Redox Homeostasis

Messens, Joris; Rouhier, Nicolas; Collet, Jean-François

doi:10.1007/978-94-007-5787-5_3

Cited by 4 publications

(4 citation statements)

References 162 publications

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“…In the spider mite T. urticae , Wolbachia infection is associated with the enrichment of gene sets related to oxidoreductase activity ( Zhang et al, 2015 ). Oxidoreductases are known to produce ROS ( Raha and Robinson, 2000 ; Esterházy et al, 2008 ), but also to control redox homeostasis ( Messens et al, 2013 ). Moreover, Wolbachia encodes an oxidoreductase ( α -DsbA1) which, due to its low redox potential, might have antioxidant properties ( Kurz et al, 2009 ).…”

Section: Wolbachia and The Insect Immune Systemmentioning

confidence: 99%

Wolbachia and the insect immune system: what reactive oxygen species can tell us about the mechanisms of Wolbachia–host interactions

2015

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Wolbachia are intracellular bacteria that infect a vast range of arthropod species, making them one of the most prevalent endosymbionts in the world. Wolbachia’s stunning evolutionary success is mostly due to their reproductive parasitism but also to mutualistic effects such as increased host fecundity or protection against pathogens. However, the mechanisms underlying Wolbachia phenotypes, both parasitic and mutualistic, are only poorly understood. Moreover, it is unclear how the insect immune system is involved in these phenotypes and why it is not more successful in eliminating the bacteria. Here we argue that reactive oxygen species (ROS) are likely to be key in elucidating these issues. ROS are essential players in the insect immune system, and Wolbachia infection can affect ROS levels in the host. Based on recent findings, we elaborate a hypothesis that considers the different effects of Wolbachia on the oxidative environment in novel vs. native hosts. We propose that newly introduced Wolbachia trigger an immune response and cause oxidative stress, whereas in coevolved symbioses, infection is not associated with oxidative stress, but rather with restored redox homeostasis. Redox homeostasis can be restored in different ways, depending on whether Wolbachia or the host is in charge. This hypothesis offers a mechanistic explanation for several of the observed Wolbachia phenotypes.

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Section: Wolbachia and The Insect Immune Systemmentioning

confidence: 99%

Wolbachia and the insect immune system: what reactive oxygen species can tell us about the mechanisms of Wolbachia–host interactions

2015

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“…Intracellular environment in general is highly reducing, which prevents the formation of disulphide bonds and such are not observed in water soluble proteins in the cytoplasm under normal conditions. [ 16 ] At least the concentration of protein thiol disulphides in controls is below the detection limit of the method used. In conditions of salt stress the concentration of ROS is expected to be increased.…”

Section: Resultsmentioning

confidence: 99%

“…Overall, the current literature is giving more and more importance to the index of protein thiols. [ 16 ] It represents the molar ratio of low molecular weight thiols involved in mixed disulphides to proteins and free protein thiols. This value combined with the total intracellular redox potential[ 19 ] is considered as sensitive and important indicators of stress levels, cell fate and development phases.…”

Section: Resultsmentioning

confidence: 99%

Changes in protein thiols in response to salt stress in embryogenic suspension cultures ofDactylis glomerataL.

Zagorchev

Terzieva

Stoichkova

et al. 2014

Biotechnology & Biotechnological Equipment

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The aim of the present study is to assess the rate of protein disulphide formation and the activity of NADPH-dependent thioredoxin and glutaredoxin systems, responsible for the reverse reduction of protein and mixed protein-glutathione disulphides, in embryogenic suspension cultures of Dactylis glomerata, subjected to salt stress. Two concentrations of NaCl previously established as enhancing (0.085 mol/L) and inhibiting (0.17 mol/L) somatic embryogenesis were used. The quantitative (by colour reaction with Ellman's reagent) and qualitative (by diagonal gel electrophoresis) analyses showed a significant increase in protein disulphide formation in salt-treated cultures compared to controls. The ratio of disulphides to free thiols is higher in 0.17 mol/L NaCl-treated cultures. The activity of the thioredoxin–thioredoxin reductase system has been increased accordingly in 0.085 mol/L NaCl-treated cultures but decreased at the higher salt concentration. The activity of glutaredoxins was also estimated, by using glutathionylated bovine serum albumin as substrate and following the decrease of NADPH absorbance at 340 nm in the presence of glutathione and glutathione reductase. Mild salt (0.085 mol/L NaCl) treated cultures again showed the highest activity compared to controls and 0.17 mol/L NaCl-treated cultures. Based on these observations it was suggested that salt treatment resulted in increased protein disulphide formation and thioredoxin and glutaredoxin systems are important regulators of this process, strongly involved in salt stress response. The highest activity at 0.085 mol/L NaCl may be also related to the regulatory mechanisms, involved in the potentiating of somatic embryogenesis at this salt concentration.

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“…These molecules function as cellular redox buffers to maintain the reduced status of the cytoplasm [ 8 ]. The most extensively characterized LMW thiol is glutathione (GSH), which is found in eukaryotes and gram negative bacteria [ 9 ]; gram positive bacteria use alternative LMW thiols, such as bacillithiol (BSH) and mycothiol (MSH) [ 9 ].…”

Section: Introductionmentioning

confidence: 99%

Cysteine Proteome Reveals Response to Endogenous Oxidative Stress in Bacillus cereus

Hamitouche

Armengaud

Dedieu

et al. 2021

IJMS

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At the end of exponential growth, aerobic bacteria have to cope with the accumulation of endogenous reactive oxygen species (ROS). One of the main targets of these ROS is cysteine residues in proteins. This study uses liquid chromatography coupled to high-resolution tandem mass spectrometry to detect significant changes in protein abundance and thiol status for cysteine-containing proteins from Bacillus cereus during aerobic exponential growth. The proteomic profiles of cultures at early-, middle-, and late-exponential growth phases reveals that (i) enrichment in proteins dedicated to fighting ROS as growth progressed, (ii) a decrease in both overall proteome cysteine content and thiol proteome redox status, and (iii) changes to the reduced thiol status of some key proteins, such as the transition state transcriptional regulator AbrB. Taken together, our data indicate that growth under oxic conditions requires increased allocation of protein resources to attenuate the negative effects of ROS. Our data also provide a strong basis to understand the response mechanisms used by B. cereus to deal with endogenous oxidative stress.

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Redox Homeostasis

Cited by 4 publications

References 162 publications

Wolbachia and the insect immune system: what reactive oxygen species can tell us about the mechanisms of Wolbachia–host interactions

Wolbachia and the insect immune system: what reactive oxygen species can tell us about the mechanisms of Wolbachia–host interactions

Changes in protein thiols in response to salt stress in embryogenic suspension cultures ofDactylis glomerataL.

Cysteine Proteome Reveals Response to Endogenous Oxidative Stress in Bacillus cereus

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