Intricate balance of dually-localized catalase modulates infectivity of Leptomonas seymouri (Kinetoplastea: Trypanosomatidae)

. 2024 Jul ; 54 (8-9) : 391-400. [epub] 20240423

Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid38663543
Odkazy

PubMed 38663543
DOI 10.1016/j.ijpara.2024.04.007
PII: S0020-7519(24)00077-8
Knihovny.cz E-zdroje

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.

Biotechnology Applied to Pathogens Instituto René Rachou Fundação Oswaldo Cruz Belo Horizonte Brazil

Department of Biochemistry Faculty of Natural Sciences Comenius University Bratislava Slovakia

Department of Parasitology Faculty of Science Charles University Prague Czechia

Institute of Parasitology Biology Centre Czech Academy of Sciences České Budějovice Czechia

Institute of Parasitology Biology Centre Czech Academy of Sciences České Budějovice Czechia; Faculty of Science University of South Bohemia České Budějovice Czechia

Life Science Research Centre Faculty of Science University of Ostrava Ostrava Czechia

Life Science Research Centre Faculty of Science University of Ostrava Ostrava Czechia; Department of Biochemistry Faculty of Natural Sciences Comenius University Bratislava Slovakia; Institute of Parasitology Biology Centre Czech Academy of Sciences České Budějovice Czechia

Life Science Research Centre Faculty of Science University of Ostrava Ostrava Czechia; Institute of Parasitology Biology Centre Czech Academy of Sciences České Budějovice Czechia; Faculty of Science University of South Bohemia České Budějovice Czechia

Life Science Research Centre Faculty of Science University of Ostrava Ostrava Czechia; Zoological Institute Russian Academy of Sciences St Petersburg Russia

Universidade Federal Fluminense Instituto de Biologia Programa de Pós Graduação em Ciências e Biotecnologia Niterói Brazil

Universidade Federal Fluminense Instituto de Biologia Programa de Pós Graduação em Ciências e Biotecnologia Niterói Brazil; Universidade Federal Fluminense Instituto de Biologia Laboratório de Biologia de Insetos Niterói Brazil; Instituto Nacional de Entomologia Molecular Rio de Janeiro Brazil

Zoological Institute Russian Academy of Sciences St Petersburg Russia

Citace poskytuje Crossref.org

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