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. 2010 Feb 5;9(2):677-88.
doi: 10.1021/pr9000866.

Characterization of the insoluble proteome of Lactococcus lactis by SDS-PAGE LC-MS/MS leads to the identification of new markers of adaptation of the bacteria to the mouse digestive tract

Jasna Beganović  1 , Alain Guillot, Maarten van de Guchte, Anne Jouan, Christophe Gitton, Valentin Loux, Karine Roy, Sylvie Huet, Hervé Monod, Véronique Monnet
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Characterization of the insoluble proteome of Lactococcus lactis by SDS-PAGE LC-MS/MS leads to the identification of new markers of adaptation of the bacteria to the mouse digestive tract

Jasna Beganović et al. J Proteome Res. .

Abstract

We characterized the insoluble proteome of Lactococcus lactis using 1D electrophoresis-LC-MS/MS and identified 313 proteins with at least two different peptides. The identified proteins include 89 proteins having a predicted signal peptide and 25 predicted to be membrane-located. In addition, 67 proteins had alkaline isoelectric point values. Using spectra and peptide counts, we compared protein abundances in two different conditions: growth in rich medium, and after transit in the mouse digestive tract. We identified the large mechanosensitive channel and a putative cation transporter as membrane markers of bacterial adaptation to the digestive tract.

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