Quantitative Observations on the Chemical Activity of "Resting" Staphylococcus Aureus: Studies in Bacterial Metabolism, XCIII

Kendall, Arthur Isaac; Friedemann, Theodore E.; Ishikawa, Mitzuteru

doi:10.1093/infdis/47.3.223

Cited by 11 publications

(9 citation statements)

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“…Accelerated reutilization of fermentation products in the complemented mutants confirmed this notion. Impairment of aerobic respiration in the ⌬mpsA or the ⌬mpsABC mutant was further indicated by increased extracellular lactate concentrations in the mutants, as lactate production was shown to be promoted under oxygen-depleted conditions (67,68), which may have consequences similar to those of respiratory impairments.…”

Section: Discussionmentioning

confidence: 99%

The Staphylococcus aureus NuoL-Like Protein MpsA Contributes to the Generation of Membrane Potential

et al. 2015

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bIn aerobic microorganisms, the entry point of respiratory electron transfer is represented by the NADH:quinone oxidoreductase. The enzyme couples the oxidation of NADH with the reduction of quinone. In the type 1 NADH:quinone oxidoreductase (Ndh1), this reaction is accompanied by the translocation of cations, such as H ؉ or Na ؉ . In Escherichia coli, cation translocation is accomplished by the subunit NuoL, thus generating membrane potential (⌬). Some microorganisms achieve NADH oxidation by the alternative, nonelectrogenic type 2 NADH:quinone oxidoreductase (Ndh2), which is not cation translocating. Since these enzymes had not been described in Staphylococcus aureus, the goal of this study was to identify proteins operating in the NADH:quinone segment of its respiratory chain. We demonstrated that Ndh2 represents a NADH:quinone oxidoreductase in S. aureus. Additionally, we identified a hypothetical protein in S. aureus showing sequence similarity to the proton-translocating subunit NuoL of complex I in E. coli: the NuoL-like protein MpsA. Mutants with deletion of the nuoL-like gene mpsA and its corresponding operon, mpsABC (mps for membrane potential-generating system), exhibited a small-colony-variant-like phenotype and were severely affected in ⌬ and oxygen consumption rates. The MpsABC proteins did not confer NADH oxidation activity. Using an Na؉ /H ؉ antiporter-deficient E. coli strain, we could show that MpsABC constitute a cation-translocating system capable of Na ؉ transport. Our study demonstrates that MpsABC represent an important functional system of the respiratory chain of S. aureus that acts as an electrogenic unit responsible for the generation of ⌬.O n the basis of Mitchell's chemiosmotic theory (1), the proton motive force (⌬p) for driving ATP synthase consists of a transmembrane pH gradient (⌬pH; acidic outside and alkaline inside) and a transmembrane electrical potential (membrane potential [⌬]; negative inside and positive outside). Despite the fact that Staphylococcus aureus is an important human pathogen, there is strikingly little knowledge regarding its respiratory chain and its capacity to generate ⌬ under aerobic conditions (2). The ⌬ generated by the respiratory chain drives ATP synthesis (3).In aerobically living, chemoorganotrophic organisms, the entry point of respiratory electron transfer and, thus, the initiation point of ⌬ generation are represented by NADH:quinone oxidoreductase. Remarkably, this complex has not been characterized in S. aureus so far. Generally, the NADH generated in glycolysis and the tricarboxylic acid (TCA) cycle during glucose degradation must be reoxidized to NAD ϩ to allow operation of the central carbon and energy metabolism. In most pro-and eukaryotes, NADH oxidation is accomplished by respiratory complex I, the electrogenic NADH:quinone oxidoreductase, a highly conserved multisubunit enzyme (4) that is composed of 13 subunits in Escherichia coli (5) and even 45 subunits in mitochondria (6). The enzyme couples the oxidation of NADH and the reduction of...

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Section: Discussionmentioning

confidence: 99%

The Staphylococcus aureus NuoL-Like Protein MpsA Contributes to the Generation of Membrane Potential

et al. 2015

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“…Reduction of NAD ϩ to NADH, without an equivalent means to oxidize NADH, can create a redox imbalance and inhibit growth. Under microaerobic or anaerobic growth conditions, the majority of pyruvate is reduced to lactic acid (29,31), concomitant with a 1:1 stoichiometric oxidation of NADH back to NAD ϩ . To compensate for the diversion of pyruvate into pyruvate formate-lyase, S. aureus also shunts pyruvate into the butanediol pathway via acetolactate synthase (EC 2.2.1.6) ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…In a complex medium containing glucose, S. aureus will preferentially catabolize glucose for carbon and energy through the glycolytic and pentose phosphate pathways (4,10,20,29,36). Despite a preference for glucose and a high concentration of glucose in the medium (Ͼ15 mM) ( Fig.…”

