Abstract
This review attempts to analyze the mechanism of action and immunity of class IIa bacteriocins. These peptides are promising alternative food preservatives and they have a great potential application in medical sciences. Class IIa bacteriocins act on the cytoplasmic membrane of Gram-positive cells dissipating the transmembrane electrical potential by forming pores. However, their toxicity and immunity mechanism remains elusive. Here we discuss the role of the mannose phosphotransferase system (man-PTS) as the receptor for class IIa bacteriocins and the influence of the membrane composition on the activity of these antimicrobial peptides. A model that is consistent with experimental results obtained by different researchers involves the non-specific binding of the bacteriocin to the negatively charged membrane of target bacteria. This step would facilitate a specific binding to the receptor protein, altering its functionality and forming an independent pore in which the bacteriocin is inserted in the membrane. An immunity protein could specifically recognize and block the pore. Bacteriocins function in bacterial ecosystems and energetic costs associated with their production are also discussed. Theoretical models based on solid experimental evidence are vital to understand bacteriocins mechanism of action and to promote new technological developments.
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Acknowledgements
Financial support was provided by Consejo Nacional de Investigaciones Científicas y Técnicas PIP 0779, PIP 0530 and PIP 0906, Agencia Nacional de Promoción Científica y Tecnológica PICT-2012-2998 and PIUNT D548/1 from Universidad Nacional de Tucumán (UNT). N.S.R.C and S.A.N. are recipients of CONICET fellowship. M.C.C. and A.B are career investigators of CONICET.
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Communicated by M. Kupiec.
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Ríos Colombo, N.S., Chalón, M.C., Navarro, S.A. et al. Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity. Curr Genet 64, 345–351 (2018). https://doi.org/10.1007/s00294-017-0757-9
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DOI: https://doi.org/10.1007/s00294-017-0757-9