Surface properties of bacteria sensitive and resistant to the class IIa carnobacteriocin Cbn BM1

Aims: Class IIa bacteriocins are small antimicrobial peptides synthesized by lactic acid bacteria. The proposed mechanisms of action for class IIa bacteriocins suggest that the physicochemical properties of the target bacterial surface govern the bacteriocin antimicrobial activity. The aim of this s...

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Veröffentlicht in:Journal of applied microbiology 2012-02, Vol.112 (2), p.372-382
Hauptverfasser: Jacquet, T, Cailliez‐Grimal, C, Borges, F, Gaiani, C, Francius, G, Duval, J.F.L, Waldvogel, Y, Revol‐Junelles, A.‐M
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Sprache:eng
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Zusammenfassung:Aims: Class IIa bacteriocins are small antimicrobial peptides synthesized by lactic acid bacteria. The proposed mechanisms of action for class IIa bacteriocins suggest that the physicochemical properties of the target bacterial surface govern the bacteriocin antimicrobial activity. The aim of this study is to decipher the relationship between both sensitivity and resistance to a class IIa bacteriocin, carnobacteriocin BM1 and physicochemical surface properties of bacteria. Methods and Results: The study was performed on 18 strains by a microbial adhesion to solvents process and with electrophoretic mobility measurements considering bacteria as soft particles. A large variation in bacterial surface properties is observed among the bacterial populations. Electro‐hydrodynamic parameters values appear to be more homogeneous for sensitive strains than for the resistant ones, which can exhibit more extreme values. Conclusions: Physicochemical surface properties of 18 strains determined show large variations between the strains. However, no direct link between these surface properties and the resistant/sensitive phenotypes of the strains can be stated. Significance and Impact of the Study: The surface physicochemical properties tested have a low predictive power to discriminate sensitive or resistant strains when determined at the bacterial population scale.
ISSN:1364-5072
1365-2672
DOI:10.1111/j.1365-2672.2011.05195.x