Evaluation of antibacterial activity of enterocin A-colicin E1 fusion peptide | ||
| Iranian Journal of Basic Medical Sciences | ||
| مقاله 14، دوره 23، شماره 11، بهمن 2020، صفحه 1471-1479 اصل مقاله (961.48 K) | ||
| نوع مقاله: Original Article | ||
| شناسه دیجیتال (DOI): 10.22038/ijbms.2020.47826.11004 | ||
| نویسندگان | ||
| Hadis Fathizadeh1؛ Mahmood Saffari1؛ Davoud Esmaeili* 2، 3؛ Rezvan Moniri1، 4؛ Morteza Salimian4 | ||
| 1Department of Microbiology and Immunology, Faculty of Medicine, Kashan University of Medical Sciences, Kashan, Iran | ||
| 2Department of Microbiology and Applied Microbiology Research Center, Systems Biology and Poisonings Institute, Baqiyatallah University of Medical Sciences, Tehran, Iran | ||
| 3Applied Virology Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran | ||
| 4Anatomical Science Research Center, Kashan University of Medical Sciences, Kashan, Iran | ||
| چکیده | ||
| Objective(s): Bacterial resistance to most common antibiotics is a harbinger of the requirement to find novel anti-infective, antimicrobials agents, and increase innovative strategies to struggle them. Numerous bacteria produce small peptides with antimicrobial activities called bacteriocin. This study aimed to investigate the antibacterial properties of the fusion protein of Enterocin A and Colicin E1 modified against pathogens. Materials and Methods: Analysis of recombinant bacteriocin Enterocin A and Colicin E1 (ent A-col E1) was performed to assay the stability and antibacterial activity of this fusion protein. The pET-22b vector was employed to express the coding sequence of the ent A-col E1 peptide in Escherichia coli BL21 (DE3). Minimum inhibitory concentration (MIC), disk diffusion, and time-kill tests were performed to evaluate the antibacterial activity of the ent A-col E1 against Pseudomonas aeruginosa (ATCC 9027), Escherichia coli (ATCC 10536), Enterococcus faecalis (ATCC 29212), and Staphylococcus aureus (ATCC 33591). Results: The suggested recombinant peptide had good antibacterial activity against both Gram-negative and Gram-positive pathogens. It has also good stability at various temperatures, pH levels, and salt concentrations. Conclusion: Because bacteriocins are harmless compounds, they can be recommended as therapeutic or preventive supplements to control pathogens. According to the obtained results, the ent A-col E1 peptide can serve as an efficient antibacterial compound to treat or prevent bacterial infections. | ||
| کلیدواژهها | ||
| Antibacterial activity؛ Bacteriocins؛ Colicin E1؛ Enterocin A؛ Fusion peptide | ||
| مراجع | ||
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1. Pogue JM, Kaye KS, Cohen DA, Marchaim D. Appropriate antimicrobial therapy in the era of multidrug-resistant human pathogens. Clin Microbiol Infect 2015; 21:302-312. 2. Magiorakos AP, Srinivasan A, Carey RB, Carmeli Y, Falagas ME, Giske CG, et al. Multidrug-resistant, extensively drug-resistant and pan drug-resistant bacteria: an international expert proposal for interim standard definitions for acquired resistance. Clin Microbiol Infect 2012; 18:268-281. 3. Lebel G, Piche F, Frenette M, Gottschalk M, Grenier D. Antimicrobial activity of nisin against the swine pathogen Streptococcus suis and its synergistic interaction with antibiotics. Peptides 2013; 50:19-23. 4. Satish Kumar R, Kanmani P, Yuvaraj N, Paari KA, Pattukumar V, Arul V. Purification and characterization of enterocin MC13 produced by a potential aquaculture probiont Enterococcus faecium MC13 isolated from the gut of Mugil cephalus. Can J Microbiol 2011; 57:993-1001. 5. Hassan M, Kjos M, Nes IF, Diep DB, Lotfipour F. Natural antimicrobial peptides from bacteria: characteristics and potential applications to fight against antibiotic resistance. J Appl Microbiol 2012; 113:723-736. 