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. 2007 Nov;73(21):6757-67.
doi: 10.1128/AEM.00637-07. Epub 2007 Sep 7.

Adaptation and response of Bifidobacterium animalis subsp. lactis to bile: a proteomic and physiological approach

Borja Sánchez  1 , Marie-Christine Champomier-Vergès, Birgitte Stuer-Lauridsen, Patricia Ruas-Madiedo, Patricia Anglade, Fabienne Baraige, Clara G de los Reyes-Gavilán, Eric Johansen, Monique Zagorec, Abelardo Margolles
Affiliations

Adaptation and response of Bifidobacterium animalis subsp. lactis to bile: a proteomic and physiological approach

Borja Sánchez et al. Appl Environ Microbiol. 2007 Nov.

Abstract

Bile salts are natural detergents that facilitate the digestion and absorption of the hydrophobic components of the diet. However, their amphiphilic nature makes them very inhibitory for bacteria and strongly influences bacterial survival in the gastrointestinal tract. Adaptation to and tolerance of bile stress is therefore crucial for the persistence of bacteria in the human colonic niche. Bifidobacterium animalis subsp. lactis, a probiotic bacterium with documented health benefits, is applied largely in fermented dairy products. In this study, the effect of bile salts on proteomes of B. animalis subsp. lactis IPLA 4549 and its bile-resistant derivative B. animalis subsp. lactis 4549dOx was analyzed, leading to the identification of proteins which may represent the targets of bile salt response and adaptation in B. animalis subsp. lactis. The comparison of the wild-type and the bile-resistant strain responses allowed us to hypothesize about the resistance mechanisms acquired by the derivative resistant strain and about the bile salt response in B. animalis subsp. lactis. In addition, significant differences in the levels of metabolic end products of the bifid shunt and in the redox status of the cells were also detected, which correlate with some differences observed between the proteomes. These results indicate that adaptation and response to bile in B. animalis subsp. lactis involve several physiological mechanisms that are jointly dedicated to reduce the deleterious impact of bile on the cell's physiology.

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Figures

FIG. 1.
FIG. 1.
Proteomes of the B. animalis WT and bile salt-resistant derivative. 2D gels of cytosolic extracts from mid-exponential-phase cells of B. animalis IPLA 4549 (a and c) and B. animalis 4549dOx (b and d) grown without (a and b) and with (c and d) bile salts are shown. Spots identified by peptide mass fingerprinting are labeled, and the identifications of the 45 spots affected by bile salts are listed in Table 1.
FIG. 2.
FIG. 2.
Proteins involved in the bile salt response of B. animalis. Left circle, proteins induced or repressed by oxgall in the WT. Right circle, proteins induced or repressed by oxgall only in the mutant. Intersection, proteins repressed or induced by oxgall in both strains. Shading indicates proteins whose expression is also constitutively modified in the mutant in the absence of oxgall. Asterisks indicate proteins whose synthesis is also affected by bile in B. longum (47). ++ indicates proteins that were detected only in the presence of bile salts.
FIG. 3.
FIG. 3.
Schematic representation of the carbon catabolic pathway, the bifid shunt, and oxalic acid degradation. Enzymes that are involved in the general bile salt response in B. animalis are marked with gray circles. Abbreviations: AckA, acetate kinase; Adh2, aldehyde-alcohol dehydrogenase 2; Aga, α-galactosidase; Agl, α-glucosidase; Frc, formyl-CoA transferase; GalE1, UDP-glucose 4-epimerase; Gap, glyceraldehyde-3-phosphate dehydrogenase C; GlkA, glucokinase; Gnt, 6-phosphogluconate dehydrogenase; Gpi, glucose 6-phosphate isomerase; Ldh2, lactate dehydrogenase; Oxc, oxalyl-CoA decarboxylase; Pgm, phosphoglucomutase; Pfl, formate acetyltransferase; Tal, transaldolase; Tkt, transketolase; UgpA, UTP-glucose-1-phosphate uridylyltransferase; Xfp, xylulose-5-phosphate/fructose-6-phosphate phosphoketolase; Zwf2, glucose-6-phosphate 1-dehydrogenase; Pi, phosphate.
FIG. 4.
FIG. 4.
Redox ratios (A), NADH-associated fluorescence (B), and FAD-associated fluorescence (C) of IPLA 4549 and 4549dOx grown in the absence of bile (solid bars) or in the presence of 3 g liter−1 (gray bars) or 10 g liter−1 (white bars) bile. Error bars represent standard deviations.
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