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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61988987%3A17310%2F20%3AA21025D1" target="_blank" >RIV/61988987:17310/20:A21025D1 - isvavai.cz</a>

Alternative codes found

RIV/60077344:_____/20:00538237 RIV/60076658:12310/20:43901856

Result on the web

<a href="https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/febs.15083" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/febs.15083</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.15083" target="_blank" >10.1111/febs.15083</a>

Result language

angličtina

Original language name

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

Original language description

Catalase is a widespread heme-containing enzyme, which converts hydrogen peroxide (H2O2) to water and molecular oxygen, thereby protecting cells from the toxic effects of H2O2. 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 H2O2 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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10600 - Biological sciences

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

FEBS JOURNAL

ISSN

1742-464X

e-ISSN

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Volume of the periodical

287

Issue of the periodical within the volume

5

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

964-977

UT code for WoS article

000493058000001

EID of the result in the Scopus database

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