Journal
FEMS MICROBIOLOGY LETTERS
Volume 334, Issue 2, Pages 143-149Publisher
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2012.02630.x
Keywords
sakacin A; dual mechanisms; Listeria spp
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Sakacin A was purified to homogeneity through simple chromatographic procedures from cultures of Lactobacillus sakei DSMZ 6333 grown on a low-cost medium. The highly purified protein dissipated both transmembrane potential (??) and transmembrane pH gradient (?pH) in Listeria cells in a very intense, rapid, and energy-dependent fashion. On a slower timescale, purified sakacin A also showed a lytic activity toward isolated cell walls of Listeria. Mass spectrometry was used to analyze the products of sakacin A action on cell walls, evidencing that sakacin A acts on various types of bonds within peptoglycans.
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