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Please use this identifier to cite or link to this item: http://hdl.handle.net/11019/1522

Title: Insights into the Mode of Action of the Sactibiotic Thuricin CD
Authors: Mathur, Harsh
Fallico, Vicenzo
O'Connor, Paula M.
Rea, Mary C.
Cotter, Paul D.
Hill, Colin
Ross, R. Paul
Keywords: Sactibiotic bacteriocins
Thuricin CD
Mode of Action
Bacillus firmus DPC6349
Lytic activity
Issue Date: 20-Apr-2017
Publisher: Frontiers
Citation: Mathur H, Fallico V, O’Connor PM, Rea MC, Cotter PD, Hill C and Ross RP (2017) Insights into the Mode of Action of the Sactibiotic Thuricin CD. Front. Microbiol. 8:696. doi: 10.3389/fmicb.2017.00696
Series/Report no.: Frontiers in Microbiology;vol 8
Abstract: Thuricin CD is a two-component bacteriocin, consisting of the peptides Trnα and Trnβ, and belongs to the newly designated sactibiotic subclass of bacteriocins. While it is clear from studies conducted thus far that it is a narrow-spectrum bacteriocin, requiring the synergistic activity of the two peptides, the precise mechanism of action of thuricin CD has not been elucidated. This study used a combination of flow cytometry and traditional culture-dependent assays to ascertain the effects of the thuricin CD peptides on the morphology, physiology and viability of sensitive Bacillus firmus DPC6349 cells. We show that both Trnα and Trnβ are membrane-acting and cause a collapse of the membrane potential, which could not be reversed even under membrane-repolarizing conditions. Furthermore, the depolarizing action of thuricin CD is accompanied by reductions in cell size and granularity, producing a pattern of physiological alterations in DPC6349 cells similar to those triggered by the pore-forming single-component bacteriocin Nisin A, and two-component lacticin 3147. Taken together, these results lead us to postulate that the lytic activity of thuricin CD involves the insertion of thuricin CD peptides into the membrane of target cells leading to permeabilization due to pore formation and consequent flux of ions across the membrane, resulting in membrane depolarization and eventual cell death.
Description: peer-reviewed
HM is a researcher in Teagasc Food Research Centre and the Alimentary Pharmabiotic Centre Microbiome Institute, funded by the Science Foundation of Ireland (SFI)-funded Centre for Science, Engineering and Technology and the Alimentary Pharmabiotic Centre Microbiome Institute (APC) Grant Number SFI/12/RC/2273. Research in PC, CH, MR, VF, and RR laboratories is supported by the Science Foundation of Ireland (SFI)-funded Centre for Science, Engineering and Technology and the APC Microbiome Institute.
URI: http://hdl.handle.net/11019/1522
Appears in Collections:Food Biosciences

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