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

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Beganovic, Jasna | Guillot, Alain, A. | van de Guchte, Maarten | Jouan, Anne | Gitton, Christophe, C. | Loux, Valentin | Roy, Karine | Huet, Sylvie | Monod, Hervé | Monnet, Veronique, V.

Edité par CCSD ; American Chemical Society -

International audience. 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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