Protein patterns of gel-entrappedEscherichia coli cells differ from those of free-floating organisms

Perrot, Frédérique; Hébraud, Michel; Charlionet, Roland; Junter, Guy-Alain; Jouenne, Thierry

doi:10.1002/(sici)1522-2683(20000201)21:3<645::aid-elps645>3.0.co;2-1

Cited by 36 publications

(27 citation statements)

References 35 publications

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“…Differences between the microcolony (2-h) proteome and the more developed biofilm (18-h) proteome were largely due to up-and down-regulation of the expression of a multitude of proteins, including cOTCase and LctE. In this respect B. cereus is similar to gram-negative rods such as Escherichia coli (32) and P. aeruginosa (39), both of which display a unique biofilm proteome. For example, transcription of 38% of the genes in E. coli is affected when the bacterium colonizes a surface (34).…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis Reveals Differential Protein Expression by Bacillus cereus during Biofilm Formation

Oosthuizen

Steyn

Theron

et al. 2002

Appl Environ Microbiol

149

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Bacillus cereus, a dairy-associated toxigenic bacterium, readily forms biofilms on various surfaces and was used to gain a better understanding of biofilm development by gram-positive aerobic rods. B. cereus DL5 was shown to readily adapt to an attached mode of growth, with dense biofilm structures developing within 18 h after inoculation when glass wool was used as a surface. Two-dimensional gel electrophoresis (2DE) revealed distinct and reproducible phenotypic differences between 2-and 18-h-old biofilm and planktonic cells (grown both in the presence and in the absence of glass wool). Whereas the 2-h-old biofilm proteome indicated expression of 15 unique proteins, the 18-h-old biofilm proteome contained 7 uniquely expressed proteins. Differences between the microcolony (2-h) proteome and the more developed biofilm (18-h) proteome were largely due to up-and down-regulation of the expression of a multitude of proteins. Selected protein spots excised from 2DE gels were subjected to N-terminal sequencing and identified with high confidence. Among the proteins were catabolic ornithine carbamoyltransferase and L-lactate dehydrogenase. Interestingly, increased levels of YhbH, a member of the sigma 54 modulation protein family which is strongly induced in response to environmental stresses and energy depletion via both B and H , could be observed within 2 h in both attached cells and planktonic cultures growing in the presence of glass wool, indicating that this protein plays an important role in regulation of the biofilm phenotype. Distinct band differences were also found between the extracellular proteins of 18-h-old cultures grown in the presence and in the absence of glass wool.

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Section: Discussionmentioning

confidence: 99%

Proteomic Analysis Reveals Differential Protein Expression by Bacillus cereus during Biofilm Formation

Oosthuizen

Steyn

Theron

et al. 2002

Appl Environ Microbiol

149

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“…Intriguingly, peptidoglycan-free L-forms up-regulate YfiD, which appears as a phosphoprotein (141). In contrast, cells entrapped in gels down-regulate YfiD (344), as do those that overproduce threonine and excrete less acetate (262) or lack the global regulator FlhDC or the aerotaxis receptor Aer (356). Since YfiD is induced in acidic and/or microaerobic environments, it has been proposed to prevent the accumulation of acidic fermentation products by facilitating carbon flux through PFL (476).…”

Section: Acetate Activation Pathwaysmentioning

confidence: 94%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,066

1,274

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To succeed, many cells must alternate between life-styles that permit rapid growth in the presence of abundant nutrients and ones that enhance survival in the absence of those nutrients. One such change in life-style, the “acetate switch,” occurs as cells deplete their environment of acetate-producing carbon sources and begin to rely on their ability to scavenge for acetate. This review explains why, when, and how cells excrete or dissimilate acetate. The central components of the “switch” (phosphotransacetylase [PTA], acetate kinase [ACK], and AMP-forming acetyl coenzyme A synthetase [AMP-ACS]) and the behavior of cells that lack these components are introduced. Acetyl phosphate (acetyl∼P), the high-energy intermediate of acetate dissimilation, is discussed, and conditions that influence its intracellular concentration are described. Evidence is provided that acetyl∼P influences cellular processes from organelle biogenesis to cell cycle regulation and from biofilm development to pathogenesis. The merits of each mechanism proposed to explain the interaction of acetyl∼P with two-component signal transduction pathways are addressed. A short list of enzymes that generate acetyl∼P by PTA-ACKA-independent mechanisms is introduced and discussed briefly. Attention is then directed to the mechanisms used by cells to “flip the switch,” the induction and activation of the acetate-scavenging AMP-ACS. First, evidence is presented that nucleoid proteins orchestrate a progression of distinct nucleoprotein complexes to ensure proper transcription of its gene. Next, the way in which cells regulate AMP-ACS activity through reversible acetylation is described. Finally, the “acetate switch” as it exists in selected eubacteria, archaea, and eukaryotes, including humans, is described

