Chmelova 2024 Int J Parasitol: Difference between revisions
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{{Publication | {{Publication | ||
|title=Chmelová Ľ, Kraeva N, Saura A, Krayzel A, Vieira CS, Ferreira TN, Soares RP, Bučková B, Galan A, Horáková E, Vojtková B, Sádlová J, Malysheva MN, Butenko A, Prokopchuk G, Frolov AO, Lukeš J, Horváth A, Škodová-Sveráková I, Feder D, Yu Kostygov A, Yurchenko V (2024) Intricate balance of dually-localized catalase modulates infectivity of Leptomonas seymouri (Kinetoplastea: Trypanosomatidae). Int J Parasitol [Epub ahead of print]. https://doi.org/10.1016/j.ijpara.2024.04.007 | |title=Chmelová Ľ, Kraeva N, Saura A, Krayzel A, Vieira CS, Ferreira TN, Soares RP, Bučková B, Galan A, Horáková E, Vojtková B, Sádlová J, Malysheva MN, Butenko A, Prokopchuk G, Frolov AO, Lukeš J, Horváth A, Škodová-Sveráková I, Feder D, Yu Kostygov A, Yurchenko V (2024) Intricate balance of dually-localized catalase modulates infectivity of ''Leptomonas seymouri'' (Kinetoplastea: Trypanosomatidae). Int J Parasitol [Epub ahead of print]. https://doi.org/10.1016/j.ijpara.2024.04.007 | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/38663543 PMID: 38663543 Open Access] | |info=[https://pubmed.ncbi.nlm.nih.gov/38663543 PMID: 38663543 Open Access] | ||
|authors= | |authors=Chmelova Lubomira, Kraeva Natalya, Saura Andreu, Krayzel Adam, Stahl Vieira Cecilia, Ferreira Taina Neves, Soares Rodrigo Pedro, Buckova Barbora, Galan Arnau, Horakova Eva, Vojtkova Barbora, Sadlova Jovana, Malysheva Marina N, Butenko Anzhelika, Prokopchuk Galina, Frolov Alexander O, Lukes Julius, Horvath Anton, Skodova-Sverakova Ingrid, Feder Denise, Kostygov Alexei Yu, Yurchenko Vyacheslav | ||
|year=2024 | |year=2024 | ||
|journal=Int J Parasitol | |journal=Int J Parasitol | ||
|abstract=Nearly all aerobic organisms are equipped with catalases, powerful enzymes scavenging hydrogen peroxide and facilitating defense against harmful reactive oxygen species. In trypanosomatids, this enzyme was not present in the common ancestor, yet it had been independently acquired by different lineages of monoxenous trypanosomatids from different bacteria at least three times. This observation posited an obvious question: why was catalase so "sought after" if many trypanosomatid groups do just fine without it? In this work, we analyzed subcellular localization and function of catalase in Leptomonas seymouri. We demonstrated that this enzyme is present in the cytoplasm and a subset of glycosomes, and that its cytoplasmic retention is | |abstract=Nearly all aerobic organisms are equipped with catalases, powerful enzymes scavenging hydrogen peroxide and facilitating defense against harmful reactive oxygen species. In trypanosomatids, this enzyme was not present in the common ancestor, yet it had been independently acquired by different lineages of monoxenous trypanosomatids from different bacteria at least three times. This observation posited an obvious question: why was catalase so "sought after" if many trypanosomatid groups do just fine without it? In this work, we analyzed subcellular localization and function of catalase in ''Leptomonas seymouri''. We demonstrated that this enzyme is present in the cytoplasm and a subset of glycosomes, and that its cytoplasmic retention is H<sub>2</sub>O<sub>2</sub>-dependent. The ablation of catalase in this parasite is not detrimental ''in vivo'', while its overexpression resulted in a substantially higher parasite load in the experimental infection of ''Dysdercus peruvianus''. We propose that the capacity of studied flagellates to modulate the catalase activity in the midgut of its insect host facilitates their development and protects them from oxidative damage at elevated temperatures. | ||
|keywords=Catalase, Hydrogen peroxide, Trypanosomatids | |||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|area=Respiration | |area=Respiration | ||
|injuries=Oxidative stress;RONS | |||
|organism=Protists | |||
|preparations=Intact cells | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional=2024-05 | |additional=2024-05 | ||
}} | }} | ||
Latest revision as of 13:54, 15 May 2024
| Chmelová Ľ, Kraeva N, Saura A, Krayzel A, Vieira CS, Ferreira TN, Soares RP, Bučková B, Galan A, Horáková E, Vojtková B, Sádlová J, Malysheva MN, Butenko A, Prokopchuk G, Frolov AO, Lukeš J, Horváth A, Škodová-Sveráková I, Feder D, Yu Kostygov A, Yurchenko V (2024) Intricate balance of dually-localized catalase modulates infectivity of Leptomonas seymouri (Kinetoplastea: Trypanosomatidae). Int J Parasitol [Epub ahead of print]. https://doi.org/10.1016/j.ijpara.2024.04.007 |
Chmelova Lubomira, Kraeva Natalya, Saura Andreu, Krayzel Adam, Stahl Vieira Cecilia, Ferreira Taina Neves, Soares Rodrigo Pedro, Buckova Barbora, Galan Arnau, Horakova Eva, Vojtkova Barbora, Sadlova Jovana, Malysheva Marina N, Butenko Anzhelika, Prokopchuk Galina, Frolov Alexander O, Lukes Julius, Horvath Anton, Skodova-Sverakova Ingrid, Feder Denise, Kostygov Alexei Yu, Yurchenko Vyacheslav (2024) Int J Parasitol
Abstract: Nearly all aerobic organisms are equipped with catalases, powerful enzymes scavenging hydrogen peroxide and facilitating defense against harmful reactive oxygen species. In trypanosomatids, this enzyme was not present in the common ancestor, yet it had been independently acquired by different lineages of monoxenous trypanosomatids from different bacteria at least three times. This observation posited an obvious question: why was catalase so "sought after" if many trypanosomatid groups do just fine without it? In this work, we analyzed subcellular localization and function of catalase in Leptomonas seymouri. We demonstrated that this enzyme is present in the cytoplasm and a subset of glycosomes, and that its cytoplasmic retention is H2O2-dependent. The ablation of catalase in this parasite is not detrimental in vivo, while its overexpression resulted in a substantially higher parasite load in the experimental infection of Dysdercus peruvianus. We propose that the capacity of studied flagellates to modulate the catalase activity in the midgut of its insect host facilitates their development and protects them from oxidative damage at elevated temperatures. • Keywords: Catalase, Hydrogen peroxide, Trypanosomatids • Bioblast editor: Plangger M
Labels: MiParea: Respiration
Stress:Oxidative stress;RONS Organism: Protists
Preparation: Intact cells
HRR: Oxygraph-2k
2024-05
