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Label-free quantitative proteomic analysis of the inhibitory activities of juglone against translation and energy metabolism in Escherichia coli
Institution:1. Department of Urology, The University of Texas MD Anderson Cancer Center, Houston, TX;2. Department of Biostatistics, The University of Texas MD Anderson Cancer Center, Houston, TX;3. Department of Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX;4. Department of Genitourinary Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX;5. Department of Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX;6. Department of Acute and Continuing Care, University of Texas Health Cizik School of Nursing, Houston, TX;7. Affiliation change since completion of this work: Merck & Co., Inc., Kenilworth, NJ;1. Diabetes Division, St. Josef-Hospital, Ruhr-University Bochum, Gudrunstrasse 56, Bochum 44791, Germany;2. Department of Pathology, Ruhr-University Bochum, Bürkle de la Camp-Platz 1, Bochum 44789, Germany;3. Department of Surgery, Knappschaftskrankenhaus Bochum, Ruhr-University Bochum, In der Schornau 23-25, Bochum 44892, Germany;4. Department of Surgery, St. Josef-Hospital, Ruhr-University Bochum, Gudrunstrasse 56, Bochum 44791, Germany;5. Department of Medicine II, St. Vinzenz Hospital, Merheimer Str. 221-223, Cologne 50733, Germany
Abstract:Plant-derived antimicrobial agents have received increasing attention owing to their potential to control pathogens and excellent efficacy despite the growing prevalence of antibiotic resistance. However, the antibacterial mechanism of juglone, a traditional medicine used to cure skin infections, is still unclear. Therefore, in this study, in order to elucidate the mechanisms underlying the antibacterial activity of juglone, label-free quantitative proteomic technology was applied for analysis of the 417 proteins that were differentially expressed in Escherichia coli after treatment with juglone at one-half of the minimum inhibitory concentration. Gene ontology enrichment analysis of differentially expressed proteins suggested that juglone effectively repressed the expression of dehydrogenase and cytochrome oxidase, indicating that energy generation was blocked. Additionally, juglone induced RNA formation and ribosome assembly, resulting in inhibition of translation. This is the first study to adopt a proteomic approach to investigate the antibacterial mechanism of action of juglone against E. coli.
Keywords:Label-free quantitative proteomics  Juglone  Antibacterial mechanism of action
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