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Applied and Environmental Microbiology, April 2006, p. 2556-2563, Vol. 72, No. 4
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.4.2556-2563.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Bioenergetic Mechanism for Nisin Resistance, Induced by the Acid Tolerance Response of Listeria monocytogenes

Marcelo Bonnet, Mohamed M. Rafi, Michael L. Chikindas, and Thomas J. Montville^*

Department of Food Science, Cook College, New Jersey Agricultural Experimental Station, Rutgers, The State University of New Jersey, New Brunswick, New Jersey

Received 30 August 2005/ Accepted 2 February 2006

This study examined the bioenergetics of Listeria monocytogenes, induced to an acid tolerance response (ATR). Changes in bioenergetic parameters were consistent with the increased resistance of ATR-induced (ATR⁺) cells to the antimicrobial peptide nisin. These changes may also explain the increased resistance of L. monocytogenes to other lethal factors. ATR⁺ cells had lower transmembrane pH (pH) and electric potential () than the control (ATR^–) cells. The decreased proton motive force (PMF) of ATR⁺ cells increased their resistance to nisin, the action of which is enhanced by energized membranes. Paradoxically, the intracellular ATP levels of the PMF-depleted ATR⁺ cells were 7-fold higher than those in ATR^– cells. This suggested a role for the F_oF₁ ATPase enzyme complex, which converts the energy of ATP hydrolysis to PMF. Inhibition of the F_oF₁ ATPase enzyme complex by N'-N'-1,3-dicyclohexylcarbodiimide increased ATP levels in ATR^– but not in ATR⁺ cells, where ATPase activity was already low. Spectrometric analyses (surface-enhanced laser desorption ionization-time of flight mass spectrometry) suggested that in ATR⁺ listeriae, the downregulation of the proton-translocating c subunit of the F_oF₁ ATPase was responsible for the decreased ATPase activity, thereby sparing vital ATP. These data suggest that regulation of F_oF₁ ATPase plays an important role in the acid tolerance response of L. monocytogenes and in its induced resistance to nisin.

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* Corresponding author. Mailing address: Department of Food Science, Rutgers, The State University of New Jersey, 65 Dudley Rd., New Brunswick, NJ 08901. Phone: (732) 932-9611. Fax: (732) 932-6776. E-mail: montville{at}aesop.rutgers.edu.

Present address: Ministry of Agriculture, Livestock and Food Supply, Brazilian Agriculture Research Corporation-Embrapa, Embrapa Headquarters, Parque Estação Biológica, Brasília DF 70770-901, Brazil.

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Applied and Environmental Microbiology, April 2006, p. 2556-2563, Vol. 72, No. 4
0099-2240/06/$08.00+0     doi:10.1128/AEM.72.4.2556-2563.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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