6. Park SC, Park Y, Hahm KS. The role of antimicrobial peptides in preventing multidrug-resistant bacterial infections and biofilm formation. Int J Mol Sci 2011; 12:5971-5992. 7. Konings WN, Kok J, Kuipers OP, Poolman B. Lactic acid bacteria: the bugs of the new millennium. Curr Opin Microbiol 2000; 3:276-282. 8. Franz CM, Stiles ME, Schleifer KH, Holzapfel WH. Enterococci in foods--a conundrum for food safety. Int J Food Microbiol 2003; 88:105-122. 9. Line JE, Svetoch EA, Eruslanov BV, Perelygin VV, Mitsevich EV, Mitsevich IP, et al. Isolation and purification of enterocin E-760 with broad antimicrobial activity against Gram-positive and Gram-negative bacteria. Antimicrob Agents Chemother 2008; 52:1094-1100. 10. Ankaiah D, Esakkiraj P, Perumal V, Ayyanna R, Venkatesan A. Probiotic characterization of Enterococcus faecium por1: Cloning, overexpression of enterocin-A and evaluation of antibacterial, anti-cancer properties. J Func Foods 2017; 38:280-292. 11. Casaus P, Nilsen T, Cintas LM, Nes IF, Hernandez PE, Holo H. Enterocin B, a new bacteriocin from Enterococcus faecium T136 which can act synergistically with enterocin A. Microbiology 1997; 143:2287-2294. 12. Martin M, Gutierrez J, Criado R, Herranz C, Cintas LM, Hernandez PE. Cloning, production, and expression of the bacteriocin enterocin A produced by Enterococcus faecium PLBC21 in Lactococcus lactis. Appl Microbiol Biotechnol 2007; 76:667-675. 13. Gutierrez J, Larsen R, Cintas LM, Kok J, Hernandez PE. High-level heterologous production and functional expression of the sec-dependent enterocin P from Enterococcus faecium P13 in Lactococcus lactis. Appl Microbiol Biotechnol 2006; 72:41-51. 14. Cascales E, Buchanan SK, Duche D, Kleanthous C, Lloubes R, Postle K, et al. Colicin biology. Microbiol Mol Biol Rev 2007; 71:158-229. 15. Smajs D, Weinstock GM. Genetic organization of plasmid ColJs, encoding colicin Js activity, immunity, and release genes. J Bacteriol 2001; 183:3949-3957. 16. Cao Z, Klebba PE. Mechanisms of colicin binding and transport through outer membrane porins. Biochimie 2002; 84:399-412. 17. Mayville P, Ji G, Beavis R, Yang H, Goger M, Novick RP, et al. Structure-activity analysis of synthetic autoinducing thiolactone peptides from Staphylococcus aureus responsible for virulence. Proc Natl Acad Sci U S A 1999; 96:1218-1223. 18. Ji G, Beavis RC, Novick RP. Cell density control of staphylococcal virulence mediated by an octapeptide pheromone. Proc Natl Acad Sci U S A 1995; 92:12055-12059. 19. Field D, Begley M, O’Connor PM, Daly KM, Hugenholtz F, Cotter PD, et al. Bioengineered nisin A derivatives with enhanced activity against both Gram-positive and Gram-negative pathogens. PLoS One 2012; 7:e46884. 20. Ankaiah D, Palanichamy E, Antonyraj CB, Ayyanna R, Perumal V, Ahamed SIB, et al. Cloning, overexpression, purification of bacteriocin enterocin-B and structural analysis, interaction determination of enterocin-A, B against pathogenic bacteria and human cancer cells. Int J Biol Macromol 2018; 116:502-512. 21. Tanhaeian A, Damavandi MS, Mansury D, Ghaznini K. Expression in eukaryotic cells and purification of synthetic gene encoding enterocin P: a bacteriocin with broad antimicrobial spectrum. AMB Express 2019; 9:6. 22. Asadi KM, Oloomi M, Habibi M, Bouzari S. Cloning of fimH and fliC and expression of the fusion protein FimH/FliC from Uropathogenic Escherichia coli (UPEC) isolated in Iran. Iran J Microbiol 2012; 4:55-62. 23. Choubini E, Habibi M, Khorshidi A, Ghasemi A, Asadi Karam MR, Bouzari S. A novel multi-peptide subunit vaccine admixed with AddaVax adjuvant produces significant immunogenicity and protection against Proteus mirabilis urinary tract infection in mice model. Mol Immunol 2018; 96:88-97. 24. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-254. 25. Kusuma CM, Kokai-Kun JF. Comparison of four methods for determining lysostaphin susceptibility of various strains of Staphylococcus aureus. Antimicrob Agents Chemother 2005; 49:3256-3263. 