Purification of the bacteriocin bavaricin MN and characterization of its mode of action against Listeria monocytogenes Scott A cells and lipid vesicles.

Applied and Environmental Microbiology
A Kaiser, Thomas J Montville

Abstract

Bavaricin MN was purified from Lactobacillus sake culture supernatant 135-fold with a final yield of 11%. Sequence analysis revealed bavaricin MN to be a 42-amino-acid peptide having a molecular weight of 4,769 and a calculated pI of 10.0. Computer analysis indicated that the C-terminal region may form an alpha-helical structure with an amphipathic nature deemed important in the interaction of bacteriocins with biological membranes. Bavaricin MN rapidly depleted the membrane potential (delta p) of energized Listeria monocytogenes cells in a concentration-dependent fashion. At a bavaricin MN concentration of 9.0 micrograms/ml, the delta p decreased by 85%. Both the electrical potential (delta psi) and Z delta pH components of the delta p were depleted, and this depletion was not dependent on a threshold level of proton motive force. In addition to studying the effect of bavaricin MN on the delta p of vegetative cells, bavaricin MN-induced carboxyfluorescein (CF) efflux from L. monocytogenes-derived lipid vesicles was also characterized. Bavaricin MN-induced CF leakage was also concentration dependent with an optimum of pH 6.0. The rate of CF efflux was 63% greater in lipid vesicles in which a delta psi was generated compared wit...Continue Reading

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Citations

Jun 21, 2007·Journal of Applied Microbiology·K NaghmouchiI Fliss
Apr 1, 2000·Applied and Environmental Microbiology·D GuyonnetJ M Berjeaud
Oct 23, 2010·Journal of Basic Microbiology·Han-Sheng GongHui Wang
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Dec 12, 2012·International Journal of Molecular Sciences·Yanhua CuiHongyu Cui
Aug 3, 2010·The Protein Journal·Abdelmajid ZouhirJeannette Ben Hamida
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Feb 15, 2002·International Journal of Food Microbiology·Winy Messens, Vuyst Luc De

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