antibiotics is problematic in part due to bacterial biofilm protection. Although recently characterized natural products, including 3′,4′,5-trihydroxy-6,7-dimethoxy-flavone [1], 3′,4′,5,6,7-pentahydroxy-flavone [2] , and 5-hydroxy-4′,7-dimethoxy-flavone [3], exhibit both antibiotic and biofilm inhibitory activities, the mode of action of such hydroxylated flavonoids with respect to S. aureus inhibition is yet to be characterized. Enzymatic digestion and high-resolution MS analysis of differentially expressed proteins from S. aureus with and without exposure to antibiotic flavonoids (1-3) allowed for the characterization of global protein alterations induced by metabolite treatment. A total of 56, 92, and 110 proteins were differentially expressed with bacterial exposure to 1, 2, or 3, respectively. The connectivity of the identified proteins was characterized using a sear",

author = "Wael Elmasri and Rui Zhu and Wenjing Peng and Moustafa Al-Hariri and Firas Kobeissy and Phat Tran and Hamood, {Abdul N.} and Hegazy, {Mohamed F.} and Par{\'e}, {Paul W.} and Yehia Mechref",

year = "2017",

month = jul,

day = "7",

language = "English",

pages = "2579--2586",

journal = "Journal of Proteome Research",

}

Multitargeted Flavonoid Inhibition of the Pathogenic Bacterium Staphylococcus aureus: A Proteomic Characterization. / Elmasri, Wael; Zhu, Rui; Peng, Wenjing; Al-Hariri, Moustafa; Kobeissy, Firas; Tran, Phat; Hamood, Abdul N.; Hegazy, Mohamed F.; Paré, Paul W.; Mechref, Yehia.

In: Journal of Proteome Research, 07.07.2017, p. 2579-2586.

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

TY - JOUR

T1 - Multitargeted Flavonoid Inhibition of the Pathogenic Bacterium Staphylococcus aureus: A Proteomic Characterization

AU - Elmasri, Wael

AU - Zhu, Rui

AU - Peng, Wenjing

AU - Al-Hariri, Moustafa

AU - Kobeissy, Firas

AU - Tran, Phat

AU - Hamood, Abdul N.

AU - Hegazy, Mohamed F.

AU - Paré, Paul W.

AU - Mechref, Yehia

PY - 2017/7/7

Y1 - 2017/7/7

N2 - © 2017 American Chemical Society. Growth inhibition of the pathogen Staphylococcus aureus with currently available antibiotics is problematic in part due to bacterial biofilm protection. Although recently characterized natural products, including 3′,4′,5-trihydroxy-6,7-dimethoxy-flavone [1], 3′,4′,5,6,7-pentahydroxy-flavone [2] , and 5-hydroxy-4′,7-dimethoxy-flavone [3], exhibit both antibiotic and biofilm inhibitory activities, the mode of action of such hydroxylated flavonoids with respect to S. aureus inhibition is yet to be characterized. Enzymatic digestion and high-resolution MS analysis of differentially expressed proteins from S. aureus with and without exposure to antibiotic flavonoids (1-3) allowed for the characterization of global protein alterations induced by metabolite treatment. A total of 56, 92, and 110 proteins were differentially expressed with bacterial exposure to 1, 2, or 3, respectively. The connectivity of the identified proteins was characterized using a sear

AB - © 2017 American Chemical Society. Growth inhibition of the pathogen Staphylococcus aureus with currently available antibiotics is problematic in part due to bacterial biofilm protection. Although recently characterized natural products, including 3′,4′,5-trihydroxy-6,7-dimethoxy-flavone [1], 3′,4′,5,6,7-pentahydroxy-flavone [2] , and 5-hydroxy-4′,7-dimethoxy-flavone [3], exhibit both antibiotic and biofilm inhibitory activities, the mode of action of such hydroxylated flavonoids with respect to S. aureus inhibition is yet to be characterized. Enzymatic digestion and high-resolution MS analysis of differentially expressed proteins from S. aureus with and without exposure to antibiotic flavonoids (1-3) allowed for the characterization of global protein alterations induced by metabolite treatment. A total of 56, 92, and 110 proteins were differentially expressed with bacterial exposure to 1, 2, or 3, respectively. The connectivity of the identified proteins was characterized using a sear

M3 - Article

SP - 2579

EP - 2586

JO - Journal of Proteome Research

JF - Journal of Proteome Research

ER -