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 (ΔΨ) and transmembrane pH gradient (ΔpH) 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.

Purified sakacin A shows a dual mechanism of action against Listeria spp: proton motive force dissipation and cell wall breakdown / V. Trinetta, A. Morleo, F. Sessa, S. Iametti, F. Bonomi, P. Ferranti. - In: FEMS MICROBIOLOGY LETTERS. - ISSN 0378-1097. - 334:2(2012 Sep), pp. 143-149. [10.1111/j.1574-6968.2012.02630.x]

Purified sakacin A shows a dual mechanism of action against Listeria spp: proton motive force dissipation and cell wall breakdown

F. Sessa;S. Iametti;F. Bonomi
Penultimo
;
2012

Abstract

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 (ΔΨ) and transmembrane pH gradient (ΔpH) 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.
Dual mechanisms; Listeria spp; Sakacin A
Settore BIO/10 - Biochimica
Settore BIO/11 - Biologia Molecolare
Settore AGR/16 - Microbiologia Agraria
Settore AGR/15 - Scienze e Tecnologie Alimentari
set-2012
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/223106
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