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“…Oxygen limitation has been previously shown to be an important parameter in controlling differential gene expression inside biofilms (Prigent-Combaret et al 1999;Schembri et al 2003). We have previously demonstrated that DppA is over-expressed by sessile E. coli K12 cells in an artificial immobilization model of gel-entrapped bacteria (Perrot et al 2000). DppA is known to be part of an osmotic-shockable transport system that is repressed by the presence of casamino acids (Olson et al 1991).…”

Section: Strain 3714mentioning

confidence: 99%

“…Thus, DNA arrays provide a sensitive but transient snapshot of gene expression and proteomics provide a partial sight of protein expression directly correlated with phenotype. While changes in protein expression during biofilm development have been investigated for a large panel of bacterial species (Arevalo-Ferro et al 2005;Dykes et al 2003;Oosthuizen et al 2001Oosthuizen et al , 2002Sauer et al 2001Sauer et al , 2002Steyn et al 2001;Svensä ter et al 2001;Tré moulet et al 2002a;Vilain et al 2004 a, b, c), a limited number of studies have been conducted to determine the impact of the sessile mode of life on E. coli protein expression (Perrot et al 2000;Perrot et al 2001;Tré moulet et al 2002b). These studies have revealed some alterations in the bacterial protein profiles ranging from 3% to more than 50% of the detected protein spots, which gives evidence of significant physiological differences between planktonic and sessile bacteria.…”

Section: Introductionmentioning

confidence: 99%

Protein expression in Escherichia coli S17-1 biofilms: impact of indole

Collet

Vilain

Cosette

et al. 2006

Antonie van Leeuwenhoek

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Bacteria undergo significant changes during adherence to surfaces and biofilm development. Cell-to-cell signalling molecules are known to be involved in these phenotypic adaptations to the sessile mode of life. We demonstrated previously that indole can act as an extracellular signal to regulate biofilm formation in E. coli. To identify proteins over- or under-expressed in response to E. coli biofilm formation and indole signalling, we compared the proteomes of the E. coli S17-1 wild-type and 3714 (S17-1 tnaA::Tn5) tryptophanase-negative mutant cells (which don't produce indole) grown as suspensions or biofilms in the presence or absence of exogenous indole. From computer-assisted image analysis, 407 spots were discriminated on two-dimensional electropherograms. Principal component analysis (PCA) of the electropherograms did not discriminate between the proteomes of the wild-type and mutant cells grown as suspensions indicating that indole has a limited impact onto protein expression of planktonic cells. The first principal component extracted by PCA, after standardization of the observations, opposed planktonic and biofilm cells confirming the existence of changes in protein expression during E. coli biofilm formation. Among proteins over- or under-expressed by both sessile wild-type and mutant cells, we identified metabolic enzymes, transporters, proteins involved in the translation and transcription machinery, stress response and regulation, and signalling proteins. The wild-type and mutant strains grown as biofilms in the presence of indole were discriminated by the second component. The role of some proteins whose expression was altered in biofilm bacteria compared to suspended counterparts is discussed.

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Protein patterns of gel-entrappedEscherichia coli cells differ from those of free-floating organisms

Cited by 36 publications

References 35 publications

Proteomic Analysis Reveals Differential Protein Expression by Bacillus cereus during Biofilm Formation

Proteomic Analysis Reveals Differential Protein Expression by Bacillus cereus during Biofilm Formation

The Acetate Switch

Protein expression in Escherichia coli S17-1 biofilms: impact of indole

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