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Applied and Environmental Microbiology, May 2007, p. 3300-3306, Vol. 73, No. 10
0099-2240/07/$08.00+0     doi:10.1128/AEM.00124-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Proteomic Approach for Characterization of Hop-Inducible Proteins in Lactobacillus brevis{triangledown}

Jürgen Behr,1 Lars Israel,2 Michael G. Gänzle,1,{dagger} and Rudi F. Vogel1*

Technische Mikrobiologie, Technische Universität München, D-85350 Freising, Germany,1 Ludwig-Maximilians-Universität München, Adolf-Butenandt-Institut (ZfP), D-80336 München, Germany2

Received 17 January 2007/ Accepted 7 March 2007

Resistance to hops is a prerequisite for the capability of lactic acid bacteria to grow in beer and thus cause beer spoilage. Bactericidal hop compounds, mainly iso-{alpha}-acids, are described as ionophores which exchange H+ for cellular divalent cations, e.g., Mn2+, and thus dissipate ion gradients across the cytoplasmic membrane. The acid stress response of Lactobacillus brevis TMW 1.465 and hop adaptation in its variant L. brevis TMW 1.465A caused changes at the level of metabolism, membrane physiology, and cell wall composition. To identify the basis for these changes, a proteomic approach was taken. The experimental design allowed the discrimination of acid stress and hop stress. A strategy for improved protein identification enabled the identification of 84% of the proteins investigated despite the lack of genome sequence data for this strain. Hop resistance in L. brevis TMW 1.465A implies mechanisms to cope with intracellular acidification, mechanisms for energy generation and economy, genetic information fidelity, and enzyme functionality. Interestingly, the majority of hop-regulated enzymes are described as manganese or divalent cation dependent. Regulation of the manganese level allows fine-tuning of the metabolism, which enables a rapid response to environmental (stress) conditions. The hop stress response indicates adaptations shifting the metabolism into an energy-saving mode by effective substrate conversion and prevention of exhaustive protein de novo synthesis. The findings further demonstrate that hop stress in bacteria not only is associated with proton motive force depletion but obviously implies divalent cation limitation.

* Corresponding author. Mailing address: Technische Mikrobiologie, Technische Universität München, Weihenstephaner Steig 16, 85350 Freising, Germany. Phone: 49 8161 713663. Fax: 49 8161 713327. E-mail: rudi.vogel{at}wzw.tum.de

{triangledown} Published ahead of print on 16 March 2007.

{dagger} Present address: Dept. Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Canada.

Applied and Environmental Microbiology, May 2007, p. 3300-3306, Vol. 73, No. 10
0099-2240/07/$08.00+0     doi:10.1128/AEM.00124-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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