Mechanism of Action of Recombinant Acc-Royalisin from RoyalJelly of Asian Honeybee against Gram-Positive BacteriaPLoS ONE, 7(10): e47194The antibacterial activity of royalisin, an antimicrobialpeptide from the royal jelly produced by honeybees, has been addressedextensively. However, its mechanism of action remains unclear. In this study, a recombinant royalisin, RAcc-royalisin fromthe royal jelly of Asian honeybee Apis cerana cerana, was expressed by fusingwith glutathione S-transferase (GST) in Escherichia coli BL21, isolated andpurified. The agar dilution assays with inhibition zone showed thatRAcc-royalisin, similar to nisin, inhibits the growth of Gram-positivebacteria. The antibacterial activity of RAcc-royalisin was associatedwith its concentration, and was weakened by heat treatment ranging from 55°C to85°C for 15 min. Both RAcc-royalisin and nisin exhibited the minimum inhibitoryconcentrations (MIC) of 62.5 µg/ml, 125 µg/ml, and 250 µg/ml againstGram-positive bacterial strains, Bacillus subtilis and Micrococcus flavus andStaphyloccocus aureus in the microplate assay, respectively. However,RAcc-royalisin did not show antimicrobial activity against tested Gram-negativebacterial and fungal strains. The antibacterial activity of RAcc-royalisinagrees well with the decrease in bacterial cell hydrophobicity, the leakage of260-nm absorbing materials, and the observation by transmission electronmicroscopy, all indicating that RAcc-royalisin induced the disruption anddysfunction of cell walls and membranes. This is the first report detailing the antibacterialmechanism of royalisin against Gram-positive bacteria, and provides insightinto the application of recombinant royalisin in food and pharmaceuticalindustries as an antimicrobial agent.
13 Ekim 2012 Cumartesi
First Report of Royal Jelly Peptide’s Antibacterial Mechanism Against Gram-Positive Bacteria
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Mechanism of Action of Recombinant Acc-Royalisin from RoyalJelly of Asian Honeybee against Gram-Positive BacteriaPLoS ONE, 7(10): e47194The antibacterial activity of royalisin, an antimicrobialpeptide from the royal jelly produced by honeybees, has been addressedextensively. However, its mechanism of action remains unclear. In this study, a recombinant royalisin, RAcc-royalisin fromthe royal jelly of Asian honeybee Apis cerana cerana, was expressed by fusingwith glutathione S-transferase (GST) in Escherichia coli BL21, isolated andpurified. The agar dilution assays with inhibition zone showed thatRAcc-royalisin, similar to nisin, inhibits the growth of Gram-positivebacteria. The antibacterial activity of RAcc-royalisin was associatedwith its concentration, and was weakened by heat treatment ranging from 55°C to85°C for 15 min. Both RAcc-royalisin and nisin exhibited the minimum inhibitoryconcentrations (MIC) of 62.5 µg/ml, 125 µg/ml, and 250 µg/ml againstGram-positive bacterial strains, Bacillus subtilis and Micrococcus flavus andStaphyloccocus aureus in the microplate assay, respectively. However,RAcc-royalisin did not show antimicrobial activity against tested Gram-negativebacterial and fungal strains. The antibacterial activity of RAcc-royalisinagrees well with the decrease in bacterial cell hydrophobicity, the leakage of260-nm absorbing materials, and the observation by transmission electronmicroscopy, all indicating that RAcc-royalisin induced the disruption anddysfunction of cell walls and membranes. This is the first report detailing the antibacterialmechanism of royalisin against Gram-positive bacteria, and provides insightinto the application of recombinant royalisin in food and pharmaceuticalindustries as an antimicrobial agent.
Mechanism of Action of Recombinant Acc-Royalisin from RoyalJelly of Asian Honeybee against Gram-Positive BacteriaPLoS ONE, 7(10): e47194The antibacterial activity of royalisin, an antimicrobialpeptide from the royal jelly produced by honeybees, has been addressedextensively. However, its mechanism of action remains unclear. In this study, a recombinant royalisin, RAcc-royalisin fromthe royal jelly of Asian honeybee Apis cerana cerana, was expressed by fusingwith glutathione S-transferase (GST) in Escherichia coli BL21, isolated andpurified. The agar dilution assays with inhibition zone showed thatRAcc-royalisin, similar to nisin, inhibits the growth of Gram-positivebacteria. The antibacterial activity of RAcc-royalisin was associatedwith its concentration, and was weakened by heat treatment ranging from 55°C to85°C for 15 min. Both RAcc-royalisin and nisin exhibited the minimum inhibitoryconcentrations (MIC) of 62.5 µg/ml, 125 µg/ml, and 250 µg/ml againstGram-positive bacterial strains, Bacillus subtilis and Micrococcus flavus andStaphyloccocus aureus in the microplate assay, respectively. However,RAcc-royalisin did not show antimicrobial activity against tested Gram-negativebacterial and fungal strains. The antibacterial activity of RAcc-royalisinagrees well with the decrease in bacterial cell hydrophobicity, the leakage of260-nm absorbing materials, and the observation by transmission electronmicroscopy, all indicating that RAcc-royalisin induced the disruption anddysfunction of cell walls and membranes. This is the first report detailing the antibacterialmechanism of royalisin against Gram-positive bacteria, and provides insightinto the application of recombinant royalisin in food and pharmaceuticalindustries as an antimicrobial agent.
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