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

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dc.contributor.author Horakova, E. en_US
dc.contributor.author Faktorova, D. en_US
dc.contributor.author Kraeva, N. en_US
dc.contributor.author Kaur, B. en_US
dc.contributor.author Van Den Abbeele, J. en_US
dc.contributor.author Yurchenko, V. en_US
dc.contributor.author Lukes, J. en_US
dc.date.accessioned 2020-08-25T09:37:52Z
dc.date.available 2020-08-25T09:37:52Z
dc.date.issued 2020 en_US
dc.identifier.issn 1742-464X en_US
dc.identifier.doi http://dx.doi.org/10.1111/febs.15083 en_US
dc.identifier.other http://lib.itg.be/pdf/itg/2019/2019febs0001.pdf en_US
dc.identifier.other 58 en_US
dc.identifier.other ITG-B5A; DBM; U-VPROT; JIF; DOI; PDF; Abstract; ITMPUB; DSPACE68 en_US
dc.identifier.other NOBIT en_US
dc.identifier.uri http://hdl.handle.net/10390/10851
dc.description.abstract Catalase is a widespread heme-containing enzyme, which converts hydrogen peroxide (H2 O2 ) to water and molecular oxygen, thereby protecting cells from the toxic effects of H2 O2 . 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 H2 O2 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. en_US
dc.language English en_US
dc.relation.uri http://www.ncbi.nlm.nih.gov/pubmed/31593329 en_US
dc.subject Trypanosoma brucei en_US
dc.subject Protozoology en_US
dc.subject Catalase en_US
dc.title Catalase compromises the development of the insect and mammalian stages of Trypanosoma brucei en_US
dc.type Article en_US
dc.citation.issue 5 en_US
dc.citation.jtitle FEBS Journal en_US
dc.citation.volume 287 en_US
dc.citation.pages 964-977 en_US
dc.citation.abbreviation FEBS J en_US


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