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Article

Potential Inhibitory Effect of Apis mellifera’s Venom and of Its Two Main Components—Melittin and PLA2—on Escherichia coli F1F0-ATPase

1
Bioactive Molecules Research Laboratory, Faculty of Sciences, Section II, Lebanese University, B.P. 90656, Jdeidet El-Matn 1202, Lebanon
2
Faculty of Agriculture & Veterinary Sciences, Lebanese University, Dekwaneh, Beirut 2832, Lebanon
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Institut de Neuro-Physiopathologie, Faculté de Médecine Secteur Nord 51, Université Aix-Marseille, UMR 7051, Boulevard Pierre Dramard-CS80011, 13344-Marseille CEDEX 15, France
4
Laboratoire de Biotechnologie Appliquée (LBA3B), Centre Azm pour la Recherche en Biotechnologie et ses Applications, EDST, Lebanese University, Tripoli 1300, Lebanon
5
Department of Biology, Faculty of Sciences, Section III, Lebanese University, Michel Slayman Tripoli Campus, Ras Maska 1352, Lebanon
*
Authors to whom correspondence should be addressed.
Antibiotics 2020, 9(11), 824; https://doi.org/10.3390/antibiotics9110824
Received: 3 November 2020 / Revised: 12 November 2020 / Accepted: 17 November 2020 / Published: 18 November 2020
(This article belongs to the Special Issue Peptide Antibiotics from Microbes and Venomous Animals)
Bacterial resistance has become a worrying problem for human health, especially since certain bacterial strains of Escherichia coli (E. coli) can cause very serious infections. Thus, the search for novel natural inhibitors with new bacterial targets would be crucial to overcome resistance to antibiotics. Here, we evaluate the inhibitory effects of Apis mellifera bee venom (BV-Am) and of its two main components -melittin and phospholipase A2 (PLA2)- on E. coli F1F0-ATPase enzyme, a crucial molecular target for the survival of these bacteria. Thus, we optimized a spectrophotometric method to evaluate the enzymatic activity by quantifying the released phosphate from ATP hydrolysis catalyzed by E. coli F1F0-ATPase. The protocol developed for inhibition assays of this enzyme was validated by two reference inhibitors, thymoquinone (IC50 = 57.5 μM) and quercetin (IC50 = 30 μM). Results showed that BV-Am has a dose-dependent inhibitory effect on E. coli F1F0-ATPase with 50% inhibition at 18.43 ± 0.92 μg/mL. Melittin inhibits this enzyme with IC50 = 9.03 ± 0.27 µM, emphasizing a more inhibitory effect than the two previous reference inhibitors adopted. Likewise, PLA2 inhibits E. coli F1F0-ATPase with a dose-dependent effect (50% inhibition at 2.11 ± 0.11 μg/mL) and its combination with melittin enhanced the inhibition extent of this enzyme. Crude venom and mainly melittin and PLA2, inhibit E. coli F1F0-ATPase and could be considered as important candidates for combating resistant bacteria. View Full-Text
Keywords: antibiotic resistance; F1F0-ATPase; Escherichia coli; Apis mellifera bee venom; inhibitory assays; antibacterial activity antibiotic resistance; F1F0-ATPase; Escherichia coli; Apis mellifera bee venom; inhibitory assays; antibacterial activity
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MDPI and ACS Style

Nehme, H.; Ayde, H.; El Obeid, D.; Sabatier, J.M.; Fajloun, Z. Potential Inhibitory Effect of Apis mellifera’s Venom and of Its Two Main Components—Melittin and PLA2—on Escherichia coli F1F0-ATPase. Antibiotics 2020, 9, 824. https://doi.org/10.3390/antibiotics9110824

AMA Style

Nehme H, Ayde H, El Obeid D, Sabatier JM, Fajloun Z. Potential Inhibitory Effect of Apis mellifera’s Venom and of Its Two Main Components—Melittin and PLA2—on Escherichia coli F1F0-ATPase. Antibiotics. 2020; 9(11):824. https://doi.org/10.3390/antibiotics9110824

Chicago/Turabian Style

Nehme, Hala, Helena Ayde, Dany El Obeid, Jean M. Sabatier, and Ziad Fajloun. 2020. "Potential Inhibitory Effect of Apis mellifera’s Venom and of Its Two Main Components—Melittin and PLA2—on Escherichia coli F1F0-ATPase" Antibiotics 9, no. 11: 824. https://doi.org/10.3390/antibiotics9110824

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