Intricate balance of dually-localized catalase in /Leptomonas seymouri/ (Kinetoplastea: Trypanosomatidae) modulates infectivity
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00604262" target="_blank" >RIV/60077344:_____/24:00604262 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1016/j.ijpara.2024.04.007" target="_blank" >https://doi.org/10.1016/j.ijpara.2024.04.007</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ijpara.2024.04.007" target="_blank" >10.1016/j.ijpara.2024.04.007</a>
Alternative languages
Result language
angličtina
Original language name
Intricate balance of dually-localized catalase in /Leptomonas seymouri/ (Kinetoplastea: Trypanosomatidae) modulates infectivity
Original language description
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. CO 2024 The Author(s). Published by Elsevier Ltd on behalf of Australian Society for Parasitology. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
<a href="/en/project/GA21-09283S" target="_blank" >GA21-09283S: Catalase: to be or not to be in two hosts</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal for Parasitology
ISSN
0020-7519
e-ISSN
1879-0135
Volume of the periodical
54
Issue of the periodical within the volume
8-9
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
10
Pages from-to
391-400
UT code for WoS article
001255604200001
EID of the result in the Scopus database
2-s2.0-85191821063