Rapid identification of stress-related fingerprint from whole bacterial cells of <i>Bifidobacterium lactis</i> using matrix assisted laser desorption/ionization mass spectrometry

Marvin-Guy, Laure F.; Parche, Stephan; Wagnière, Sandrine; Moulin, Julie; Zink, Ralf; Kussmann, Martin; Fay, Laurent B.

doi:10.1016/j.jasms.2004.04.035

Cited by 20 publications

(16 citation statements)

References 23 publications

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“…Reproducibility of the MALDI-MS profiles obtained from sub-cultures of several Gram-positive and Gram-negative representatives analyzed over 2, 3, or 4-month period was proved by Claydon et al (1996), Welham et al (1998. According to Marvin-Guy et al (2004), day-to-day reproducibility of Bifidobacterium lactis MALDI-MS peak relative intensities was characterized with a correlation coefficient of 0.98. Smole et al (2002) examined the reproducibility of S. aureus lysate MS profile over a 4-month period, documenting stable presence in just one half of the peaks.…”

Section: Reproducibilitymentioning

confidence: 99%

“…With no regard on whether the bacteria were Gram-positive or Gram-negative, the role of 0.1% TFA as a solvent can be found in protein extraction from bacterial cells (Dai, Whittal, & Li, 1999;Nilsson, 1999;Wang et al, 2002), suspending the cells Marvin-Guy et al, 2004;Ruelle et al, 2004;Liu et al, 2007;Vanlaere et al, 2008) or for cell washing (Welham et al, 1998), followed, moreover, with subsequent extraction step with another solvent (Camara and Hays, 2007).…”

Section: A Choice Of Solvent For Cell Suspension/extractionmentioning

confidence: 99%

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Sample preparation methods for MALDI‐MS profiling of bacteria

Šedo¹,

Sedláček²,

Zdráhal³

2010

Mass Spectrometry Reviews

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Direct matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) bacterial cell or lysate analysis appears to meet all the criteria required for a rapid and reliable analytical microorganism identification and taxonomical classification tool. Few-minute analytical procedure providing information extending up to sub-species level underlines the potential of the MALDI-MS profiling in comparison with other methods employed in the field. However, the quality of MALDI-MS profiles and consequently the performance of the method are influenced by numerous factors, which involve particular steps of the sample preparation procedure. This review is aimed at advances in development and optimization of the MALDI-MS profiling methodology. Approaches improving the quality of the MALDI-MS profiles and universal feasibility of the method are discussed.

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Section: Reproducibilitymentioning

confidence: 99%

Section: A Choice Of Solvent For Cell Suspension/extractionmentioning

confidence: 99%

Sample preparation methods for MALDI‐MS profiling of bacteria

Šedo¹,

Sedláček²,

Zdráhal³

2010

Mass Spectrometry Reviews

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“…Furthermore, sublethal bile concentrations can also trigger a physiological adaptive response in bifidobacteria (7,23,28), being DnaK induced in some species of Bifidobacterium in the presence of bile (49). Marvin-Guy et al (36) recently used matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry for rapid identification of bile salt stress-related fingerprints from whole Bifidobacterium lactis cells, but no information was provided about protein identification and function. Furthermore, a proteomic study of Bifidobacterium infantis generated by multidimensional chromatography coupled to tandem mass spectrometry led to the identification of 136 proteins of this species (59).…”

mentioning

confidence: 99%

Proteomic Analysis of Global Changes in Protein Expression during Bile Salt Exposure of Bifidobacterium longum NCIMB 8809

Sánchez

Champomier‐Vergès²,

Anglade³

et al. 2005

J Bacteriol

179

171

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Adaptation to and tolerance of bile stress are among the main limiting factors to ensure survival of bifidobacteria in the intestinal environment of humans. The effect of bile salts on protein expression patterns of Bifidobacterium longum was examined. Protein pattern comparison of strains grown with or without bile extract allowed us to identify 34 different proteins whose expression was regulated. The majority of these proteins were induced after both a minor (0.6 g liter ؊1 ) and a major (1.2 g liter ؊1 ) exposure to bile. These include general stress response chaperones, proteins involved in transcription and translation and in the metabolism of amino acids and nucleotides, and several enzymes of glycolysis and pyruvate catabolism. Remarkably, xylulose 5-phosphate/fructose 6-phosphate phosphoketolase, the key enzyme of the so-called bifidobacterial shunt, was found to be upregulated, and the activity on fructose 6-phosphate was significantly higher for protein extracts of cells grown in the presence of bile. Changes in the levels of metabolic end products (acetate and lactate) were also detected. These results suggest that bile salts, to which bifidobacteria are naturally exposed, induce a complex physiological response rather than a single event in which proteins from many different functional categories take part. This study has extended our understanding of the molecular mechanism underlying the capacity of intestinal bifidobacteria to tolerate bile.

