Role of the<i>Listeria monocytogenes</i>2-Cys peroxiredoxin homologue in protection against oxidative and nitrosative stress and in virulence

Dons, Lone; Mosa, Ahmed; Rottenberg, Martı́n E.; Rosenkrantz, Jesper T.; Kristensson, Krister; Olsen, John Elmerdahl

doi:10.1111/2049-632x.12081

Cited by 26 publications

(23 citation statements)

References 31 publications

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“…Our comparison of H 2 O 2 and CHP confirms previous reports showing that H 2 O 2 is a more effective listericidal agent [27,30]. The presence of molecular oxygen, growth phase and serovar may all affect the response to oxidative conditions [26,31].…”

Section: Discussionsupporting

confidence: 88%

“…In food processing environments (FPE), various stressful conditions can influence L. monocytogenes growth and survival, especially refrigeration temperatures, osmotic, acid and oxidative stresses [24,25]. L. monocytogenes is also exposed to stressful conditions in hosts and some are common to FPE stresses: gastric acids provide acid and both invasion of phagolysosomes or macrophages and antibiotic treatments can cause oxidative stress [26,27]. L. monocytogenes is able to increase its tolerance to stressful conditions over time following repeated exposure to sub-lethal doses.…”

Section: Discussionmentioning

confidence: 99%

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The Response to Oxidative Stress in Listeria monocytogenes Is Temperature Dependent

et al. 2020

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The stress response of 11 strains of Listeria monocytogenes to oxidative stress was studied. The strains included ST1, ST5, ST7, ST6, ST9, ST87, ST199 and ST321 and were isolated from diverse food processing environments (a meat factory, a dairy plant and a seafood company) and sample types (floor, wall, drain, boxes, food products and water machine). Isolates were exposed to two oxidizing agents: 13.8 mM cumene hydroperoxide (CHP) and 100 mM hydrogen peroxide (H2O2) at 10 °C and 37 °C. Temperature affected the oxidative stress response as cells treated at 10 °C survived better than those treated at 37 °C. H2O2 at 37 °C was the condition tested resulting in poorest L. monocytogenes survival. Strains belonging to STs of Lineage I (ST5, ST6, ST87, ST1) were more resistant to oxidative stress than those of Lineage II (ST7, ST9, ST199 and ST321), with the exception of ST7 that showed tolerance to H2O2 at 10 °C. Isolates of each ST5 and ST9 from different food industry origins showed differences in oxidative stress response. The gene expression of two relevant virulence (hly) and stress (clpC) genes was studied in representative isolates in the stressful conditions. hly and clpC were upregulated during oxidative stress at low temperature. Our results indicate that conditions prevalent in food industries may allow L. monocytogenes to develop survival strategies: these include activating molecular mechanisms based on cross protection that can promote virulence, possibly increasing the risk of virulent strains persisting in food processing plants.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

The Response to Oxidative Stress in Listeria monocytogenes Is Temperature Dependent

et al. 2020

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“…Consistent with this, there have been only a few studies on these nonclassical Ahp proteins (22,(27)(28)(29)(41)(42)(43). Although they are obviously homologs of E. coli and B. subtilis AhpC, the nonclassical Ahp proteins are a distinct class of proteins with significant sequence differences and, therefore, possibly functional differences from the classical Ahp proteins.…”

Section: Resultsmentioning

confidence: 99%

Insights into the Function of a Second, Nonclassical Ahp Peroxidase, AhpA, in Oxidative Stress Resistance in Bacillus subtilis

et al. 2016

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Organisms growing aerobically generate reactive oxygen-containing molecules, such as hydrogen peroxide (H 2 O 2 ). These reactive oxygen molecules damage enzymes and DNA and may even cause cell death. In response, Bacillus subtilis produces at least nine potential peroxide-scavenging enzymes, two of which appear to be the primary enzymes responsible for detoxifying peroxides during vegetative growth: a catalase (encoded by katA) and an alkylhydroperoxide reductase (Ahp, encoded by ahpC). AhpC uses two redox-active cysteine residues to reduce peroxides to nontoxic molecules. A specialized thioredoxin-like protein, AhpF, is then required to restore oxidized AhpC back to its reduced state. Curiously, B. subtilis has two genes encoding Ahp: ahpC and ahpA. Although AhpC is well characterized, very little is known about AhpA. In fact, numerous bacterial species have multiple ahp genes; however, these additional Ahp proteins are generally uncharacterized. We seek to understand the role of AhpA in the bacterium's defense against toxic peroxide molecules in relation to the roles previously assigned to AhpC and catalase. Our results demonstrate that AhpA has catalytic activity similar to that of the primary enzyme, AhpC. Furthermore, our results suggest that a unique thioredoxin redox protein, AhpT, may reduce AhpA upon its oxidation by peroxides. However, unlike AhpC, which is expressed well during vegetative growth, our results suggest that AhpA is expressed primarily during postexponential growth. IMPORTANCEB. subtilis appears to produce nine enzymes designed to protect cells against peroxides; two belong to the Ahp class of peroxidases. These studies provide an initial characterization of one of these Ahp homologs and demonstrate that the two Ahp enzymes are not simply replicates of each other, suggesting that they instead are expressed at different times during growth of the cells. These results highlight the need to further study the Ahp homologs to better understand how they differ from one another and to identify their function, if any, in protection against oxidative stress. Through these studies, we may better understand why bacteria have multiple enzymes designed to scavenge peroxides and thus have a more accurate understanding of oxidative stress resistance.

