Catalase and Ascorbate Peroxidase in Euglenozoan Protists

Škodová-Sveráková, Ingrid; Záhonová, Kristína; Bučková, Barbora; Füssy, Zoltán; Yurchenko, Vyacheslav; Lukeš, Julius

doi:10.3390/pathogens9040317

Cited by 14 publications

(11 citation statements)

References 83 publications

(104 reference statements)

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“…This protein is responsible for the decomposition of H 2 O 2 and, thus helps to protect from dangerous reactive oxygen species (ROS). We have recently performed a broad genomic screening for the presence of catalase in Euglenozoa [ 25 , 26 ]. The catalase-encoding gene was absent in the common ancestor of trypanosomatids and acquired independently, at least twice, by monoxenous Leishmaniinae and members of the Blastocrithidia /” jaculum ” clade [ 27 ].…”

Section: Introductionmentioning

confidence: 99%

Catalase impairs Leishmania mexicana development and virulence

et al. 2021

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Catalase is one of the most abundant enzymes on Earth. It decomposes hydrogen peroxide, thus protecting cells from dangerous reactive oxygen species. The catalase-encoding gene is conspicuously absent from the genome of most representatives of the family Trypanosomatidae. Here, we expressed this protein from the Leishmania mexicana Β-TUBULIN locus using a novel bicistronic expression system, which relies on the 2A peptide of Teschovirus A . We demonstrated that catalase-expressing parasites are severely compromised in their ability to develop in insects, to be transmitted and to infect mice, and to cause clinical manifestation in their mammalian host. Taken together, our data support the hypothesis that the presence of catalase is not compatible with the dixenous life cycle of Leishmania , resulting in loss of this gene from the genome during the evolution of these parasites.

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Section: Introductionmentioning

confidence: 99%

Catalase impairs Leishmania mexicana development and virulence

et al. 2021

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“…is now also extended for Endotrypanum/Porcisia spp. As in all Leishmania [ 109 ], the gene encoding catalase was not retained in the Endotrypanum/Porcisia genomes, further supporting the hypothesis of its incompatibility with the dixenous life cycle [ 110 ].…”

Section: Resultsmentioning

confidence: 80%

Genome Analysis of Endotrypanum and Porcisia spp., Closest Phylogenetic Relatives of Leishmania, Highlights the Role of Amastins in Shaping Pathogenicity

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Gerasimov

Shaw

et al. 2021

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While numerous genomes of Leishmania spp. have been sequenced and analyzed, an understanding of the evolutionary history of these organisms remains limited due to the unavailability of the sequence data for their closest known relatives, Endotrypanum and Porcisia spp., infecting sloths and porcupines. We have sequenced and analyzed genomes of three members of this clade in order to fill this gap. Their comparative analyses revealed only minute differences from Leishmaniamajor genome in terms of metabolic capacities. We also documented that the number of genes under positive selection on the Endotrypanum/Porcisia branch is rather small, with the flagellum-related group of genes being over-represented. Most significantly, the analysis of gene family evolution revealed a substantially reduced repertoire of surface proteins, such as amastins and biopterin transporters BT1 in the Endotrypanum/Porcisia species when compared to amastigote-dwelling Leishmania. This reduction was especially pronounced for δ-amastins, a subfamily of cell surface proteins crucial in the propagation of Leishmania amastigotes inside vertebrate macrophages and, apparently, dispensable for Endotrypanum/Porcisia, which do not infect such cells.

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“…Catalase is present, yet it differs from its counterparts documented in Leishmaniinae [ 41 , 42 ] or Blastocrithidia spp. [ 43 ].…”

Section: Resultsmentioning

confidence: 99%

The Remarkable Metabolism of Vickermania ingenoplastis: Genomic Predictions

et al. 2021

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A recently redescribed two-flagellar trypanosomatid Vickermania ingenoplastis is insensitive to the classical inhibitors of respiration and thrives under anaerobic conditions. Using genomic and transcriptomic data, we analyzed its genes of the core metabolism and documented that subunits of the mitochondrial respiratory complexes III and IV are ablated, while those of complexes I, II, and V are all present, along with an alternative oxidase. This explains the previously reported conversion of glucose to acetate and succinate by aerobic fermentation. Glycolytic pyruvate is metabolized to acetate and ethanol by pyruvate dismutation, whereby a unique type of alcohol dehydrogenase (shared only with Phytomonas spp.) processes an excess of reducing equivalents formed under anaerobic conditions, leading to the formation of ethanol. Succinate (formed to maintain the glycosomal redox balance) is converted to propionate by a cyclic process involving three enzymes of the mitochondrial methyl-malonyl-CoA pathway, via a cyclic process, which results in the formation of additional ATP. The unusual structure of the V. ingenoplastis genome and its similarity with that of Phytomonas spp. imply their relatedness or convergent evolution. Nevertheless, a critical difference between these two trypanosomatids is that the former has significantly increased its genome size by gene duplications, while the latter streamlined its genome.

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Catalase and Ascorbate Peroxidase in Euglenozoan Protists

Cited by 14 publications

References 83 publications

Catalase impairs Leishmania mexicana development and virulence

Catalase impairs Leishmania mexicana development and virulence

Genome Analysis of Endotrypanum and Porcisia spp., Closest Phylogenetic Relatives of Leishmania, Highlights the Role of Amastins in Shaping Pathogenicity

The Remarkable Metabolism of Vickermania ingenoplastis: Genomic Predictions

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