Abstract
Listeria phage endolysin cell wall-binding domain (CBD) from the Listeria phage A500 was fused with flagellar subunit FliC in Escherichia coli, aiming at binding of E. coli cells to Listeria cells, followed by enhanced killing of Listeria by pediocin production. FliC::CBD chimeric flagella were expressed and detected by Western blot. However, only few chimeric flagella could be isolated from the recombinant cells compared with sufficient amount of wild-type flagella obtained from the host cells. Interestingly, wild-type flagella extract showed capacity of binding Listeria cells. Pediocin-secreting E. coli cells with Listeria-binding flagella killed approximately 40 % of the Listeria cells, whereas cell-free spent growth medium with the same pediocin concentration only inhibited Listeria growth. These results suggested that binding the Listeria to bacteriocin-secreting cells improves killing.
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References
Gálvez A, Abriouel H, López RL, Omar NB (2007) Bacteriocin-based strategies for food biopreservation. Int J Food Microbiol 120:51–70
Gandhi M, Chikindas ML (2007) Listeria: a foodborne pathogen that knows how to survive. Int J Food Microbiol 113(1):1–15
García P, Rodríguez L, Rodríguez A, Martínez B (2010) Food biopreservation: promising strategies using bacteriocins, bacteriophages and endolysins. Trends Food Sci Technol 21(8):373–382
Li R, Takala TM, Qiao M, Xu H, Saris PEJ (2011) Nisin-selectable food-grade secretion vector for Lactococcus lactis. Biotechnol Lett 33(4):797–803
Liu S (2014) Enhanced antibacterial action of bacteriocin producing cells by binding to the target pathogen. PhD thesis, University of Helsinki. Hansaprint, Helsinki, Dissertiones Biocentri Viikki Universitatis Helsingiensis 25:1–57
Loessner MJ, Schneider A, Scherer S (1996) Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins. Appl Environ Microbiol 62(8):3057–3060
Loessner MJ, Kramer K, Ebel F, Scherer S (2002) C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol Microbiol 44(2):335–349
Lohans CT, Vederas JC (2012) Development of class IIa bacteriocins as therapeutic agents. Int J Microbiol. doi:10.1155/2012/386410
Majander K, Anton L, Antikainen J, Lång H, Brummer M, Korhonen TK, Westerlund-Wikström B (2005) Extracellular secretion of polypeptides using a modified Escherichia coli flagellar secretion apparatus. Nat Biotechnol 23(4):475–481
Papagianni M, Anastasiadou S (2009) Pediocin: the bacteriocins of pediococci, sources, production, properties and applications. Microb Cell Fact 8:3
Westerlund-Wikström B, Tanskanen J, Virkola R, Hacker J, Lindberg M, Skurnik M, Korhonen TK (1997) Functional expression of adhesive peptides as fusions to Escherichia coli flagellin. Protein Eng 10(11):1319–1326
Acknowledgment
This work was supported by China Scholarship Council, the University of Helsinki, Finland, and the Academy of Finland (project number 177321). Professor Martin Loessner is acknowledged for the kind gift of the Listeria strain and the CBD500 encoding DNA.
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Liu, S., Takala, T.M., Reunanen, J. et al. Attachment of Escherichia coli to Listeria monocytogenes for Pediocin-Mediated Killing. Curr Microbiol 70, 195–198 (2015). https://doi.org/10.1007/s00284-014-0703-8
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DOI: https://doi.org/10.1007/s00284-014-0703-8