Potentiating activity of luteolin on membrane permeabilizing agent and ATPase inhibitor against methicillin-resistant Staphylococcus aureus
10.1016/j.apjtm.2015.12.004
- Author:
Su-Hyun MUN
1
;
Ryong KONG
1
;
Ho-Jun SONG
1
;
Dong-Yeul KWON
1
;
Young-Seob LEE
2
;
Sin-Hee HAN
2
;
Sang-Won LEE
2
;
Seon-Woo CHA
2
;
Dae-Ki JOUNG
3
;
Ok-Hwa KANG
3
;
Dong-Yeul KWON
3
;
Dong-Won SHIN
4
Author Information
1. BK21 Plus Team, Professional Graduate School of Oriental Medicine, Wonkwang University
2. Department of Herbal Crop Research, National Institute of Horticultural and Herbal Science, RDA
3. Department of Oriental Pharmacy, College of Pharmacy and Wonkwang-Oriental Medicines Research Institute, Wonkwang University
4. Department of Oriental Medicine Resources, Sunchon National University
- Publication Type:Journal Article
- Keywords:
ATPase inhibitor;
Luteolin;
Membrane permeabilizing agent;
Methicillin-resistant Staphylococcus aureus;
Peptidoglycan
- From:
Asian Pacific Journal of Tropical Medicine
2016;9(1):19-22
- CountryChina
- Language:Chinese
-
Abstract:
Objective: To investigate the mechanism of antibacterial activity of luteolin (LUT) against methicillin-resistant Staphylococcus aureus (MRSA). Methods: The mechanism of anti-MRSA activity of LUT was analyzed by the viability assay in membrane permeabilizing agent, ATPase inhibitors, and peptidoglycan (PGN) derived from Staphylococcus aureus (S. aureus). Also, transmission electron microscopy was used to monitor survival characteristics and changes in S. aureus morphology. Results: Compared to the LUT alone, the optical density of suspensions treated with the combination of 125 μg/mL Tris and 250 μg/mL N,N'-dicyclohexylcarbodiimide were reduced to 60% and 46% of the control, respectively. PGN (15.6 μg/mL) gradually impeded the activity of LUT, and PGN (62.5 μg/mL) completely blocked the activity of LUT on S. aureus. Conclusions: Increased susceptibility to LUT with the Tris-dicyclohexylcarbodiimide combinations is evident in all tested MRSA isolates. The results indicate LUT synergy in increasing cytoplasmic membrane permeability and inhibiting ATPase. S. aureus PGN directly blocks the antibacterial activity of LUT, suggesting the direct binding of LUT with PGN. These findings may be validated for the development of antibacterial agent for low MRSA resistance.