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“…The 20 M serpin and 10 M protease mixture was incubated for 5 min in the reaction buffer at room temperature. The masses of the peptide fragments were determined by MALDI-MS (Bruker Autoflex ToF) in linear mode (19).…”

mentioning

confidence: 99%

A Serpin from the Gut Bacterium Bifidobacterium longum Inhibits Eukaryotic Elastase-like Serine Proteases

Ivanov

Emonet

Foata

et al. 2006

Journal of Biological Chemistry

150

118

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Serpins form a large class of protease inhibitors involved in regulation of a wide spectrum of physiological processes. Recently identified prokaryotic members of this protein family may provide a key to the evolutionary origins of the unique serpin fold and the associated inhibitory mechanism. We performed a biochemical characterization of a serpin from Bifidobacterium longum, an anaerobic Gram-positive bacterium that naturally colonizes human gastrointestinal tract. The B. longum serpin was shown to efficiently inhibit eukaryotic elastase-like proteases with a stoichiometry of inhibition close to 1. Porcine pancreatic elastase and human neutrophil elastase were inhibited with the second order association constants of 4. , respectively. The B. longum serpin is expected to be active in the gastrointestinal tract, because incubation of the purified recombinant serpin with mouse feces produces a stable covalent serpin-protease adduct readily detectable by SDS-PAGE. Bifidobacteria may encounter both pancreatic elastase and neutrophil elastase in their natural habitat and protection against exogenous proteolysis may play an important role in the interaction between these commensal bacteria and their host.Numerous signaling pathways in higher organisms, such as apoptosis, inflammation, blood clotting, and others, involve proteolytic events as mediators of signal initiation, transmission, and termination. Substrate specificity of the involved proteases and a tight regulation of their activation and inhibition are essential regulatory mechanisms of temporal and spatial control in proteolytic signaling. Serpins (serine protease inhibitors) represent a large class of polypeptide serine protease inhibitors that are involved in regulation of a wide spectrum of proteasemediated processes (1, 2). They fold into a metastable native structure with an exposed substrate-like reactive center loop (RCL) 3 (3) and, unlike the small polypeptide inhibitors from the Kunitz or Kazal family, they do not act as reversible competitive inhibitors of the target proteases but rather as stoichiometric suicide inactivators with a unique inhibition mechanism driven by conformational change. Upon cleavage of RCL by the target protease and formation of the covalent acyl-enzyme reaction intermediate, the serpin fold undergoes a major conformational rearrangement, and the RCL is inserted as the middle strand of the beta sheet A to form a six-stranded anti-parallel ␤ sheet at the core of the cleaved serpin structure (4). This conformational change creates a steric clash with the protease and the resulting distortion inactivates the enzyme and traps it as a covalent serpin-protease adduct (5).Serpins are widely distributed in higher eukaryotic organisms and are also found in some viruses where they appear to modulate virus-host interactions and viral infectivity (1). Thirty-four serpins identified in the human genome belong to nine different phylogenetic clades in the currently adopted serpin classification (2). Notably, some members of the serpin ...

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Rapid identification of stress-related fingerprint from whole bacterial cells of Bifidobacterium lactis using matrix assisted laser desorption/ionization mass spectrometry

Cited by 20 publications

References 23 publications

Sample preparation methods for MALDI‐MS profiling of bacteria

Sample preparation methods for MALDI‐MS profiling of bacteria

Proteomic Analysis of Global Changes in Protein Expression during Bile Salt Exposure of Bifidobacterium longum NCIMB 8809

A Serpin from the Gut Bacterium Bifidobacterium longum Inhibits Eukaryotic Elastase-like Serine Proteases

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