Section: Discussionmentioning

confidence: 99%

Staphylococcus aureus Biofilm Metabolism and the Influence of Arginine on Polysaccharide Intercellular Adhesin Synthesis, Biofilm Formation, and Pathogenesis

et al. 2007

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Staphylococcus aureus and Staphylococcus epidermidis are the leading causes of nosocomial infections in the United States and often are associated with biofilms attached to indwelling medical devices. Despite the importance of biofilms, there is very little consensus about the metabolic requirements of S. aureus during biofilm growth. To assess the metabolic requirements of S. aureus growing in a biofilm, we grew USA200 and USA300 clonal types in biofilm flow cells and measured the extraction and accumulation of metabolites. In spite of the genetic differences, both clonal types extracted glucose and accumulated lactate, acetate, formate, and acetoin, suggesting that glucose was catabolized to pyruvate that was then catabolized via the lactate dehydrogenase, pyruvate formate-lyase, and butanediol pathways. Additionally, both clonal types selectively extracted the same six amino acids (serine, proline, arginine, glutamine, glycine, and threonine) from the culture medium. These data and recent speculation about the importance of arginine in biofilm growth and the function of arginine deiminase in USA300 clones led us to genetically inactivate the sole copy of the arginine deiminase operon by deleting the arginine/ornithine antiporter gene (arcD) in the USA200 clonal type and to assess the effect on biofilm development and pathogenesis. Although inactivation of arcD did completely inhibit arginine transport and did reduce polysaccharide intercellular adhesin accumulation, arcD mutants formed biofilms and achieved cell densities in catheter infection studies that were equivalent to those for isogenic wild-type strains.

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“…The catabolic fate of pyruvate is determined by the growth conditions, specifically, the availability of oxygen. During anaerobic growth, pyruvate is reduced primarily to lactic acid (115,125), with the concomitant reoxidation of NADH allowing for the continuation of glycolysis. In aerobically grown staphylococci, pyruvate is enzymatically oxidized to acetyl coenzyme A (acetyl-CoA) and CO 2 by the pyruvate dehydrogenase complex (71).…”

Section: Overview Of Staphylococcal Metabolismmentioning

confidence: 99%

At the Crossroads of Bacterial Metabolism and Virulence Factor Synthesis in Staphylococci

Somerville

Proctor

2009

Microbiol Mol Biol Rev

329

348

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SUMMARY Bacteria live in environments that are subject to rapid changes in the availability of the nutrients that are necessary to provide energy and biosynthetic intermediates for the synthesis of macromolecules. Consequently, bacterial survival depends on the ability of bacteria to regulate the expression of genes coding for enzymes required for growth in the altered environment. In pathogenic bacteria, adaptation to an altered environment often includes activating the transcription of virulence genes; hence, many virulence genes are regulated by environmental and nutritional signals. Consistent with this observation, the regulation of most, if not all, virulence determinants in staphylococci is mediated by environmental and nutritional signals. Some of these external signals can be directly transduced into a regulatory response by two-component regulators such as SrrAB; however, other external signals require transduction into intracellular signals. Many of the external environmental and nutritional signals that regulate virulence determinant expression can also alter bacterial metabolic status (e.g., iron limitation). Altering the metabolic status results in the transduction of external signals into intracellular metabolic signals that can be “sensed” by regulatory proteins (e.g., CodY, Rex, and GlnR). This review uses information derived primarily using Bacillus subtilis and Escherichia coli to articulate how gram-positive pathogens, with emphasis on Staphylococcus aureus and Staphylococcus epidermidis, regulate virulence determinant expression in response to a changing environment.

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Quantitative Observations on the Chemical Activity of "Resting" Staphylococcus Aureus: Studies in Bacterial Metabolism, XCIII

Cited by 11 publications

References 0 publications

The Staphylococcus aureus NuoL-Like Protein MpsA Contributes to the Generation of Membrane Potential

The Staphylococcus aureus NuoL-Like Protein MpsA Contributes to the Generation of Membrane Potential

Staphylococcus aureus Biofilm Metabolism and the Influence of Arginine on Polysaccharide Intercellular Adhesin Synthesis, Biofilm Formation, and Pathogenesis

At the Crossroads of Bacterial Metabolism and Virulence Factor Synthesis in Staphylococci

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