Thymoquinone Inhibits Escherichia coli ATP Synthase and Cell Growth

Ahmad, Zulfiqar; Laughlin, Thomas F.; Kady, Ismail O.

doi:10.1371/journal.pone.0127802

Cited by 38 publications

(47 citation statements)

References 55 publications

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“…Double mutants αI346R/βR182A, αI346R/αR376A, and αI348R/βR182A augmented the ATPase activity by about 70-fold from 0.07, 0.065 to 4.61, 4.97, and 4.87, respectively. Purity and integrity of α and β subunits in wild-type and mutant membrane bound F 1 F o were in excellent agreement with previously published data [8, 30]. This result also confirmed that the reduced ATPase in mutants was not due to contaminants, impaired assembly of ATP synthase, or loss of F 1 during membrane preparation, thus attributing the low mutant activities to mutant F 1 .…”

Section: Resultssupporting

confidence: 91%

“…In previous studies, both membrane bound F 1 F o and purified F 1 preparations provided equivalent assay results [5, 8, 9, 14, 15, 30, 32–35]. Therefore, all the inhibition assays in this study were carried out using membrane bound F 1 F o because it is convenient and less time consuming.…”

Section: Resultsmentioning

confidence: 99%

“…All reactions were found to be linear with respect to time and protein concentration. The purity of membrane bound F 1 F o was checked by SDS-gel electrophoresis on 10% acrylamide gels and by immunoblotting with rabbit polyclonal anti-F 1 -α and anti-F 1 -β antibodies as described previously [30] and shown in Fig 2.…”

Section: Methodsmentioning

confidence: 99%

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Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase

Zhao

Syed

Hassan

et al. 2016

Archives of Biochemistry and Biophysics

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We studied the functional role of highly conserved VISIT-DG sequence residues αIle-346 and αIle-348 in the catalytic sites of Escherichia coli F1Fo ATP synthase. αIle-346 is in close proximity, 2.98 and 3.63 Å, to the two known phosphate binding residues αR376 and βR182; αIle-348 is situated within 3.66 Å from βR182. Single or double mutants of both αI346 and αI348 resulted in a variable loss of oxidative phosphorylation and ATPase activity. Azide, fluoroaluminate, and fluoroscandium caused insignificant to significant inhibition of mutants. Whereas the wild-type enzyme was completely inhibited by NBD-Cl (7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole), a variable extent of inhibition was observed for αI346 and αI348 mutants. MgPi protection against NBD-Cl induced inhibition of wild-type, αI346, and αI348 demonstrated that, although strongly conserved, αI346 and αI348 have no direct role in phosphate binding. Insertion of Arginine in the form of αI346R/βR182A, αI346R/αR376A, or αI348R/βR182A was able to compensate for the absence of known phosphate-binding Arginine residues βR182 and αR376. Results also suggest that αIle-346 and αIle-348 seem to have functional importance in upholding the phosphate-binding subdomain and transition state stabilization in the catalytic sites of E. coli ATP synthase. Keywords

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

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Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase

Zhao

Syed

Hassan

et al. 2016

Archives of Biochemistry and Biophysics

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“…This cell wall structure-related effect may explain a higher antibacterial efficacy of our N. sativa seed oil extract on Gram positive bacteria than Gram negative bacteria. In addition, inhibition of cell wall synthesis gene expression was also reported to cell wall integrity, inhibition of ATP production and cell growth were as also reported due to the phenolic content of DLBS1355 45 . Facing the multi-drug resistant pathogenic bacteria, discovery and development of new antimicrobial agents have already become a global concern.…”

Section: Discussionmentioning

confidence: 70%

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2017

IJPSR

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Our previous study highlighted the antimicrobial activity evaluation of Nigella sativa seed oil extract that was obtained from supercritical fluid extraction using carbon dioxide (SCFE-CO 2 ) on Gram positive pathogenic bacteria. The aim of this study was to formulate oil-in-water (o/w) emulsion of previous N. sativa seed oil extract and to investigate its antimicrobial activity against Streptococcus mutans and Streptococcus sanguis as the most common causative bacteria of dental caries. Oil-in-water emulsion containing 10% N. sativa seed oil extract (DLBS1355) exhibited good inhibition activity on both S. mutans and S. sanguis. Time-kill assay and biofilm inhibition assay were conducted using emulsion with 0.5% N. sativa seed oil extract content. The results showed bactericidal and biofilm inhibition activities on both tested bacteria. Antimicrobial activity of the emulsion was found higher on S. sanguis than S. mutans. Results of the present study showed that emulsification process did not significantly affect the antimicrobial activity of N. sativa seed oil extract and the formulated N. sativa oil-in-water emulsion could further be used as an antimicrobial agent against dental cariogenic bacteria.

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“…Reactions were found to be linear with time and protein concentration. SDS-gel electrophoresis (10% acrylamide) and immunoblotting with rabbit polyclonal anti-F 1 -α and anti-F 1 -β antibodies was used to check the integrity and purity of protein [40]. …”

Section: Methodsmentioning

confidence: 99%

Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase

Azim

McDowell

Cartagena

et al. 2016

International Journal of Biological Macromolecules

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Venom peptides are known to have strong antimicrobial activity and anticancer properties. King cobra cathelicidin or OH-CATH (KF-34), banded krait cathelicidin (BF-30), wolf spider lycotoxin I (IL-25), and wolf spider lycotoxin II (KE-27) venom peptides were found to strongly inhibit E. coli membrane bound F1Fo ATP synthase. The potent inhibition of wild-type E. coli in comparison to the partial inhibition of null E. coli by KF-34, BF-30, Il-25, or KE-27 clearly links the bactericidal properties of these venom peptides to the binding and inhibition of ATP synthase along with the possibility of other inhibitory targets. The four venom peptides KF-34, BF-30, IL-25, and KE-27, caused ≥85% inhibition of wild-type membrane bound E.coli ATP synthase. Venom peptide induced inhibition of ATP synthase and the strong abrogation of wild-type E. coli cell growth in the presence of venom peptides demonstrates that ATP synthase is a potent membrane bound molecular target for venom peptides. Furthermore, the process of inhibition was found to be fully reversible.

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Thymoquinone Inhibits Escherichia coli ATP Synthase and Cell Growth

Cited by 38 publications

References 55 publications

Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase

Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase

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Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase

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