26. Hemaiswarya S, Doble M. Synergistic interaction of phenylpropanoids with antibiotics against bacteria. J Med Microbiol 2010; 59:1469-1476. 27. CLSI C. Performance standards for antimicrobial susceptibility testing. Clinical Lab Standards Institute 2016. 28. Tiwari SK, Sutyak Noll K, Cavera VL, Chikindas ML. Improved antimicrobial activities of synthetic-hybrid bacteriocins designed from enterocin E50-52 and pediocin PA-1. Appl Environ Microbiol 2015; 81:1661-1667. 29. Klaenhammer TR. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol Rev 1993; 12:39-85. 30. Balla E, Dicks LM, Du Toit M, Van Der Merwe MJ, Holzapfel WH. Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071. Appl Environ Microbiol 2000; 66:1298-1304. 31. Franz CM, van Belkum MJ, Holzapfel WH, Abriouel H, Galvez A. Diversity of enterococcal bacteriocins and their grouping in a new classification scheme. FEMS Microbiol Rev 2007; 31:293-310. 32. Gutierrez J, Criado R, Martin M, Herranz C, Cintas LM, Hernandez PE. Production of enterocin P, an antilisterial pediocin-like bacteriocin from Enterococcus faecium P13, in Pichia pastoris. Antimicrob Agents Chemother 2005; 49:3004-3008. 33. Basanta A, Gomez-Sala B, Sanchez J, Diep DB, Herranz C, Hernandez PE, et al. Use of the yeast Pichia pastoris as an expression host for the secretion of enterocin L50, a leaderless two-peptide (L50A and L50B) bacteriocin from Enterococcus faecium L50. Appl Environ Microbiol 2010; 76:3314-3324. 34. Yoon SH, Kim SK, Kim JF. Secretory production of recombinant proteins in Escherichia coli. Recent Pat Biotechnol 2010; 4:23-29. 35. Berkmen M. Production of disulfide-bonded proteins in Escherichia coli. Protein Expr Purif 2012; 82:240-251. 36. De Kwaadsteniet M, Todorov SD, Knoetze H, Dicks LM. Characterization of a 3944 Da bacteriocin, produced by Enterococcus mundtii ST15, with activity against Gram-positive and Gram-negative bacteria. Int J Food Microbiol 2005; 105:433-444. 37. Drider D, Fimland G, Hechard Y, McMullen LM, Prevost H. The continuing story of class IIa bacteriocins. Microbiol Mol Biol Rev 2006; 70:564-582. 38. Padilla C, Lobos O, Brevis P, Abaca P, Hubert E. Plasmid-mediated bacteriocin production by Shigella flexneri isolated from dysenteric diarrhea and their transformation into Escherichia coli. Lett Appl Microbiol 2006; 42:300-303. 39. Cramer WA, Heymann JB, Schendel SL, Deriy BN, Cohen FS, Elkins PA, et al. Structure-function of the channel-forming colicins. Annu Rev Biophys Biomol Struct 1995; 24:611-641. 40. Pugsley AP. The ins and outs of colicins. Part II. Lethal action, immunity, and ecological implications. Microbiol Sci 1984; 1:203-205. 41. Breukink E, de Kruijff B. Lipid II as a target for antibiotics. Nat Rev Drug Discov 2006; 5:321-332. 42. Pag U, Sahl HG. Multiple activities in lantibiotics-models for the design of novel antibiotics? Curr Pharm Des 2002; 8:815-833. 43. Beric T, Stankovic S, Draganic V, Kojic M, Lozo J, Fira D. Novel antilisterial bacteriocin licheniocin 50.2 from Bacillus licheniformis VPS50.2 isolated from the soil sample. J Appl Microbiol 2014; 116:502-510. 44. Yeung AT, Gellatly SL, Hancock RE. Multifunctional cationic host defense peptides and their clinical applications. Cell Mol Life Sci 2011; 68:2161-2176. 45. Chu HL, Yu HY, Yip BS, Chih YH, Liang CW, Cheng HT, et al. Boosting salt resistance of short antimicrobial peptides. Antimicrob Agents Chemother 2013; 57:4050-4052. 46. Cantisani M, Finamore E, Mignogna E, Falanga A, Nicoletti GF, Pedone C, et al. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. Antimicrob Agents Chemother 2014; 58:5280-5290. 47. Delves-Broughton J, Blackburn P, Evans RJ, Hugenholtz J. Applications of the bacteriocin, nisin. Antonie Van Leeuwenhoek 1996; 69:193-202. | ||
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