Catalase in Leishmaniinae: With me or against me?

Kraeva, Natalya; Horáková, Eva; Kostygov, Alexei Y.; Kořený, Luděk; Butenko, Anzhelika; Yurchenko, Vyacheslav; Lukeš, Julius

doi:10.1016/j.meegid.2016.06.054

Cited by 40 publications

(51 citation statements)

References 55 publications

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“…It was previously shown that kinetoplastid flagellates acquired their CAT enzyme at least two times independently from bacteria. As revealed by the phylogenetic analysis, CAT of Leishmaniinae and the Blastocrithidia/"jaculum" clade derive from different bacterial groups [29,30], and this was confirmed here using a larger dataset (Figure 2A; File S2). While euglenids, studied so far, do not encode CAT [11,31], we wondered whether the same pattern applies to diplonemids, which constitute a sister clade to kinetoplastids [32,33].…”

Section: Euglenozoans Encode Unique Hpxs and Cat Of Different Originssupporting

confidence: 79%

Catalase and Ascorbate Peroxidase in Euglenozoan Protists

et al. 2020

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In this work, we studied the biochemical properties and evolutionary histories of catalase (CAT) and ascorbate peroxidase (APX), two central enzymes of reactive oxygen species detoxification, across the highly diverse clade Eugenozoa. This clade encompasses free-living phototrophic and heterotrophic flagellates, as well as obligate parasites of insects, vertebrates, and plants. We present evidence of several independent acquisitions of CAT by horizontal gene transfers and evolutionary novelties associated with the APX presence. We posit that Euglenozoa recruit these detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids.

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Section: Euglenozoans Encode Unique Hpxs and Cat Of Different Originssupporting

confidence: 79%

Catalase and Ascorbate Peroxidase in Euglenozoan Protists

et al. 2020

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“…Excited by the idea that the metabolic repurposing of the mitochondria during the developmental progression leads to the production of signaling molecules, we sought to investigate whether ROS elimination would halt the in vitro-induced differentiation. We took advantage of the fact that T. brucei genome lacks catalase, a natural and very potent scavenger of ROS molecules [46]. We introduced the catalase gene from a related organism, Crithidia fasciculata, into the T. brucei genome under the control of a tetracyclineinducible system.…”

Section: Repurposing Of the Mitochondrion To A Ros-producing Signalinmentioning

confidence: 99%

Cell-based and multi-omics profiling reveals dynamic metabolic repurposing of mitochondria to drive developmental progression of Trypanosoma brucei

et al. 2020

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Mitochondrial metabolic remodeling is a hallmark of the Trypanosoma brucei digenetic life cycle because the insect stage utilizes a cost-effective oxidative phosphorylation (OxPhos) to generate ATP, while bloodstream cells switch to aerobic glycolysis. Due to difficulties in acquiring enough parasites from the tsetse fly vector, the dynamics of the parasite's metabolic rewiring in the vector have remained obscure. Here, we took advantage of in vitroinduced differentiation to follow changes at the RNA, protein, and metabolite levels. This multi-omics and cell-based profiling showed an immediate redirection of electron flow from the cytochrome-mediated pathway to an alternative oxidase (AOX), an increase in proline consumption, elevated activity of complex II, and certain tricarboxylic acid (TCA) cycle enzymes, which led to mitochondrial membrane hyperpolarization and increased reactive oxygen species (ROS) levels. Interestingly, these ROS molecules appear to act as signaling molecules driving developmental progression because ectopic expression of catalase, a ROS scavenger, halted the in vitro-induced differentiation. Our results provide insights into the mechanisms of the parasite's mitochondrial rewiring and reinforce the emerging concept that mitochondria act as signaling organelles through release of ROS to drive cellular differentiation.

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“…The catalase is present in almost all extant organisms exposed to oxygen . Still, some free‐living eukaryotes, such as secondary algae (Cryptophyta, Haptophyta, and Chlorarachniophyta), hematozoan Apicomplexa, and the bodonid and euglenid flagellates, lack catalase in their genomes . Recently, it was shown that the distribution of catalase in the kinetoplastid protists of the family Trypanosomatidae is particularly idiosyncratic .…”

Section: Introductionmentioning

confidence: 99%

Catalase compromises the development of the insect and mammalian stages of Trypanosoma brucei

et al. 2019

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Catalase is a widespread heme‐containing enzyme, which converts hydrogen peroxide (H2O2) to water and molecular oxygen, thereby protecting cells from the toxic effects of H2O2. Trypanosoma brucei is an aerobic protist, which conspicuously lacks this potent enzyme, present in virtually all organisms exposed to oxidative stress. To uncover the reasons for its absence in T. brucei, we overexpressed different catalases in procyclic and bloodstream stages of the parasite. The heterologous enzymes originated from the related insect‐confined trypanosomatid Crithidia fasciculata and the human. While the trypanosomatid enzyme (cCAT) operates at low temperatures, its human homolog (hCAT) is adapted to the warm‐blooded environment. Despite the presence of peroxisomal targeting signal in hCAT, both human and C. fasciculata catalases localized to the cytosol of T. brucei. Even though cCAT was efficiently expressed in both life cycle stages, the enzyme was active in the procyclic stage, increasing cell's resistance to the H2O2 stress, yet its activity was suppressed in the cultured bloodstream stage. Surprisingly, following the expression of hCAT, the ability to establish the T. brucei infection in the tsetse fly midgut was compromised. In the mouse model, hCAT attenuated parasitemia and, consequently, increased the host's survival. Hence, we suggest that the activity of catalase in T. brucei is beneficial in vitro, yet it becomes detrimental for parasite's proliferation in both invertebrate and vertebrate hosts, leading to an inability to carry this, otherwise omnipresent, enzyme.

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Catalase in Leishmaniinae: With me or against me?

Cited by 40 publications

References 55 publications

Catalase and Ascorbate Peroxidase in Euglenozoan Protists

Catalase and Ascorbate Peroxidase in Euglenozoan Protists

Cell-based and multi-omics profiling reveals dynamic metabolic repurposing of mitochondria to drive developmental progression of Trypanosoma brucei

Catalase compromises the development of the insect and mammalian stages of Trypanosoma brucei

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