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“…Dons et al showed that 2-Cys peroxiredoxin (Prx) homologue (Lmo1604) showed protection against oxidative and nitrosative stress in vitro and in vivo. Lmo1604 also plays a role during infection to the host and protection against stress [20]. During host-pathogen interactions, oxidative stress genes were elevated indicating that these genes actively participate in this mechanism and are important for virulence [21].…”

Section: 1mentioning

confidence: 99%

LmTDRM Database: A Comprehensive Database on Thiol Metabolic Gene/Gene Products in Listeria monocytogenes EGDe

Srinivas

Gopal

2014

Journal of Integrative Bioinformatics

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SummaryThere are a number of databases on the Listeria species and about their genome. However, these databases do not specifically address a set of network that is important in defence mechanism of the bacteria. Listeria monocytogenes EGDe is a well-established intracellular model organism to study host pathogenicity because of its versatility in the host environment. Here, we have focused on thiol disulphide redox metabolic network proteins, specifically in L. monocytogenes EGDe. The thiol redox metabolism is involved in oxidative stress mechanism and is found in all living cells. It functions to maintain the thiol disulphide balance required for protein folding by providing reducing power. Nevertheless, they are involved in the reversible oxidation of thiol groups in biomolecules by creating disulphide bonds; therefore, the term thiol disulphide redox metabolism (TDRM). TDRM network genes play an important role in oxidative stress mechanism and during host-pathogen interaction. Therefore, it is essential to have detailed information on these proteins with regard to other bacteria and its genome analysis to understand the presence of tRNA, transposons, and insertion elements for horizontal gene transfer. LmTDRM database is a new comprehensive web-based database on thiol proteins and their functions. It includes: Description, Search, TDRM analysis, and genome viewer. The quality of these data has been evaluated before they were aggregated to produce a final representation. The web interface allows for various queries to understand the protein function and their annotation with respect to their relationship with other bacteria. LmTDRM is a major step towards the development of databases on thiol disulphide redox proteins; it would definitely help researchers to understand the mechanism of these proteins and their interaction. Database URL: www.lmtdrm.com IntroductionBacteria during their interaction with the host or during other conditions generate reactive oxygen species (ROS) and reactive nitrogen species (RNS). These serve as secondary messengers and/or can also damage proteins, nucleic acids, and lipids [1,2]. To avoid cellular damage by these processes, most bacteria have developed a series of antioxidants that can convert ROS and RNS to unreactive derivatives. They are (i) a number of enzymes such as catalase, glutathione peroxidase, glutathione-S-transferase, thiol-specific peroxidase, methionine sulphoxide reductase, thioredoxin peroxidase, glutathione reductase, and glutaredoxins; (ii) various metal binding proteins such as ceruloplasmin, ferritin, transferrin, various metabolites, and cofactors (NADs, lipoic acid, uric acid, bilirubin, etc); (iii) a number of dietary components (vitamin A, C, E, quercetin, etc.) and (iv) metal ions (Mg 2+ , Mn 2+ , Zn 2+ ) with enzymes or metalloenzymes like superoxide dismutase. Among them, thiol proteins are the major ones [3,4].

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Role of theListeria monocytogenes2-Cys peroxiredoxin homologue in protection against oxidative and nitrosative stress and in virulence

Cited by 26 publications

References 31 publications

The Response to Oxidative Stress in Listeria monocytogenes Is Temperature Dependent

The Response to Oxidative Stress in Listeria monocytogenes Is Temperature Dependent

Insights into the Function of a Second, Nonclassical Ahp Peroxidase, AhpA, in Oxidative Stress Resistance in Bacillus subtilis

LmTDRM Database: A Comprehensive Database on Thiol Metabolic Gene/Gene Products in Listeria monocytogenes EGDe

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