Effects of Polycephalomyces nipponicus extract on protein profiles of methicillin-Resistant Staphylococcus aureus
Keywords:
Methicillin Resistant Staphylococcus aureus, Polycephalomyces nipponicus, proteomesAbstract
Abstract
The entomopathogenic fungus Polycephalomyces nipponicus has been reported to have both antibacterial and antimalarial activities. Previous studies have shown that the crude mycelial extract is active against several Gram-negative and Gram-positive bacteria, including methicillin-resistant Staphylococcus aureus (MRSA). However, the mechanism underlying this antibacterial activity has yet to be elucidated. This study sought to determine which bacterial metabolic pathways or proteins P. nipponicus might be targeting by examining the in vitro effects of crude mycelial extract on MRSA using a gel-based proteomic approach. The MRSA strains DMST 20651 and DMST 20654 were treated with a sub-inhibitory concentration of P. nipponicus Cod-MK1201 mycelium extract (1.5 mg/ml or 0.5 MIC) for 18 hours. The protein extracts were then obtained from the MRSA cells by sonication, and the proteins were separated by 2D polyacrylamide gels. After this, the protein expression profiles of untreated control and extract-treated cells were analyzed by Image Master 2D platinum software for any significant differences. Protein spots of interest were extracted from the gels and identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). A total of 22 protein spots that were significantly changed in protein expression with a greater than 1.5-fold increase or decrease relative to the control cells were identified. The analysis of the protein profiles showed a general decrease in the expression of proteins related to carbohydrate metabolism and energy production in both strain DMST 20651 and strain DMST 20654. The proteins related to translation were also present at lower levels in both strains, while the expression of stress response proteins was increased. It was postulated that P. nipponicus mycelial extract exerted its antibacterial effects by disrupting energy metabolism and/or translation.
References
Klevens RM, Morrison MA, Nadle J, et al. Invasivemethicillin - resistant Staphylococcus aureus infections in the United States. JAMA 2007;298:1763-71.
Chang S, Sievert DM, Hageman JC, et al. Infection with vancomycin-resistant Staphylococcus aureus containing the vanA resistance gene. N Engl J Med 2003;348:1342-7.
Hiramatsu K. Vancomycin-resistant Staphylococcus aureus: A new model of antibiotic resistance. Lancet Infect Dis 2001;1:147-55.
Yue K, Ye M, Zhou Z, et al. The genus Cordyceps: a chemical and pharmacological review: A review of Cordyceps. J Pharm Pharmacol 2013;65:474-93.
Tuli HS, Sharma AK, Sandhu SS, et al. Cordycepin: a bioactive metabolite with therapeutic potential. Life Sci 2013;93:863-9.
Yeon SH, Kim A, Y J. Comparison of growthinhibiting activities of Cordyceps militaris and Paecilomyces japonica cultured on Bombyx mori pupae towards human gastrointestinal bacteria. J Sci Food Agric 2007;87:54-9.
Xiao JH, Xiao DM, Sun ZH, et al. Chemical compositions and antimicrobial property of three edible and medicinal Cordyceps species. J Food Agric Environ 2009;7:91-100.
Imtiaj A, Lee TS. Screening of antibacterial and antifungal activities from Korean wild mushrooms. WJAS 2007;3:316-21.
Sangdee K, Nakbanpote W, Sangdee A. Isolation of the entomopathogenic fungal strain Cod-MK1201 from a cicada nymph and assessment of its antibacterial activities. Int J Med Mushrooms 2015;17:51-63.
Yu X, Zheng L, Yang J, et al. Characterization of essential enolase in Staphylococcus aureus. World J Microbiol Biotechnol 2011;27:897-905.
Sianglum W, Srimanote P, WonglumsomW, et al. Proteome analyses of cellular proteins in methicillin-resistant Staphylococcus aureus treated with rhodomyrtone, a novel antibiotic candidate. PLoS One 2011;6:e16628.
Lin X, Kang L, Li H, et al. Fluctuation of multiple metabolic pathways is required for Escherichia coli in response to chlortetracycline stress. Mol Biosyst 2014;10:901-8.
Stefanopoulou M, Kokoschka M, Sheldrick WS, et al. Cell response of Escherichia coli to cisplatin-induced stress. Proteomics 2011;11:4174-88.
