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.
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.
Beganović
Jasna
J
INRA, PAPPSO (Plate-Forme d'Analyse Protéomique de Paris Sud-Ouest), Jouy en Josas, France.
Guillot
Alain
A
van de Guchte
Maarten
M
Jouan
Anne
A
Gitton
Christophe
C
Loux
Valentin
V
Roy
Karine
K
Huet
Sylvie
S
Monod
Hervé
H
Monnet
Véronique
V
D000222:Adaptation, Physiological; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D002853:Chromatography, Liquid / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D013294:Lactococcus lactis / Q000378:metabolism*; D051379:Mice; D020543:Proteome; D012995:Solubility; D053719:Tandem Mass Spectrometry / Q000379:methods*
D001426:Bacterial Proteins; D020543:Proteome