Ľubomíra Chmelová , Natalya Kraeva , Andreu Saura , Adam Krayzel , Cecilia Stahl Vieira , Tainá Neves Ferreira , Rodrigo Pedro Soares , Barbora Bučková , Arnau Galan , Eva Horáková , Barbora Vojtková , Jovana Sádlová , Marina N. Malysheva , Anzhelika Butenko , Galina Prokopchuk , Alexander O. Frolov , Julius Lukeš , Anton Horváth , Ingrid Škodová-Sveráková , Denise Feder , Vyacheslav Yurchenko
{"title":"双定位过氧化氢酶的复杂平衡调节了西摩里钩端螺旋体(Kinetoplastea: Trypanosomatidae)的感染性。","authors":"Ľubomíra Chmelová , Natalya Kraeva , Andreu Saura , Adam Krayzel , Cecilia Stahl Vieira , Tainá Neves Ferreira , Rodrigo Pedro Soares , Barbora Bučková , Arnau Galan , Eva Horáková , Barbora Vojtková , Jovana Sádlová , Marina N. Malysheva , Anzhelika Butenko , Galina Prokopchuk , Alexander O. Frolov , Julius Lukeš , Anton Horváth , Ingrid Škodová-Sveráková , Denise Feder , Vyacheslav Yurchenko","doi":"10.1016/j.ijpara.2024.04.007","DOIUrl":null,"url":null,"abstract":"<div><p>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 <em>Leptomonas seymouri</em>. 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 <em>Dysdercus peruvianus</em>. 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.</p></div>","PeriodicalId":13725,"journal":{"name":"International journal for parasitology","volume":null,"pages":null},"PeriodicalIF":3.7000,"publicationDate":"2024-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0020751924000778/pdfft?md5=441d21891e548dfcb69956b13122b010&pid=1-s2.0-S0020751924000778-main.pdf","citationCount":"0","resultStr":"{\"title\":\"Intricate balance of dually-localized catalase modulates infectivity of Leptomonas seymouri (Kinetoplastea: Trypanosomatidae)\",\"authors\":\"Ľubomíra Chmelová , Natalya Kraeva , Andreu Saura , Adam Krayzel , Cecilia Stahl Vieira , Tainá Neves Ferreira , Rodrigo Pedro Soares , Barbora Bučková , Arnau Galan , Eva Horáková , Barbora Vojtková , Jovana Sádlová , Marina N. Malysheva , Anzhelika Butenko , Galina Prokopchuk , Alexander O. Frolov , Julius Lukeš , Anton Horváth , Ingrid Škodová-Sveráková , Denise Feder , Vyacheslav Yurchenko\",\"doi\":\"10.1016/j.ijpara.2024.04.007\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>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 <em>Leptomonas seymouri</em>. 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 <em>Dysdercus peruvianus</em>. 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Intricate balance of dually-localized catalase modulates infectivity of Leptomonas seymouri (Kinetoplastea: Trypanosomatidae)
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.
期刊介绍:
International Journal for Parasitology offers authors the option to sponsor nonsubscriber access to their articles on Elsevier electronic publishing platforms. For more information please view our Sponsored Articles page. The International Journal for Parasitology publishes the results of original research in all aspects of basic and applied parasitology, including all the fields covered by its Specialist Editors, and ranging from parasites and host-parasite relationships of intrinsic biological interest to those of social and economic importance in human and veterinary medicine and agriculture.