Cui H, Zhang C, Li C, et al. Antimicrobial mechanism of clove oil on Listeria monocytogenes. Food Control 2018;94:140-6.
Myasnikov AG, Simonetti A, Marzi S, et al. Structure-function insights into prokaryotic and eukaryotic translation initiation. Curr Opin Struct Biol 2009;19:300-9.
Moll I, Grill S, A. G, et al. Effects of ribosomal proteins S1, S2 and the DeaD/CsdA DEADbox helicase on translation of leaderless and canonical mRNAs in Escherichia coli. Mol Microbiol 2002;44:1387-96.
Palmer SO, Rangel EY, Montalvo AE, et al.Cloning and characterization of EF-Tu and EF-Ts from Pseudomonas aeruginosa. Biomed Res Int 2013;2013:585748.
Wang J, Wang Z, Wu R, et al. Proteomic analysis of the antibacterial mechanism of action of juglone againstStaphylococcus aureus. Nat Prod Commun 2016;11:825-7.
Wong FC, Yong AL, Sim KM, et al. Proteomic analysis of bacterial expression profiles following exposure to organic solvent flower extract of Melastoma candidum D Don (Melastomataceae). Trop J Pharm Res 2014;13:1085-92.
Hedstrom L, Liechti G, Goldberg JB, et al. The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors. Curr Med Chem 2011;18:1909-18.
Turner AK, Barber LZ, Wigley P, et al. Contribution of proton-translocating proteins to the virulence of Salmonella enterica serovars Typhimurium, Gallinarum, and Dublin in chickens and mice. Infect Immun 2003;71:3392-401.
Ng TB, Wang HX. Pharmacological actions of Cordyceps, a prized folk medicine. J Pharm Pharmacol 2005;57:1509-19.
Sangdee A, Sangdee K, Seephonkai P, et al. Colony characteristics, nucleoside analog profiles, and genetic variations of medicinal fungus Polycephalomyces nipponicus (ascomycetes) isolates from northeast Thailand. Int J Med Mushrooms 2017;19:445-55.
Haslbeck M. sHsps and their role in the chaperone network. Cell Mol Life Sci 2002;59:1649-57.
Tadtong S. Heat Shock Protein 90: Target for Cancer Therapy. Thai Pharm Health Sci 2009;4.
Abdallah J, Mihoub M, Gautier V, et al. The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal. Biochem Biophys Res Commun 2016;470:282-6.
Ralser M, Wamelink MM, Kowald A, et al. Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress. J Biol 2007;6:10.
Huang G, Li C, Cao Y. Proteomic analysis of differentially expressed proteins in Lactobacillus brevis NCL912 under acid stress: Differentially expressed proteins under acid stress. FEMS Microbiol Lett 2011;318:177-82.
Zhai Z, Douillard FP, An H, et al. Proteomic characterization of the acid tolerance response in Lactobacillus delbrueckii subsp. bulgaricus CAUH1 and functional identification of a novel acid stress-related transcriptional regulator Ldb0677. Environ Microbiol 2014;16:1524-37.
Len ACL, Harty DWS, Jacques NA. Proteome analysis of Streptococcus mutans metabolic phenotype during acid tolerance. Microbiology 2004;150:1353-66.
Budin-Verneuil A, Pichereau V, Auffray Y, et al. Proteomic characterization of the acid tolerance response in Lactococcus lactis MG1363. Proteomics 2005;5:4794-807.
Nishiyama Y, Massey V, Takeda K, et al. Hydrogen peroxide-forming NADH oxidase belonging to the peroxiredoxin oxidoreductase family: existence and physiological role in bacteria. J Bacteriol 2001;183:2431-8.
Seib KL, Wu H-J, Kidd SP, et al. Defenses against oxidative stress in Neisseria gonorrhoeae: a system tailored for a challenging environment. Microbiol Mol Biol Rev 2006;70:344-61.
Hussain RM, Razak ZNRA, Saad WMM, et al. Mechanism of antagonistic effects of Andrographis paniculata methanolic extract against Staphylococcus aureus. Asian Pac J Trop Med 2017;10:685-95.
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